1eyp

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{{STRUCTURE_1eyp| PDB=1eyp | SCENE= }}
{{STRUCTURE_1eyp| PDB=1eyp | SCENE= }}
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'''CHALCONE ISOMERASE'''
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===CHALCONE ISOMERASE===
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==Overview==
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Chalcone isomerase (CHI) catalyzes the intramolecular cyclization of chalcone synthesized by chalcone synthase (CHS) into (2S)-naringenin, an essential compound in the biosynthesis of anthocyanin pigments, inducers of Rhizobium nodulation genes, and antimicrobial phytoalexins. The 1.85 A resolution crystal structure of alfalfa CHI in complex with (2S)-naringenin reveals a novel open-faced beta-sandwich fold. Currently, proteins with homologous primary sequences are found only in higher plants. The topology of the active site cleft defines the stereochemistry of the cyclization reaction. The structure and mutational analysis suggest a mechanism in which shape complementarity of the binding cleft locks the substrate into a constrained conformation that allows the reaction to proceed with a second-order rate constant approaching the diffusion controlled limit. This structure raises questions about the evolutionary history of this structurally unique plant enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 10966651 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10966651}}
==About this Structure==
==About this Structure==
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[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Chalcone isomerase]]
[[Category: Chalcone isomerase]]
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Revision as of 23:13, 30 June 2008

Image:1eyp.png

Template:STRUCTURE 1eyp

CHALCONE ISOMERASE

Template:ABSTRACT PUBMED 10966651

About this Structure

1EYP is a Single protein structure of sequence from Medicago sativa. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase., Jez JM, Bowman ME, Dixon RA, Noel JP, Nat Struct Biol. 2000 Sep;7(9):786-91. PMID:10966651

Page seeded by OCA on Tue Jul 1 02:13:23 2008

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