Lyases;
carbon-phosphorus lyases;
carbon-phosphorus lyases (only sub-subclass identified to date)
BRITE hierarchy

alpha-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)

alpha-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine + reduced electron acceptor = alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + methane + L-methionine + 5'-deoxyadenosine + oxidized electron acceptor [RN:R10204]

R10204
Reaction

alpha-D-ribose 1-methylphosphonate 5-phosphate [CPD:C20423];
S-adenosyl-L-methionine [CPD:C00019];
reduced electron acceptor

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 alpha-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. alpha-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and alpha-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).

EC 4.7.1.1 created 2013, modified 2016

1  [PMID:22089136]

Kamat SS, Williams HJ, Raushel FM

Intermediates in the transformation of phosphonates to phosphate by bacteria.

Nature 480:570-3 (2011)
DOI:10.1038/nature10622

[eco:b4098]

2  [PMID:21705661]

Jochimsen B, Lolle S, McSorley FR, Nabi M, Stougaard J, Zechel DL, 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 U S A 108:11393-8 (2011)
DOI:10.1073/pnas.1104922108

3  [PMID:22334536]

Zhang Q, van der Donk WA

Answers to the carbon-phosphorus lyase conundrum.

Chembiochem 13:627-9 (2012)
DOI:10.1002/cbic.201200020