ENZYME entry: EC 188.8.131.526
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|2 S-adenosyl-L-methionine + N-acetyl-demethylphosphinothricin + reduced acceptor <=> S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetyl-phosphinothricin + oxidized acceptor|
- The enzyme was originally characterized from bacteria that produce
the tripeptides bialaphos and phosalacine, which inhibit plant and
bacterial glutamine synthetases.
- It is a radical S-adenosyl-L-methionine (SAM) enzyme.
- According to the proposed mechanism, the reduced iron-sulfur center
donates an electron to SAM, resulting in homolytic cleavage of the
carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts
the hydrogen atom from the P-H bond of the substrate, forming a
- This radical reacts with methylcob(III)alamin to produce the
methylated product and cob(II)alamin, which is reduced by an unknown
donor to cob(I)alamin.
- A potential route for restoring the latter back to
methylcob(III)alamin is a nucleophilic attack on a second SAM
- The enzyme acts in vivo on N-acetyl-demethylphosphinothricin-L-
alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-
leucine, the intermediates in the biosynthesis of bialaphos and
- This transformation produces the only example of a carbon-phosphorus-
carbon linkage known to occur in nature.
|PRIAM enzyme-specific profiles||184.108.40.2066|
|KEGG Ligand Database for Enzyme Nomenclature||220.127.116.116|
|IUBMB Enzyme Nomenclature||18.104.22.1686|
|MEDLINE||Find literature relating to 22.214.171.1246|
|Rhea expert-curated reactions||126.96.36.1996|
entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-