EC |
2.1.1.398 |
Accepted name: |
isoflavone 3′-O-methyltransferase |
Reaction: |
S-adenosyl-L-methionine + a 3′-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 3′-methoxyisoflavone |
Other name(s): |
PlOMT4; OMT4; 3′-OMT |
Systematic name: |
S-adenosyl-L-methionine:3′-hydroxyisoflavone 3′-O-methyltransferase |
Comments: |
The enzyme catalyses a step in the biosynthesis of 3′-methoxypuerarin, an isoflavone with bioactive properties isolated from the roots of the leguminous plant Pueraria lobata var. leguminosa. The highest activity has been found for 3′-hydroxydaidzein. The enzyme has low activity on the 3′-hydroxyflavones luteolin and quercetin. 3′-hydroxypuerarin is not a substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Li, J., Li, C., Gou, J. and Zhang, Y. Molecular cloning and functional characterization of a novel isoflavone 3′-O-methyltransferase from Pueraria lobata. Front. Plant Sci. 7:793 (2016). [DOI] [PMID: 27458460] |
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[EC 2.1.1.398 created 2024] |
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