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| - | [[Image:2byx.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2byx.png|left|200px]] |
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| | {{STRUCTURE_2byx| PDB=2byx | SCENE= }} | | {{STRUCTURE_2byx| PDB=2byx | SCENE= }} |
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| - | '''KAS I LYS328ALA MUTANT IN COMPLEX WITH FATTY ACID'''
| + | ===KAS I LYS328ALA MUTANT IN COMPLEX WITH FATTY ACID=== |
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| - | ==Overview==
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| - | Beta-ketoacyl-acyl carrier protein (ACP) synthase enzymes join short carbon units to construct fatty acyl chains by a three-step Claisen condensation reaction. The reaction starts with a trans thioesterification of the acyl primer substrate from ACP to the enzyme. Subsequently, the donor substrate malonyl-ACP is decarboxylated to form a carbanion intermediate, which in the third step attacks C1 of the primer substrate giving rise to an elongated acyl chain. A subgroup of beta-ketoacyl-ACP synthases, including mitochondrial beta-ketoacyl-ACP synthase, bacterial plus plastid beta-ketoacyl-ACP synthases I and II, and a domain of human fatty acid synthase, have a Cys-His-His triad and also a completely conserved Lys in the active site. To examine the role of these residues in catalysis, H298Q, H298E and six K328 mutants of Escherichia colibeta-ketoacyl-ACP synthase I were constructed and their ability to carry out the trans thioesterification, decarboxylation and/or condensation steps of the reaction was ascertained. The crystal structures of wild-type and eight mutant enzymes with and/or without bound substrate were determined. The H298E enzyme shows residual decarboxylase activity in the pH range 6-8, whereas the H298Q enzyme appears to be completely decarboxylation deficient, showing that H298 serves as a catalytic base in the decarboxylation step. Lys328 has a dual role in catalysis: its charge influences acyl transfer to the active site Cys, and the steric restraint imposed on H333 is of critical importance for decarboxylation activity. This restraint makes H333 an obligate hydrogen bond donor at Nepsilon, directed only towards the active site and malonyl-ACP binding area in the fatty acid complex.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16441657}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16441657 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16441657}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipid synthesis]] | | [[Category: Lipid synthesis]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:59:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:43:45 2008'' |
Revision as of 01:43, 29 July 2008
Template:STRUCTURE 2byx
KAS I LYS328ALA MUTANT IN COMPLEX WITH FATTY ACID
Template:ABSTRACT PUBMED 16441657
About this Structure
2BYX is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1oer. Full crystallographic information is available from OCA.
Reference
Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases., von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A, FEBS J. 2006 Feb;273(4):695-710. PMID:16441657
Page seeded by OCA on Tue Jul 29 04:43:45 2008
