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2.1.1.15: fatty-acid O-methyltransferase

This is an abbreviated version!
For detailed information about fatty-acid O-methyltransferase, go to the full flat file.

Reaction

S-adenosyl-L-methionine
+
a fatty acid
=
S-adenosyl-L-homocysteine
+
a fatty acid methyl ester

Synonyms

BP2936, FAMT, fatty acid methyl-transferase, fatty acid methyltransferase, fatty acid O-methyltransferase, FmtB, MMAR_3356

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.15 fatty-acid O-methyltransferase

Crystallization

Crystallization on EC 2.1.1.15 - fatty-acid O-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure
the cocrystal structure of with S-adenosyl-L-homocysteine and octanoate shows that the substrate-binding site is largely localized within the alpha-helical domain that caps the Rossmann-like fold domain. Aliphatic and aromatic residues encircle the acyl chain of the fatty acid substrate, including Trp155, Met214, Phe222, Tyr224, Val256, Phe311, and Leu316. In the cocrystal structure with 3-hydroxydecanoate, only the S enantiomer is bound in the active site