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2iwy
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="2iwy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iwy, resolution 2.06Å" /> '''HUMAN MITOCHONDRIAL...)
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Revision as of 16:06, 29 October 2007
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HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE
Overview
Two distinct ways of organizing fatty acid biosynthesis exist: the, multifunctional type I fatty acid synthase (FAS) of mammals, fungi, and, lower eukaryotes with activities residing on one or two polypeptides; and, the dissociated type II FAS of prokaryotes, plastids, and mitochondria, with individual activities encoded by discrete genes. The beta-ketoacyl, [ACP] synthase (KAS) moiety of the mitochondrial FAS (mtKAS) is targeted, by the antibiotic cerulenin and possibly by the other antibiotics, inhibiting prokaryotic KASes: thiolactomycin, platensimycin, and the, alpha-methylene butyrolactone, C75. The high degree of structural, similarity between mitochondrial and prokaryotic KASes complicates, development of novel antibiotics targeting prokaryotic KAS without, affecting KAS domains of ... [(full description)]
About this Structure
2IWY is a [Single protein] structure of sequence from [Homo sapiens] with NH4 as [ligand]. Active as [[1]], with EC number [2.3.1.41]. Full crystallographic information is available from [OCA].
Reference
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase., Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A, Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430
Page seeded by OCA on Mon Oct 29 18:11:25 2007
Categories: Homo sapiens | Single protein | Christensen, C.E. | Henriksen, A. | Kragelund, B. | Wettstein-Knowles, P.Von. | NH4 | Acyltransferase | Beta- ketoacyl acp synthase | Cerulenin | Claisen condensation | Fatty acid biosynthesis | Fatty acid synthesis | Kas | Lipid synthesis | Mitochondria | Mitochondrion | Transferase | Transit peptide
