Information on EC 2.1.1.326 - N-acetyldemethylphosphinothricin P-methyltransferase

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The expected taxonomic range for this enzyme is: Kitasatospora phosalacinea

EC NUMBER
COMMENTARY hide
2.1.1.326
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RECOMMENDED NAME
GeneOntology No.
N-acetyldemethylphosphinothricin P-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + N-acetyldemethylphosphinothricin + reduced acceptor = S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetylphosphinothricin + oxidized acceptor
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phosalacine biosynthesis
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phosphinothricin tripeptide biosynthesis
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + N-acetyldemethylphosphinothricin + reduced acceptor
S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetylphosphinothricin + oxidized acceptor
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + N-acetyldemethylphosphinothricin + reduced acceptor
S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + N-acetylphosphinothricin + oxidized acceptor
show the reaction diagram
A0A059U454
N-acetyldemethylphosphinothricin i.e. (2S)-2-acetamido-4-phosphinatobutanoate. In vivo the enzyme acts on N-acetyldemethylphosphinothricin-L-alanyl-L-alanine or N-acetyl-demethylphosphinothricin-L-alanyl-L-leucine, the intermediates in the biosynthesis of the tripeptides bialaphos and phosalacine (which inhibit plant and bacterial glutamine synthetases)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylcob(III)alamin
the enzyme is a radical S-adenosyl-L-methionine 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 S-adenosyl-L-methionine, 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 S-adenosyl-L-methionine molecule
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S] center
the enzyme is a radical S-adenosyl-L-methionine 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 S-adenosyl-L-methionine, 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 S-adenosyl-L-methionine molecule