2.1.1.326: N-acetyldemethylphosphinothricin P-methyltransferase

This is an abbreviated version!
For detailed information about N-acetyldemethylphosphinothricin P-methyltransferase, go to the full flat file.

Reaction

2 S-adenosyl-L-methionine +

Synonyms

BcpD, P-methylase, PhpK, SD_1168

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.326 N-acetyldemethylphosphinothricin P-methyltransferase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	AA Sequence
3	Cloned(Commentary)
4	Cofactor
3	General Information
2	Metals/Ions
1	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
10	Organism
4	Pathway
1	Purification (Commentary)
1	Reaction
9	Reference
14	Substrates and Products (Substrate)
2	Subunits
8	Synonyms
1	Systematic Name

Systematic Name

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Systematic Name on EC 2.1.1.326 - N-acetyldemethylphosphinothricin P-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Systematic Name Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SYSTEMATIC NAME

IUBMB Comments

S-adenosyl-L-methionine:N-acetyldemethylphosphinothricin P-methyltransferase

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 that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. 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 phosphinate-centered radical. 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 molecule. The enzyme acts in vivo on N-acetyldemethylphosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of bialaphos and phosalacine, respectively. This transformation produces the only example of a carbon-phosphorus-carbon linkage known to occur in nature.