Molecular aspects of beta-ketoacyl synthase (KAS) catalysis.

Abstract:

:Crystal structure data for Escherichia coli beta-ketoacyl synthase (KAS) I with C(10) and C(12) fatty acid substrates bound in conjunction with results from mutagenizing residues in the active site leads to a model for catalysis. Differences from and similarities to the other Claisen enzymes carrying out decarboxylations reveal two catalytic mechanisms, one for KAS I and KAS II, the other for KAS III and chalcone synthase. A comparison of the structures of KAS I and KAS II does not reveal the basis of chain-length specificity. The structures of the Arabidopsis thaliana KAS family are compared.

journal_name

Biochem Soc Trans

authors

von Wettstein-Knowles P,Olsen J,Arnvig Mcguire K,Larsen S

doi

10.1042/0300-5127:0280601

keywords:

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

601-7

issue

6

eissn

0300-5127

issn

1470-8752

journal_volume

28

pub_type

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