1bi5

From Proteopedia

Revision as of 13:49, 5 November 2007

CHALCONE SYNTHASE FROM ALFALFA

Overview

Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid, antimicrobial phytoalexins and anthocyanin pigments in plants. It produces, chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A, thioesters into a polyketide reaction intermediate that cyclizes. The, crystal structures of CHS alone and complexed with substrate and product, analogs reveal the active site architecture that defines the sequence and, chemistry of multiple decarboxylation and condensation reactions and, provides a molecular understanding of the cyclization reaction leading to, chalcone synthesis. The structure of CHS complexed with resveratrol also, suggests how stilbene synthase, a related enzyme, uses the same substrates, and an alternate cyclization pathway to form resveratrol. By using the, three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product, specificity. The structure elucidates the chemical basis of plant, polyketide biosynthesis and provides a framework for engineering CHS-like, enzymes to produce new products.

About this Structure

1BI5 is a Single protein structure of sequence from Medicago sativa. Active as Naringenin-chalcone synthase, with EC number 2.3.1.74 Structure known Active Site: CYS. Full crystallographic information is available from OCA.

Reference

Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis., Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP, Nat Struct Biol. 1999 Aug;6(8):775-84. PMID:10426957

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