1bg6

<table><tr><td colspan='2'>[[1bg6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Artsc Artsc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BG6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BG6 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ODH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79670 ARTSC])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg6 OCA], [http://pdbe.org/1bg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bg6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bg6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/ODH_ARTSC ODH_ARTSC]] In the forward direction acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. In the reverse direction, the enzyme also acts on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.

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== Publication Abstract from PubMed ==

Opine dehydrogenases catalyze the NAD(P)H-dependent reversible reaction to form opines that contain two asymmetric centers exhibiting either (L,L) or (D,L) stereochemistry. The first structure of a (D,L) superfamily member, N-(1-D-carboxylethyl)-L-norvaline dehydrogenase (CENDH) from Arthrobacter sp. strain 1C, has been determined at 1.8 A resolution and the location of the bound nucleotide coenzyme has been identified. Six conserved residues cluster in the cleft between the enzyme's two domains, close to the nucleotide binding site, and are presumed to define the enzyme's catalytic machinery. Conservation of a His-Asp pair as part of this cluster suggests that the enzyme mechanism is related to the 2-hydroxy acid dehydrogenases. The pattern of sequence conservation and substitution between members of this enzyme family has permitted the tentative location of the residues that define their differential substrate specificities.

Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase.,Britton KL, Asano Y, Rice DW Nat Struct Biol. 1998 Jul;5(7):593-601. PMID:9665174<ref>PMID:9665174</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Artsc]]

[[Category: Asano, Y]]

[[Category: Britton, K L]]

[[Category: Rice, D W]]

[[Category: Oxidoreductase]]