Entry Name (+)-6a-hydroxymaackiain 3-O-methyltransferase;
Class Transferases;BRITE hierarchy
Sysname S-adenosyl-L-methionine:(+)-6a-hydroxymaackiain 3-O-methyltransferase
Reaction(IUBMB) S-adenosyl-L-methionine + (+)-6a-hydroxymaackiain = S-adenosyl-L-homocysteine + (+)-pisatin [RN:
R07750 ]
Reaction(KEGG) Substrate S-adenosyl-L-methionine [CPD:
C00019 ];
(+)-6a-hydroxymaackiain [CPD:
C16230 ]
Product S-adenosyl-L-homocysteine [CPD:
C00021 ];
(+)-pisatin [CPD:
C10516 ]
Comment The protein from the plant Pisum sativum (garden pea) methylates (+)-6a-hydroxymaackiain at the 3-position. It also methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position (cf. EC
2.1.1.212 , 2,7,4-trihydroxyisoflavanone 4-O-methyltransferase) with lower activity.
History EC 2.1.1.270 created 2013
Pathway ec01110 Biosynthesis of secondary metabolites
Orthology K21513 (+)-6a-hydroxymaackiain 3-O-methyltransferase
Genes Taxonomy Reference Authors Preisig CL, Matthews DE, Vanetten HD
Title Purification and Characterization of S-Adenosyl-l-methionine:6a-Hydroxymaackiain 3-O-Methyltransferase from Pisum sativum.
Journal Reference Authors Wu Q, Preisig CL, VanEtten HD
Title Isolation of the cDNAs encoding (+)6a-hydroxymaackiain 3-O-methyltransferase, the terminal step for the synthesis of the phytoalexin pisatin in Pisum sativum.
Journal Sequence Reference Authors Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP
Title Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
Journal Reference Authors Akashi T, VanEtten HD, Sawada Y, Wasmann CC, Uchiyama H, Ayabe S
Title Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis.
Journal Sequence Other DBs ExPASy - ENZYME nomenclature database: 2.1.1.270
