IUBMB Enzyme Nomenclature

EC 4.7.1.1

Accepted name: α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase

Reaction: α-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine + reduced electron acceptor = α-D-ribose 1,2-cyclic phosphate 5-phosphate + methane + L-methionine + 5'-deoxyadenosine + oxidized electron acceptor

For diagram of reaction click here.

Other name(s): phnJ (gene name)

Systematic name: α-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)

Comments: This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional α-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. α-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and α-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).

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

References:

1. Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570-573. [PMID: 22089136]

2. Jochimsen, B., Lolle, S., McSorley, F.R., Nabi, M., Stougaard, J., Zechel, D.L. and Hove-Jensen, B. Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc. Natl. Acad. Sci. USA 108 (2011) 11393-11398. [PMID: 21705661]

3. Zhang, Q. and van der Donk, W.A. Answers to the carbon-phosphorus lyase conundrum. Chembiochem 13 (2012) 627-629. [PMID: 22334536]

[EC 4.7.1.1 created 2013, modified 2016]


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