1mka

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(New page: 200px<br /> <applet load="1mka" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mka, resolution 2.0&Aring;" /> '''E. COLI BETA-HYDROXY...)
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==About this Structure==
==About this Structure==
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1MKA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with DAC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.60 4.2.1.60]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MKA OCA]].
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1MKA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with DAC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/3-hydroxydecanoyl-[acyl-carrier-protein]_dehydratase 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.60 4.2.1.60]]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MKA OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805534 8805534]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805534 8805534]
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[[Category: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: fatty acid biosynthesis]]
[[Category: fatty acid biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:35:57 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:16:18 2007''

Revision as of 09:11, 30 October 2007


1mka, resolution 2.0Å

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E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE

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

1MKA is a [Single protein] structure of sequence from [Escherichia coli] with DAC as [ligand]. 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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