1dap
From Proteopedia
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C. GLUTAMICUM DAP DEHYDROGENASE IN COMPLEX WITH NADP+
Overview
Diaminopimelate dehydrogenase catalyzes the NADPH-dependent reduction of, ammonia and L-2-amino-6-ketopimelate to form meso-diaminopimelate, the, direct precursor of L-lysine in the bacterial lysine biosynthetic pathway., Since mammals lack this metabolic pathway inhibitors of enzymes in this, pathway may be useful as antibiotics or herbicides. Diaminopimelate, dehydrogenase catalyzes the only oxidative deamination of an amino acid of, D configuration and must additionally distinguish between two chiral amino, acid centers on the same symmetric substrate. The Corynebacterium, glutamicum enzyme has been cloned, expressed in Escherichia coli, and, purified to homogeneity using standard biochemical procedures [Reddy, S., G., Scapin, G., & Blanchard, J. S. (1996) Proteins: Structure, ... [(full description)]
About this Structure
1DAP is a [Single protein] structure of sequence from [Corynebacterium glutamicum] with ACT and NDP as [ligands]. Active as [Diaminopimelate dehydrogenase], with EC number [1.4.1.16]. Structure known Active Sites: ACE, N1 and N2. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of meso-diaminopimelic acid dehydrogenase from Corynebacterium glutamicum., Scapin G, Reddy SG, Blanchard JS, Biochemistry. 1996 Oct 22;35(42):13540-51. PMID:8885833
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