Document Detail

Effect of polar side chains at position 172 on thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus.
MedLine Citation:
PMID:  9237617     Owner:  NLM     Status:  MEDLINE    
To understand the role of the amino acid residue at position 172 in the conformational stability, four mutant enzymes of Thermus thermophilus 3-isopropylmalate dehydrogenase in which Ala172 was replaced with Asp, Glu, Asn, and Gln were prepared by site-directed mutagenesis. Three mutants were more stable than the wild-type enzyme. No significant change in catalytic properties was found in the mutant enzymes. The molecular modeling studies suggested that the enhanced thermostability of the mutant enzymes resulted from the formation of extra electrostatic interactions and/or improvement of hydrophobic packing of the interior core.
S Akanuma; C Qu; A Yamagishi; N Tanaka; T Oshima
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  410     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1997 Jun 
Date Detail:
Created Date:  1997-09-03     Completed Date:  1997-09-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  141-4     Citation Subset:  IM    
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.
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MeSH Terms
3-Isopropylmalate Dehydrogenase
Alcohol Oxidoreductases / chemistry*,  genetics
Enzyme Stability
Glutamic Acid
Molecular Structure
Mutagenesis, Site-Directed
Protein Conformation
Structure-Activity Relationship
Thermus thermophilus / enzymology*
Reg. No./Substance:
56-41-7/Alanine; 56-85-9/Glutamine; 56-86-0/Glutamic Acid; 7006-34-0/Asparagine; EC 1.1.-/Alcohol Oxidoreductases; EC Dehydrogenase

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