Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase | Zendy

JeanLuc Ferrer | Zendy; Chloé Zubieta | Zendy; Richard A. Dixon | Zendy; Joseph P. Noel | Zendy

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Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase

Author(s) -

JeanLuc Ferrer,

Chloé Zubieta,

Richard A. Dixon,

Joseph P. Noel

Publication year - 2005

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.104.048751

Subject(s) - o methyltransferase , phenylpropanoid , methyltransferase , methylation , biosynthesis , biochemistry , transferase , methionine , biology , methionine synthase , chemistry , coenzyme a , enzyme , gene , amino acid , reductase

Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-l-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with the reaction products S-adenosine-l-homocysteine and feruloyl/sinapoyl CoAs presented here belong to a structurally and mechanistically distinct family of plant small molecule OMTs. These structures provide a new understanding of the substrate preferences and the catalytic mechanism accompanying CCoAOMT-mediated O-methylation of CoA-linked phenylpropanoid substrates.

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