Title : Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference.

Pub. Date : 2010 Dec

PMID : 21177481






1 Functional Relationships(s)
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1 While distal from the site of transmethylation, the propanoid tail substituent governs the kinetic preference of ryegrass COMT for aldehydes over alcohols and acids due to a single hydrogen bond donor for the C9 oxygenated moiety dictating the preference for an aldehyde. propanoid catechol-O-methyltransferase Homo sapiens