1mkb
From Proteopedia
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[[Category: fatty acid biosynthesis]] | [[Category: fatty acid biosynthesis]] | ||
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Revision as of 13:38, 30 October 2007
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ESCHERICHIA COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE AT PH 5 AND 21 DEGREES C
Overview
BACKGROUND. Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, (dehydrase) is essential to the biosynthesis of unsaturated fatty acids, by shunting a 10-carbon intermediate from the saturated fatty acid pathway, into the unsaturated fatty acid pathway. Dehydrase catalyzes reactions of, dehydration and of double-bond isomerization on 10-carbon thiol esters of, acyl carrier protein (ACP). The aim of this work is to elucidate, mechanisms for the two enzymatic reactions, which occur in an unusual, bifunctional active site, and to understand the specificity of the enzyme, for substrates with 10-carbon fatty acyl chains. RESULTS. Crystal, structures at 2.0 A resolution for free dehydrase and for the enzyme, modified by its classic, mechanism-based inactivator, ... [(full description)]
About this Structure
1MKB is a [Single protein] structure of sequence from [Escherichia coli]. Active as [[acyl-carrier-protein_dehydratase 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase]], with EC number [4.2.1.60]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].
Reference
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site., Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL, Structure. 1996 Mar 15;4(3):253-64. PMID:8805534 [[Category: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase]]
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