IUBMB Enzyme Nomenclature

EC 2.4.1.250

Accepted name: D-inositol-3-phosphate glycosyltransferase

Reaction: UDP-N-acetyl-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP

For diagram of reaction click here

Other name(s): mycothiol glycosyltransferases; MshA

Systematic name: UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase

Comments: The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3]

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476-3479. [PMID: 12754249]

2. Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910-33920. [PMID: 16940050]

3. Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834-15844. [PMID: 18390549]

[EC 2.4.1.250 created 2010]


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