3c3y
From Proteopedia
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'''Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum''' | '''Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum''' | ||
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[[Category: Rauh, D.]] | [[Category: Rauh, D.]] | ||
[[Category: Stubbs, M T.]] | [[Category: Stubbs, M T.]] | ||
| - | [[Category: | + | [[Category: O-methyltransferase]] |
| - | [[Category: | + | [[Category: Plant secondary metabolism]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 9 14:46:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr | + | |
Revision as of 11:46, 9 April 2008
Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum
Overview
Plant S-adenosyl-l-methionine-dependent class I natural product O-methyltransferases (OMTs), related to animal catechol OMTs, are dependent on bivalent cations and strictly specific for the meta position of aromatic vicinal dihydroxy groups. While the primary activity of these class I enzymes is methylation of caffeoyl coenzyme A OMTs, a distinct subset is able to methylate a wider range of substrates, characterized by the promiscuous phenylpropanoid and flavonoid OMT. The observed broad substrate specificity resides in two regions: the N-terminus and a variable insertion loop near the C-terminus, which displays the lowest degree of sequence conservation between the two subfamilies. Structural and biochemical data, based on site-directed mutagenesis and domain exchange between the two enzyme types, present evidence that only small topological changes among otherwise highly conserved 3-D structures are sufficient to differentiate between an enzymatic generalist and an enzymatic specialist in plant natural product methylation.
About this Structure
3C3Y is a Single protein structure of sequence from Mesembryanthemum crystallinum. Full crystallographic information is available from OCA.
Reference
Biochemical and Structural Analysis of Substrate Promiscuity in Plant Mg(2+)-Dependent O-Methyltransferases., Kopycki JG, Rauh D, Chumanevich AA, Neumann P, Vogt T, Stubbs MT, J Mol Biol. 2008 Feb 20;. PMID:18342334 Page seeded by OCA on Wed Apr 9 14:46:30 2008
