2dap
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(New page: 200px<br /> <applet load="2dap" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dap, resolution 2.2Å" /> '''C. GLUTAMICUM DAP DE...)
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Revision as of 18:59, 29 October 2007
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C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH DAP
Overview
The three-dimensional structures of Corynebacterium glutamicum, diaminopimelate dehydrogenase as a binary complex with the substrate, meso-diaminopimelate (meso-DAP) and a ternary complex with NADP+ and an, isoxazoline inhibitor [Abbot, S.D., Lane-Bell, P., Kanwar, P.S.S., and, Vederas, J. C. (1994) J. Am. Chem. Soc. 116, 6513-6520] have been solved, and refined against X-ray diffraction data to 2.2 A. Diaminopimelate, dehydrogenase is a homodimer of approximately 35,000 molecular weight, subunits and is the only dehydrogenase present in the bacterial, diaminopimelate/lysine biosynthetic pathway. Inhibitors of the enzymes of, L-lysine biosynthesis have been proposed as potential antibiotics or, herbicides, since mammals lack this metabolic pathway. Diaminopimelate, dehydrogenase catalyzes ... [(full description)]
About this Structure
2DAP is a [Single protein] structure of sequence from [Corynebacterium glutamicum] with API as [ligand]. Active as [[1]], with EC number [1.4.1.16]. Full crystallographic information is available from [OCA].
Reference
Substrate and inhibitor binding sites in Corynebacterium glutamicum diaminopimelate dehydrogenase., Scapin G, Cirilli M, Reddy SG, Gao Y, Vederas JC, Blanchard JS, Biochemistry. 1998 Mar 10;37(10):3278-85. PMID:9521647
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