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| - | [[Image:1leh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1leh| PDB=1leh | SCENE= }} | | {{STRUCTURE_1leh| PDB=1leh | SCENE= }} |
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| - | '''LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS'''
| + | ===LEUCINE DEHYDROGENASE FROM BACILLUS SPHAERICUS=== |
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| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8591046}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8591046 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8591046}} |
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| | ==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
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
Page seeded by OCA on Wed Jul 2 14:19:42 2008
