The Enzyme Database

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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 phosphonate metabolism, 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
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. [DOI] [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. [DOI] [PMID: 21705661]
3.  Zhang, Q. and van der Donk, W.A. Answers to the carbon-phosphorus lyase conundrum. ChemBioChem 13 (2012) 627–629. [DOI] [PMID: 22334536]
[EC created 2013, modified 2016]

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