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3)-1D-myo-inositol + raffinose = myo-inositol + stachyose
An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: methylated-DNA—[protein]-cysteine S-methyltransferase
Reaction: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine
Systematic name: DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase
Comments: This protein is involved in the repair of alkylated DNA. It acts only on the alkylated DNA (cf. EC 3.2.2.20 DNA-3-methyladenine glycosidase I and EC 3.2.2.21 DNA-3-methyladenine glycosidase II). This enzyme catalyses only one turnover and therefore is not strictly catalytic.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 77271-19-3
References:
1. Foote, R.S., Mitra, S. and Pal, B.C. Demethylation of O6-methylguanine in a synthetic DNA polymer by an inducible activity in Escherichia coli. Biochem. Biophys. Res. Commun. 97 (1980) 654-659. [PMID: 81133635]
2. Olsson, M. and Lindehl, T. Repair of alkylated DNA in Escherichia coli. Methyl group transfer from O6-methylguanine to a protein cysteine residue. J. Biol. Chem. 255 (1980) 10569-10571. [PMID: 81046903]
3. Pegg, A.E. and Byers, T.L. Repair of DNA containing O6-alkylguanine. FASEB J. 6 (1992) 2302-2310. [PMID: 92184065]
[EC 2.1.1.135 Transferred entry: now EC 1.16.1.8 [methionine synthase] reductase. (EC 2.1.1.135 created 1999, deleted 2003)]
Common name: isoflavone 7-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 7-hydroxyisoflavone = S-adenosyl-L-homocysteine + 7-methoxyisoflavone
For diagram of reaction click here.
Other name(s):
Systematic name: S-adenosyl-L-methionine:hydroxyisoflavone 7-O-methyltransferase
Comments: The enzyme from alfalfa can methylate daidzein, genistein and 6,7,4'-trihydroxyisoflavone but not flavones or flavanones.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 136111-54-1
References:
1. Edwards, R. and Dixon, R.A. Isoflavone O-methyltransferase activities in elicitor-treated cell suspension cultures of Medicago sativa. Phytochemistry 30 (1991) 2597-2606.
2. He, X.Z. and Dixon, R.A. Genetic manipulation of isoflavone 7-O-methyltransferase enhances biosynthesis of 4'-O-methylated isoflavonoid phytoalexins and disease resistance in alfalfa. Plant Cell 12 (2000) 1689-1702. [PMID: 11006341]
3. He, X.-Z. and Dixon, R.A. Affinity chromatography, substrate/product specificity, and amino acid sequence analysis of an isoflavone O-methyltransferase from alfalfa (Medicago sativa L.). Arch. Biochem. Biophys. 336 (1996) 121-129. [PMID: 8951042]
4. He, X.Z., Reddy, J.T. and Dixon, R.A. Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and characterization of an elicitor-inducible isoflavone 7-O-methyltransferase. Plant Mol. Biol. 36 (1998) 43-54. [PMID: 9484461]
5. Liu, C.-J. and Dixon, R.A. Elicitor-induced association of isoflavone O-methyltransferase with endomembranes prevents the formation and 7-O-methylation of daidzein during isoflavonoid phytoalexin biosynthesis. Plant Cell 13 (2001) 2643-2658. [PMID: 11752378]
6. Zubieta, C., He, X.-Z., Dixon, R.A. and Noel, J.P. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat. Struct. Biol. 8 (2001) 271-279. [PMID: 11224575]
7. Christensen, A.B., Gregersen, P.L., Olsen, C.E. and Collinge, D.B. A flavonoid 7-O-methyltransferase is expressed in barley leaves in response to pathogen attack. Plant Mol. Biol. 36 (1998) 219-227. [PMID: 9484434]
Common name: aminomethyltransferase
Reaction: protein-S-aminomethyldihydrolipoyllysine + tetrahydrofolate = protein-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
For diagram of reaction click here.
Glossary: dihydrolipoyl group
Other name(s): S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming); T-protein; glycine synthase; tetrahydrofolate aminomethyltransferase
Systematic name: protein-S-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
Comments: A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37257-08-2
References:
1. Okamura-Ikeda, J., Fujiwara, K. and Motokawa, Y. Purification and characterization of chicken liver T protein, a component of the glycine cleavage system. J. Biol. Chem. 257 (1982) 135-139.
2. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Common name: dihydrolipoyllysine-residue acetyltransferase
Reaction: acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine
For diagram of reaction click here.
Glossary: dihydrolipoyl group
Other name(s): acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; dihydrolipoate acetyltransferase; dihydrolipoic transacetylase; dihydrolipoyl acetyltransferase; lipoate acetyltransferase; lipoate transacetylase; lipoic acetyltransferase; lipoic acid acetyltransferase; lipoic transacetylase; lipoylacetyltransferase; thioltransacetylase A; transacetylase X
Systematic name: enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase
Comments: A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-29-5
References:
1. Brady, R.O. and Stadtman, E.R. Enzymatic thioltransacetylation. J. Biol. Chem. 211 (1954) 621-629.
2. Gunsalus, I.C. Group transfer and acyl-generating functions of lipoic acid derivatives. In: McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism of Enzyme Action Johns Hopkins Press, Baltimore, 1954, pp. 545-480.
3. Gunsalus, I.C., Barton, L.S. and Gruber, W. Biosynthesis and structure of lipoic acid derivatives. J. Am. Chem. Soc. 78 (1956) 1763-1766.
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Common name: dihydrolipoyllysine-residue succinyltransferase
Reaction: succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
For diagram of reaction click here (mechanism).
Glossary: dihydrolipoyl group
Other name(s): dihydrolipoamide S-succinyltransferase; dihydrolipoamide succinyltransferase; dihydrolipoic transsuccinylase; dihydrolipolyl transsuccinylase; dihydrolipoyl transsuccinylase; lipoate succinyltransferase (Escherichia coli); lipoic transsuccinylase; lipoyl transsuccinylase; succinyl-CoA:dihydrolipoamide S-succinyltransferase; succinyl-CoA:dihydrolipoate S-succinyltransferase
Systematic name: enzyme-dihydrolipoyllysine:succinyl-CoA S-succinyltransferase
Comments: A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalysed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-28-4
References:
1. Derosier, D.J., Oliver, R.M. and Reed, L.J. Crystallization and preliminary structural analysis of dihydrolipoyl transsuccinylase, the core of the 2-oxoglutarate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 68 (1971) 1135-1137. [PMID: 4942179]
2. Reed, L.J. and Cox, D.J. Multienzyme complexes. In: Boyer, P.D. (Ed.), The Enzymes 3rd ed., vol. 1, Academic Press, New York, 1970, pp. 213-240.
3. Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655-668. [PMID: 9677295]
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Common name: indoleacetylglucose—inositol O-acyltransferase
Reaction: indole-3-acetyl β-1-D-glucoside + myo-inositol = D-glucose + indole-3-acetyl-myo-inositol
Systematic name: indole-3-acetyl-β-1-D-glucoside:myo-inositol indoleacetyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 74082-57-8
References:
1. Michalczuk, L. and Bandurski, R.S. Enzymic synthesis of 1-O-indol-3-ylacetyl-β-D-glucose and indol-3-ylacetyl-myo-inositol. Biochem. J. 207 (1982) 273-281. [PMID: 6218801]
2. Michalczuk, L. and Bandurski, R.S. UDP-glucose: indoleacetic acid glucosyl transferase and indoleacetyl-glucose: myo-inositol indoleacetyl transferase. Biochem. Biophys. Res. Commun. 93 (1980) 588-592. [PMID: 6446303]
Common name: fatty-acyl-CoA synthase
Reaction: acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+
Other name(s): yeast fatty acid synthase
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl- reducing)
Comments: The yeast enzyme is a multi-functional protein catalysing the reactions of EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase, EC 2.3.1.41 3-oxoacyl-[acyl-carrier-protein] synthase, EC 1.1.1.100 3-oxoacyl-[acyl-carrier-protein] reductase, EC 1.1.1.279, (R)-3-hydroxyacid ester dehydrogenase, EC 4.2.1.61 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase and EC 1.3.1.9 enoyl-[acyl-carrier-protein] reductase (NADH).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9045-77-6
References:
1. Schweitzer, E., Kniep, B., Castorph, H. and Holzner, U. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Eur. J. Biochem. 39 (1973) 353-362. [PMID: 74090015]
2. Wakil, S.J., Stoops, J.K. and Joshi, V.C. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52 (1983) 537-579. [PMID: 83307244]
Common name: dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Reaction: 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
For diagram of reaction click here.
Glossary: dihydrolipoyl group
Other name(s): dihydrolipoyl transacylase
Systematic name: enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA S-(2-methylpropanoyl)transferase
Comments: A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalysed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A. In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Massey, L.K., Sokatch, J.R. and Conrad, R.S. Branched-chain amino acid catabolism in bacteria. Bacteriol. Rev. 40 (1976) 42-54. [PMID: 773366]
2. Chuang, D.T., Hu, C.C., Ku, L.S., Niu, W.L., Myers, D.E. and Cox R.P. Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase. J. Biol. Chem. 259 (1984) 9277-9284. [PMID: 6746648]
3. Wynn, R.M., Davie, J.R., Zhi, W., Cox, R.P. and Chuang, D.T. In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES. Biochemistry 33 (1994) 8962-8968. [PMID: 7913832]
4. Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004. [PMID: 10966480]
Common name: CO-methylating acetyl-CoA synthase
Reaction: acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA
Systematic name: acetyl-CoA:corrinoid protein O-acetyltransferase
Comments: Contains nickel, copper and iron-sulfur clusters. Also catalyses exchange reactions of carbon between C-1 of acetyl-CoA and CO, and between C-2 of acetyl-CoA and methyl corrinoid protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin), in the synthesis of acetyl-CoA from CO2 and H2. To follow its stoichiometry, the reaction can be written as:
CH3-CO-S-CoA + protein Co+ + H+ = CO + protein Co2+-CH3 + HS-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Ragsdale, S.W. and Wood, H.G. Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis. J. Biol. Chem. 260 (1985) 3970-3977. [PMID: 2984190]
2. Doukov, T.I., Iverson, T., Seravalli, J., Ragsdale, S.W. and Drennan, C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298 (2002) 567-572. [PMID: 12386327]
Common name: phosphatidylinositol α-mannosyltransferase
Reaction: Transfers one or more α-D-mannose residues from GDP-mannose to positions 2,6 and others in 1-phosphatidyl-myo-inositol
Other name(s): GDP mannose-phosphatidyl-myo-inositol α-mannosyltransferase; GDPmannose:1-phosphatidyl-myo-inositol α-D-mannosyltransferase; guanosine diphosphomannose-phosphatidyl-inositol α-mannosyltransferase; phosphatidyl-myo-inositol α-mannosyltransferase
Systematic name: GDP-mannose:1-phosphatidyl-1D-myo-inositol α-D-mannosyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37277-65-9
References:
1. Brennan, P. and Ballou, G.E. Phosphatidylmyoinositol monomannoside in Propionibacterium shermanii. Biochem. Biophys. Res. Commun. 30 (1968) 69-75.
Common name: galactinol—raffinose galactosyltransferase
Reaction: α-D-galactosyl-(13)-1D-myo-inositol + raffinose = myo-inositol + stachyose
For diagram of reaction click here.
Other name(s): galactinol-raffinose galactosyltransferase; stachyose synthetase
Systematic name: α-D-galactosyl-(13)-myo-inositol:raffinose galactosyltransferase
Comments: This enzyme also catalyses galactosyl transfer from stachyose to raffinose (shown by labelling) [4]. For synthesis of the substrate, see EC 2.4.1.123, inositol 1-α-galactosyltransferase. See also EC 2.4.1.82, galactinol—sucrose galactosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37277-70-6
References:
1. Tanner, W. Die Biosynthese der Stachyose. Ber. Dtsch. Bot. Ges. 80 (1967) 111 only.
2. Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of stachyose. Eur. J. Biochem. 4 (1968) 233-239. [PMID: 5655499]
3. Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103-110. [PMID: 4774118]
4. Kandler, O. and Hopf, H. Occurrence, metabolism and function of oligosaccharides. In: Preiss, J. (Ed.), The Biochemistry of Plant vol. 3, Academic Press, New York, 1980, pp. 221-270.
Common name: galactinol—sucrose galactosyltransferase
Reaction: α-D-galactosyl-(13)-1D-myo-inositol + sucrose = myo-inositol + raffinose
For diagram of reaction click here.
Other name(s): 1-α-D-galactosyl-myo-inositol:sucrose 6-α-D-galactosyltransferase
Systematic name: α-D-galactosyl-(13)-myo-inositol:sucrose 6-α-D-galactosyltransferase
Comments: 4-Nitrophenyl α-D-galactopyranoside can also act as donor. The enzyme also catalyses an exchange reaction between raffinose and sucrose (cf. EC 2.4.1.123, inositol 3-α-galactosyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 62213-45-0
References:
1. Lehle, L. and Tanner, W. The function of myo-inositol in the biosynthesis of raffinose. Purification and characterization of galactinol:sucrose 6-galactosyltransferase from Vicia faba seeds. Eur. J. Biochem. 38 (1973) 103-110. [PMID: 4774118]
2. Lehle, L., Tanner, W. and Kandler, O. Myo-inositol, a cofactor in the biosynthesis of raffinose. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 1494-1498. [PMID: 5491608]
Common name: inositol 3-α-galactosyltransferase
Reaction: UDP-galactose + myo-inositol = UDP + O-α-D-galactosyl-(13)-1D-myo-inositol
For diagram of reaction click here.
Other name(s): UDP-galactose:myo-inositol 3-α-D-galactosyltransferase
Systematic name: UDP-D-galactose:inositol galactosyltransferase; UDP-galactose:myo-inositol 1-α-D-galactosyltransferase; UDPgalactose:myo-inositol 1-α-D-galactosyltransferase; galactinol synthase; inositol 1-α-galactosyltransferase; uridine diphosphogalactose-inositol galactosyltransferase
Comments: An enzyme from plants involved in the formation of raffinose and stachyose [cf. EC 2.4.1.67 (galactinol—raffinose galactosyltransferase) and EC 2.4.1.82 (galactinol—sucrose galactosyltransferase)].
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 79955-89-8
References:
1. Pharr, D.M., Sox, H.N., Locy, R.D. and Huber, S.C. Partial characterization of the galactinol forming enzyme from leaves of Cucumis sativus L. Plant Sci. Lett. 23 (1981) 25-33.
Common name: kojibiose phosphorylase
Reaction: 2-α-D-glucosyl-D-glucose + phosphate = D-glucose + β-D-glucose 1-phosphate
Systematic name: 2-α-D-glucosyl-D-glucose:phosphate β-D-glucosyltransferase
Comments: The enzyme from Thermoanaerobacter brockii can act with α-1,2-oligoglucans, such as selaginose, as substrate, but more slowly. The enzyme is inactive when dissaccharides with linkages other than α-1,2 linkages, such as sophorose, trehalose, neotrehalose, nigerose, laminaribiose, maltose, cellobiose, isomaltose, gentiobiose, sucrose and lactose, are used as substrates.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Chaen, H., Yamamoto, T., Nishimoto, T., Nakada, T., Fukuda, S., Sugimoto, T., Kurimoto, M. and Tsujisaka, Y. Purification and characterization of a novel phosphorylase, kojibiose phosphorylase, from Thermoanaerobium brockii. J. Appl. Glycosci. 46 (1999) 423-429.
2. Chaen, H., Nishimoto, T., Nakada, T., Fukuda, S., Kurimoto, M. and Tsujisaka, Y. Enzymatic synthesis of kojioligosaccharides using kojibiose phosphorylase. J. Biosci. Bioeng. 92 (2001) 177-182.
Common name: α,α-trehalose phosphorylase (configuration-retaining)
Reaction: α,α-trehalose + phosphate = α-D-glucose + α-D-glucose 1-phosphate
Other name(s): trehalose phosphorylase[ambiguous]
Systematic name: α,α-trehalose:phosphate α-D-glucosyltransferase
Comments: Unlike EC 2.4.1.64, α,α-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Eis, C. and Nidetzky, B. Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. Biochem. J. 363 (2002) 335-340. [PMID: 11931662]
2. Eis, C., Watkins, M., Prohaska, T. and Nidetzky, B. Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem. J. 356 (2001) 757-767. [PMID: 11389683]
3. Nidetzky, B. and Eis, C. α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem. J. 360 (2001) 727-736. [PMID: 11736665]
Common name: indolylacetylinositol arabinosyltransferase
Reaction: UDP-L-arabinose + indol-3-ylacetyl-1D-myo-inositol = UDP + indol-3-ylacetyl-myo-inositol 3-L-arabinoside
Other name(s): arabinosylindolylacetylinositol synthase
Systematic name: UDP-L-arabinose:indol-3-ylacetyl-myo-inositol L-arabinosyltransferase
Comments: The position of acylation is indeterminate because of the ease of acyl transfer between hydroxy groups. For a diagram showing the biosynthesis of UDP-L-arabinose, click here.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 84720-96-7
References:
1. Corcuera, L.J. and Bandurski, R.S. Biosynthesis of indol-3-yl-acetyl-myo-inositol arabinoside in kernels of Zea mays L. Plant Physiol. 70 (1982) 1664-1666.
Common name: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
Reaction: 2-oxoglutarate + isochorismate = (1S,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate + pyruvate + CO2
For diagram of reaction click here and mechanism click here.
Other name(s): 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase—α-ketoglutarate decarboxylase; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase; 6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate synthase; SHCHC synthase;
Systematic name: isochorismate:2-oxoglutarate:cyclodienyltransferase (decarboxylating, pyruvate-forming)
Comments: In the first step of the reaction, the oxoglutarate is decarboxylated and an adduct of the succinic semialdhyde is formed with thiamine diphosphate of the enzyme, as in both E1 of the 2-oxoglutarate dehydrogenase complex [EC 1.2.4.2, oxoglutarate dehydrogenase (lipoamide)] and in the reaction of 2-oxoglutarate decarboxylase (EC 4.1.1.71), which liberates free succinic semialdehyde.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Palaniappan, C., Sharma, V., Hudspeth, M.E. and Meganathan, R. Menaquinone (vitamin K2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and α-ketoglutarate decarboxylase activities. J. Bacteriol. 174 (1992) 8111-8118. [PMID: 1459959]
2. Palaniappan, C., Taber, H. and Meganathan, R. Biosynthesis of o-succinylbenzoic acid in Bacillus subtilis: identification of menD mutants and evidence against the involvement of the α-ketoglutarate dehydrogenase complex. J. Bacteriol. 176 (1994) 2648-2653. [PMID: 8169214]
[EC 2.7.1.152 Transferred entry: now EC 2.7.4.21 inositol-hexakisphosphate kinase. (EC 2.7.1.152 created 2002, deleted 2003)]
Common name: diphosphoinositol-pentakisphosphate kinase
Reaction: ATP + 5-diphospho-1D-myo-inositol pentakisphosphate = ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate (isomeric configuration unknown)
Systematic name: ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Shears, S.B., Ali, N., Craxton, A. and Bembenek, M.E. Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo. J. Biol. Chem. 270 (1995) 10489-10497. [PMID: 7737983]
2. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]
Common name: inositol-hexakisphosphate kinase
Reaction: (1) ATP + 1D-myo-inositol hexakisphosphate = ADP + 5- diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate
(2) ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + diphospho-1D-myo-inositol tetrakisphosphate (isomeric configuration unknown)
Other name(s): ATP:1D-myo-inositol-hexakisphosphate phosphotransferase
Systematic name: ATP:1D-myo-inositol-hexakisphosphate 5-phosphotransferase
Comments: Three mammalian isoforms are known to exist.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]
2. Schell, M.J., Letcher, A.J., Brearley, C.A., Biber, J., Murer, H. and Irvine, R.F. PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase. FEBS Lett. 461 (1999) 169-172. [PMID: 10567691]
3. Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553-560. [PMID: 9359429]
Common name: cysteine desulfurase
Reaction: L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
Other name(s): IscS; NIFS; NifS; SufS; cysteine desulfurylase
Systematic name: L-cysteine:[enzyme cysteine] sulfurtransferase
Comments: A pyridoxal-phosphate protein. The reaction shown is the first part of a catalytic reaction, which is completed by passing on its extra sulfur to other acceptors. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1]. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) and functions by mobilizing sulfur [2].
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Zheng, L.M., White, R.H., Cash, V.L., Jack, R.F. and Dean, D.R. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90 (1993) 2754-2758. [PMID: 8464885]
2. Mihara, H. and Esaki, N. Bacterial cysteine desulfurases: Their function and mechanisms. Appl. Microbiol. Biotechnol. 60 (2002) 12-23. [PMID: 12382038]
3. Frazzon, J. and Dean, D.R. Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7 (2003) 166-173. [PMID: 12714048]
Common name: crossover junction endodeoxyribonuclease
Reaction: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction)
Other name(s): Hje endonuclease; Holliday junction endonuclease CCE1; Holliday junction resolvase; Holliday junction-cleaving endonuclease; Holliday junction-resolving endoribonuclease; RusA Holliday junction resolvase; RusA endonuclease; RuvC endonuclease; SpCCe1 Holliday junction resolvase; crossover junction endoribonuclease; cruciform-cutting endonuclease; endo X3; endonuclease RuvC; endonuclease VII; endonuclease X3; resolving enzyme CCE1
Comments: The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 99676-43-4
References:
1. Symington, L.S. and Kolodner, R. Partial purification of an enzyme from Saccharomyces cerevisiae that cleaves Holliday junctions. Proc. Natl. Acad. Sci. USA 82 (1985) 7247-7251. [PMID: 9308179]
2. Shida, T., Iwasaki, H., Saito, A., Kyogoku, Y. and Shinagawa, H. Analysis of substrate specificity of the RuvC holliday junction resolvase with synthetic Holliday junctions. J. Biol. Chem. 271 (1996) 26105-26109.[PMID: 8824253]
3. Shah, R., Cosstick, R. and West, S.C. The RuvC protein dimer resolves Holliday junctions by a dual incision mechanism that involves base-specific contacts. EMBO J. 16 (1997) 1464-1472. [PMID: 9135161]
4. Fogg, J.M., Schofield, M.J., White, M.F. and Lilley, D.M. Sequence and functional-group specificity for cleavage of DNA junctions by RuvC of Escherichia coli. Biochemistry 38 (1999) 11349-11358. [PMID: 10471285]
5.Middleton, C.L., Parker, J.L., Richard, D.J., White, M.F. and Bond, C.S. Crystallization and preliminary X-ray diffraction studies of Hje, a Holliday junction resolving enzyme from Sulfolobus solfataricus. Acta Crystallogr. D Biol. Crystallogr. 59 (2003) 171-173. [PMID: 12499561]
[EC 3.2.1.138 Transferred entry: now EC 4.2.2.15 anhydrosialidase. (EC 3.2.1.138 created 1992, deleted 2003)]
Common name: oligoxyloglucan reducing-end-specific cellobiohydrolase
Reaction: Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a β-1,4-linked glucan carrying α-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
Systematic name: oligoxyloglucan reducing-end cellobiohydrolase
Comments: The enzyme is found in the fungus Geotrichum sp. M128. The substrate is a hemicellulose found in plant cell walls.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Yaoi, K. and Mitsuishi, Y. Purification, characterization, cloning, and expression of a novel xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase. J. Biol. Chem. 277, (2002) 48276-48281. [PMID: 12374797]
Common name: xyloglucan-specific endo-β-1,4-glucanase
Reaction: xyloglucan + H2O = xyloglucan oligosaccharides (endohydrolysis of 1,4-β-D-glucosidic linkages in xyloglucan)
Other name(s): XEG; xyloglucan endo-β-1,4-glucanase; xyloglucanase; xyloglucanendohydrolase (XH)
Systematic name: 1,4-β-D-glucan glucanohydrolase
Comments: The enzyme for Aspergillus aculeatus is specific for xyloglucan and does not hydrolyse other cell-wall components. It cleaves glycosidic bonds with retention of the β-configuration of the glycosyl residues.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Pauly, M., Andersen, L.N., Kaupinnen, S., Kofod, L.V., York, W.S., Albersheim, P. and Darvill, A. A xyloglucan specific endo-β-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme. Glycobiology 9 (1999) 93-100. [PMID: 9884411]
Common name: dCTP deaminase (dUMP-forming)
Reaction: dCTP + 2 H2O = dUMP + diphosphate + NH3
Systematic name: dCTP aminohydrolase (dUMP-forming)
Comments: Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Li, H., Xu, H., Graham, D.E. and White, R.H. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278 (2003) 11100-11106. [PMID: 12538648]
[EC 3.6.1.46 Transferred entry: now EC 3.6.5.1 heterotrimeric G-protein GTPase. (EC 3.6.1.46 created 2000, deleted 2003)]
[EC 3.6.1.47 Transferred entry: now EC 3.6.5.2 small monomeric GTPase. (EC 3.6.1.47 created 2000, deleted 2003)]
[EC 3.6.1.48 Transferred entry: now EC 3.6.5.3 protein-synthesizing GTPase. (EC 3.6.1.48 created 2000, deleted 2003)]
[EC 3.6.1.49 Transferred entry: now EC 3.6.5.4 signal-recognition-particle GTPase. (EC 3.6.1.49 created , deleted 2003)]
[EC 3.6.1.50 Transferred entry: now EC 3.6.5.5 dynamin GTPase. (EC 3.6.1.50 created 2000, deleted 2003)]
[EC 3.6.1.51 Transferred entry: now EC 3.6.5.6 tubulin GTPase. (EC 3.6.1.51 created 2000, deleted 2003)]
EC 3.6.5 Acting on GTP; involved in cellular and subcellular movement
Common name: heterotrimeric G-protein GTPase
Reaction: GTP + H2O = GDP + phosphate
Systematic name: GTP phosphohydrolase (signalling)
Comments: This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different α subunits (39-52 kDa), 5 β subunits (36 kDa) and 12 γ subunits (6-9 kDa) are known.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Neer, E.J. Heterotrimeric G proteins: organizers of transmembrane signals. Cell 80 (1995) 249-259. [PMID: 7834744]
2. Sprang, S.R. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66 (1997) 639-678. [PMID: 9242920]
3. Bondarenko, V.A., Deasi, M., Dua, S., Yamazaki, M., Amin, R.H., Yousif, K.K., Kinumi, T., Ohashi, M., Komori, N., Matsumoto, H., Jackson, K.W., Hayashi, F., Usukura, J., Lipikin, V.M. and Yamazaki, A. Residues within the polycationic region of cGMP phosphodiesterase γ subunit crucial for the interaction with transducin α subunit. Identification by endogenous ADP-ribosylation and site-directed mutagenesis. J. Biol. Chem. 272 (1997) 15856-15864. [PMID: 9188484]
4. Ming, D., Ruiz-Avila, L. and Margolskee, R.F. Characterization and solubilization of bitter-responsive receptors that couple to gustducin. Proc. Natl. Acad. Sci. USA 95 (1998) 8933-8938. [PMID: 9671782]
Common name: small monomeric GTPase
Reaction: GTP + H2O = GDP + phosphate
Systematic name: GTP phosphohydrolase (cell-regulating)
Comments:A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the α-subunit of heterotrimeric G-protein GTPase (EC 3.6.1.46). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Bourne, H.R., Sanders, D.A. and McCormick, F. The GTPase superfamily: conserved structure and molecular mechanisms. Nature 349 (1991) 117-127. [PMID: 1898771]
2. Hall, A. Small GTP-binding proteins and the regulation of actin cytoskeleton. Annu. Rev. Cell Biol. 10 (1994) 31-54. [PMID: 7888179]
3. Geyer, M. and Wittinghofer, A. GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins. Curr. Opin. Struct. Biol. 7 (1997) 786-792. [PMID: 9434896]
4. Vitale, N., Moss, J. and Vaughan, M. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). J. Biol. Chem. 273 (1998) 2553-2560. [PMID: 9446556]
Common name: protein-synthesizing GTPase
Reaction: GTP + H2O = GDP + phosphate
Other name(s): elongation factor (EF); initiation factor (IF); peptide-release or termination factor
Systematic name: GTP phosphohydrolase (mRNA-translation-assisting)
Comments: This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis. In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyses it in prokaryotes. In eukaryotes, it is eIF-2 (150 kDa) that binds GTP. In the elongation phase, the GTP-hydrolysing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1α (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa). EF-Tu and EF-1α catalyse binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyse the translocation of peptidyl-tRNA from the A-site to the P-site. GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Kurzchalia, T.V., Bommer, U.A., Babkina, G.T. and Karpova, G.G. GTP interacts with the γ-subunit of eukaryotic initiation factor EIF-2. FEBS Lett. 175 (1984) 313-316. [PMID: 6566615]
2. Kisselev, L.L. and Frolova, L.Yu. Termination of translation in eukaryotes. Biochem. Cell Biol. 73 (1995) 1079-1086. [PMID: 8722024]
3. Rodnina, M.V., Savelsberg, A., Katunin, V.I. and Wintermeyer, W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385 (1997) 37-41. [PMID: 8985244]
4. Freistroffer, D.V., Pavlov, M.Y., MacDougall, J., Buckingham, R.H. and Ehrenberg, M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J. 16 (1997) 4126-4133. [PMID: 9233821]
5. Krab, I.M. and Parmeggiani, A. EF-Tu, a GTPase odyssey. Biochim. Biophys. Acta 1443, (1998) 1-22. [PMID: 9838020]
Common name: signal-recognition-particle GTPase
Reaction: GTP + H2O = GDP + phosphate
Systematic name: GTP phosphohydrolase (protein-synthesis-assisting)
Comments: Activity is associated with the signal-recognition particle (a protein- and RNA-containing structure involved in endoplasmic-reticulum-associated protein synthesis).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Connolly, T. and Gilmore, R. The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide. Cell 57 (1989) 599-610. [PMID: 2541918]
2. Connolly, T., Rapiejko, P.J. and Gilmore, R. Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor. Science 252 (1991) 1171-1173. [PMID: 1851576]
3. Miller, J.D., Wilhelm, H., Gierasch, L., Gilmore, R. and Walter, P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366 (1993) 351-354. [PMID: 8247130]
4. Freymann, D.M., Keenan, R.J., Stroud, R.M. and Walter, P. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385 (1997) 361-364. [PMID: 9002524]
Common name: dynamin GTPase
Reaction: GTP + H2O = GDP + phosphate
Systematic name: GTP phosphohydrolase (vesicle-releasing)
Comments: An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Warnock, D.E. and Schmid, S.L. Dynamin GTPase, a force-generating molecular switch. Bioessays 18 (1996) 885-893. [PMID: 8939066]
2. McClure, S.J. and Robinson, P.J. Dynamin, endocytosis and intracellular signalling. Mol. Membr. Biol. 13 (1996) 189-215. [PMID: 9116759]
3. Oh, P., McIntosh, D.P. and Schnitzer, J.E. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141 (1998) 101-114. [PMID: 9531551]
Common name: tubulin GTPase
Reaction: GTP + H2O = GDP + phosphate
Systematic name: GTP phosphohydrolase (microtubule-releasing)
Comments: An intrinsic activity of α-tubulin involved in tubulin folding, division plane formation in prokaryotic cells and others.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Yu, X.C. and Margolin, W. Ca2+-mediated GTP-dependent dynamic assembly of bacetrial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 16, (1997) 5455-5463. [PMID: 9312004]
2. Tian, G., Bhamidipati, A., Cowan, N.J . and Lewis, S.A. Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the α/β-tubulin heterodimer. J. Biol. Chem. 274, (1999) 24054-24058. [PMID: 10446175]
3. Roychowdhury, S., Panda, D., Wilson, L. and Rasenick, M.M. G protein α subunits activate tubulin GTPase and modulate microtubule polymerization dynamics. J. Biol. Chem. 274, (1999) 13485-13490. [PMID: 10224115]
Common name: (S)-2-haloacid dehalogenase
Reaction: (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
For diagram click here.
Other name(s): 2-haloacid dehalogenase[ambiguous]; 2-haloacid halidohydrolase [ambiguous][ambiguous]; 2-haloalkanoic acid dehalogenase; 2-haloalkanoid acid halidohydrolase; 2-halocarboxylic acid dehalogenase II; DL-2-haloacid dehalogenase[ambiguous]; L-2-haloacid dehalogenase; L-DEX
Systematic name: (S)-2-haloacid halidohydrolase
Comments: Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.9 (R)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37289-39-7
References:
1. Goldman, P., Milne, G.W.A. and Keister, D.B. Carbon-halogen bond cleavage. 3. Studies on bacterial halidohyrolases. J. Biol. Chem. 243 (1968) 428-434. [PMID: 5635785]
2. Motosugi, M., Esaki, N. and Soda, K. Preparation and properties of 2-halo acid dehalogenase from Pseudomonas putida. Agric. Biol. Chem. 46 (1982) 837-838.
3. Klages, M., Krauss, S. and Lingens, F. 2-Haloacid dehalogenase from a 4-chlorobenzoate-degrading Pseudomonas spec. CBS 3. Hoppe-Seyler's Z. Physiol. Chem. 364 (1983) 529-535. [PMID: 6873881]
4. Diez, A., Prieto, M.I., Alvarez, M.J., Bautista, J.M., Garrido, J. and Puyet, A. Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation. Biochem. Biophys. Res. Commun. 220 (1996) 828-833. [PMID: 8607850]
5. Mörsberger, F.-M., Müller, R., Otto, M.K., Lingens, F. and Kulbe, K.D. Purification and characterization of 2-halocarboxylic acid dehalogenase II from Pseudomonas spec. CBS 3. Biol. Chem. Hoppe-Seyler 372 (1991) 915-922. [PMID: 1772590]
6. Köhler, R., Brokamp, A., Schwarze, R., Reiting, R.H. and Schmidt, F.R.J. Characteristics and DNA-sequence of a cryptic haloalkanoic acid dehalogenase from Agrobacterium tumefaciens RS5. Curr. Microbiol. 36 (1998) 96-101. [PMID: 9425247]
7. Motosugi, K., Esahi, N. and Soda, K. Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase. Arch. Microbiol. 131, (1982) 179-183. [PMID: 7103659]
8. Kurihara, T., Esaki, N. and Soda, K. Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms. J. Mol. Catal. B 10, (2000) 57-65.
9. Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi, M., Tsunasawa, S. and Esaki, N. Bacterial 2-haloacid dehalogenases: Structures and catalytic properties. Pure Appl. Chem. 68, (1996) 2097-2103.
[EC 3.8.1.4 Transferred entry: now EC 1.97.1.10 thyroxine 5'-deiodinase (EC 3.8.1.4 created 1984, deleted 2003)]
Common name: (R)-2-haloacid dehalogenase
Reaction: (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
Other name(s): 2-haloalkanoic acid dehalogenase[ambiguous]; 2-haloalkanoid acid halidohydrolase[ambiguous]; D-2-haloacid dehalogenase; D-DEX
Systematic name: (R)-2-haloacid halidohydrolase
Comments: Acts on acids of short chain lengths, C2 to C4, with inversion of configuration at C-2. [See also EC 3.8.1.2(S)-2-haloacid dehalogenase, EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting) and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 119345-29-8
References:
1. Smith, J.M., Harrison, K. and Colby, J. Purification and characterization of D-2-haloacid dehalogenase from Pseudomonas putida strain AJ1/23. J. Gen. Microbiol. 136 (1990) 881-886. [PMID: 2380688]
2. Leigh, J.A., Skinner, A.J. and Cooper, R.A. Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species. FEMS Microbiol. Lett. 49 (1988) 353-356.
3. Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi, M., Tsunasawa, S. and Esaki, N. Bacterial 2-haloacid dehalogenases: Structures and catalytic properties. Pure Appl. Chem. 68 (1996) 2097-2103.
Common name: 2-haloacid dehalogenase (configuration-inverting)
Reaction: (1) (S)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
or
(2) (R)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
For diagram click here.
Other name(s): 2-haloalkanoic acid dehalogenase; 2-haloalkanoid acid halidohydrolase; DL-2-haloacid dehalogenase; DL-2-haloacid dehalogenase (inversion of configuration); DL-2-haloacid halidohydrolase (inversion of configuration); DL-DEXi
Systematic name: (R,S)-2-haloacid dehalogenase (configuration-inverting)
Comments: Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. The enzyme from Pseudomonas sp. 113 acts on 2-haloalkanoic acids whose carbon chain lengths are five or less. [See also EC 3.8.1.2(S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.11 2-haloacid dehalogenase (configuration-retaining)]
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Motosugi, K., Esahi, N. and Soda, K. Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase. Arch. Microbiol. 131 (1982) 179-183. [PMID: 7103659]
2. Motosugi, K., Esahi, N. and Soda, K. Purification and properties of a new enzyme, DL-2-haloacid dehalogenase, from Pseudomonas sp. J. Bacteriol. 150 (1982) 522-527. [PMID: 7068529]
3. Motosugi, K., Esahi, N. and Soda, K. Enzymatic preparation of D- and L-lactic acid from racemic 2-chloropropionic acid. Biotechnol. Bioeng. 26 (1984) 805-806.
4. Kurihara, T., Esaki, N. and Soda, K. Bacterial 2-haloacid dehalogenases: structures and reaction mechanisms. J. Mol. Catal. B 10 (2000) 57-65.
5. Liu, J.-Q., Kurihara, T., Hasan, A.K.M.Q., Nardi-Dei, V., Koshikawa, H., Esaki, N. and Soda, K. Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL. Appl. Environ. Microbiol. 60 (1994) 2389-2393. [PMID: 8074519]
6. Cairns, S.S., Cornish, A. and Cooper, R.A. Cloning, sequencing and expression in Escherichia coli of two Rhizobium sp. genes encoding haloalkanoate dehalogenases of opposite stereospecificity. Eur. J. Biochem. 235 (1996) 744-749. [PMID: 8654424]
7. Leigh, J.A., Skinner, A.J. and Cooper, R.A. Partial purification, stereospecificity and stoichiometry of three dehalogenases from a Rhizobium species. FEMS Microbiol. Lett. 49 (1988) 353-356.
8. Weightman, A.J., Weightman, A.L. and Slater, J.H. Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: evidence for two different dehalogenation mechanisms. J. Gen. Microbiol. 128 (1982) 1755-1762. [PMID: 7142958]
9. Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi, M., Tsunasawa, S. and Esaki, N. Bacterial 2-haloacid dehalogenases: Structures and catalytic properties. Pure Appl. Chem. 68 (1996) 2097-2103.
Common name: 2-haloacid dehalogenase (configuration-retaining)
Reaction: (1) (S)-2-haloacid + H2O = (S)-2-hydroxyacid + halide
or
(2) (R)-2-haloacid + H2O = (R)-2-hydroxyacid + halide
Systematic name: (R,S)-2-haloacid dehalogenase (configuration-retaining)
Other name(s): 2-haloalkanoic acid dehalogenase; 2-haloalkanoid acid halidohydrolase; DL-2-haloacid dehalogenase; DL-DEXr
Systematic name:
Comments: Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (S)- and (R)-hydroxyalkanoic acids, respectively, with retention of configuration at C-2. [See also EC 3.8.1.2(S)-2-haloacid dehalogenase, EC 3.8.1.9 (R)-2-haloacid dehalogenase and EC 3.8.1.10 2-haloacid dehalogenase (configuration-inverting)]
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Weightman, A.J., Weightman, A.L. and Slater, J.H. Stereospecificity of 2-monochloropropionate dehalogenation by the two dehalogenases of Pseudomonas P3: evidence for two different dehalogenation mechanisms. J. Gen. Microbiol. 128 (1982) 1755-1762. [PMID: 7142958]
2. Soda, K., Kurihara, T., Liu, J.-Q., Nardi-Dei, V., Park, C., Miyagi, M., Tsunasawa, S. and Esaki, N. Bacterial 2-haloacid dehalogenases: Structures and catalytic properties. Pure Appl. Chem. 68 (1996) 2097-2103.
Common name: anhydrosialidase
Reaction: Elimination of α-sialyl groups in N-acetylneuraminic acid glycosides, releasing 2,7-anhydro-α-N-acetylneuraminate
For diagram click here.
Other name(s): anhydroneuraminidase; sialglycoconjugate N-acylneuraminylhydrolase (2,7-cyclizing); sialidase L
Systematic name: glycoconjugate sialyl-lyase (2,7-cyclizing)
Comments: Also acts on N-glycolylneuraminate glycosides. cf. EC 3.2.1.18 (exo-α-sialidase) and EC 3.2.1.129 (endo-α-sialidase).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 157857-11-9
References:
1. Li, Y.-T., Nakagawa, H., Ross, S.A., Hansson, G.C. and Li, S.C. A novel sialidase which releases 2,7-anhydro-α-N-acetylneuraminic acid from sialoglycoconjugates. J. Biol. Chem. 265 (1990) 21629-21633. [PMID: 91072361]
Common name: (4S)-limonene synthase
Reaction: geranyl diphosphate = (-)-(4S)-limonene + diphosphate
For diagram click here.
Glossary:
limonene: a monoterpenoid
Other name(s): (-)-(4S)-limonene synthase; 4S-(-)-limonene synthase; geranyldiphosphate diphosphate lyase (limonene forming)
Systematic name: geranyldiphosphate diphosphate lyase [(4S)-limonene-forming]
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) requires Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784-21792. [PMID: 9268308]
2. Collby, S.M., Alonso, W.R., Katahira, E.J., McGarvey, D.J. and Croteau, R. 4S-Limonene synthase from the oil glands of spearmint (Mentha spicata). cDNA isolation, characterization, and bacterial expression of the catalytically active monoterpene cyclase. J. Biol. Chem. 268 (1993) 23016-23024. [PMID: 8226816]
3. Yuba, A., Yazaki, K., Tabata, M., Honda, G. and Croteau, R. cDNA cloning, characterization, and functional expression of 4S-(-)-limonene synthase from Perilla frutescens. Arch. Biochem. Biophys. 332 (1996) 280-287. [PMID: 8806736]
Common name: 3-(hydroxyamino)phenol mutase
Reaction: 3-hydroxyaminophenol = aminohydroquinone
Other name(s): 3-hydroxylaminophenol mutase; 3HAP mutase
Systematic name: 3-(hydroxyamino)phenol hydroxymutase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Schenzle, A., Lenke, H., Spain, J.C. and Knackmuss, H.J. 3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement. J. Bacteriol. 181 (1999) 1444-1450. [PMID: 10049374]
Common name: phosphopantothenate—cysteine ligase
Reaction: CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + PPi + (R)-4'-phosphopantothenoyl-L-cysteine
For diagram click here.
Other name(s): phosphopantothenoylcysteine synthetase
Systematic name: (R)-4'-phosphopantothenate:L-cysteine ligase
Comments: Cysteine can be replaced by some of its derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9023-50-1
References:
1. Brown, G.M. The metabolism of pantothenic acid. J. Biol. Chem. 234 (1959) 370-378.
2. Strauss, E., Kinsland, C., Ge, Y., McLafferty, F.W. and Begley, T.P. Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified Coenzyme A biosynthetic enzymes in bacteria. J. Biol. Chem. 276 (2001) 13513-13516. [PMID: 11278255]
3. Kupke, T. Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial Dfp flavoproteins. J. Biol. Chem. 277 (2002) 36137-36145. [PMID: 12140293]