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).
deletion of the enzyme gene from Escherichia coli leads to the detection of alpha-D-ribose 1-methylphosphonate in the growth medium. alpha-D-Ribose 1-methylphosphonate is the ultimate substrate for the actual C-P lyase reaction
the carbon-phosphorus bond of the substrate is cleaved via a radical-based reaction to alpha-D-ribose 1,2-cyclic-phosphate 5-phosphate and methane in the presence of S-adenosyl-L-methionine. Enzyme additionally requires S-adenosyl-L-methionine