1leh: Difference between revisions

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[[Image:1leh.gif|left|200px]]
{{Seed}}
[[Image:1leh.png|left|200px]]


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{{STRUCTURE_1leh|  PDB=1leh  |  SCENE=  }}  
{{STRUCTURE_1leh|  PDB=1leh  |  SCENE=  }}  


'''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS'''
===LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8591046}}


==About this Structure==
==About this Structure==
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[[Category: Turnbull, A P.]]
[[Category: Turnbull, A P.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:50:43 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 14:19:42 2008''

Revision as of 11:35, 2 July 2008

File:1leh.png

Template:STRUCTURE 1leh

LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS

Template:ABSTRACT PUBMED 8591046

About this Structure

1LEH is a Single protein structure of sequence from Lysinibacillus sphaericus. Full crystallographic information is available from OCA.

Reference

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

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