1mkb

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spinqualitylabelsall models 1mkb, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [[1]], with EC number [4.2.1.60]. 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

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