1leh

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

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucine_dehydrogenase Leucine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.9 1.4.1.9] </span></td></tr>

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

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== Publication Abstract from PubMed ==

BACKGROUND: Glutamate, phenylalanine and leucine dehydrogenases catalyze the NAD(P)(+)-linked oxidative deamination of L-amino acids to the corresponding 2-oxoacids, and sequence homology between these enzymes clearly indicates the existence of an enzyme superfamily related by divergent evolution. We have undertaken structural studies on a number of members of this family in order to investigate the molecular basis of their differential amino acid specificity. RESULTS: We have solved the X-ray structure of the leucine dehydrogenase from Bacillus sphaericus to a resolution of 2.2 A. Each subunit of this octameric enzyme contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. CONCLUSIONS: Comparison of the structure of leucine dehydrogenase with a hexameric glutamate dehydrogenase has shown that these two enzymes share a related fold and possess a similar catalytic chemistry. A mechanism for the basis of the differential amino acid specificity between these enzymes involves point mutations in the amino acid side-chain specificity pocket and subtle changes in the shape of this pocket caused by the differences in quaternary structure.

A role for quaternary structure in the substrate specificity of leucine dehydrogenase.,Baker PJ, Turnbull AP, Sedelnikova SE, Stillman TJ, Rice DW Structure. 1995 Jul 15;3(7):693-705. PMID:8591046<ref>PMID:8591046</ref>

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

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== References ==

<references/>

[[Category: Leucine dehydrogenase]]

[[Category: Baker, P J]]

[[Category: Rice, D W]]

[[Category: Sedelnikova, S E]]

[[Category: Stillman, T J]]

[[Category: Turnbull, A P]]

[[Category: Oxidoreductase]]