| 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 |
Abstract/OtherAbstract:
|
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. |
| | |
Authors:
|
S Akanuma; C Qu; A Yamagishi; N Tanaka; T Oshima |
Related Documents
:
|
14592457 - Critical residues for the coenzyme specificity of nad+-dependent 15-hydroxyprostaglandi... 3140237 - Tyrosinases of murine melanocytes with mutations at the albino locus. 1831757 - Complementation of soluble phosphofructokinase activity in yeast mutants. 18636597 - Metabolic and physiological studies of corynebacterium glutamicum mutants. 3792297 - New ideas about enzyme reactions. 6118977 - Species variations in the renal and hepatic conjugation of 3-phenoxybenzoic acid with g... |
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 |
Affiliation:
|
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan. akanuma@ls.toyaku.ac.jp |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
3-Isopropylmalate Dehydrogenase Alanine Alcohol Oxidoreductases / chemistry*, genetics Asparagine Enzyme Stability Glutamic Acid Glutamine Heating Molecular Structure Mutagenesis, Site-Directed Protein Conformation Structure-Activity Relationship Thermus thermophilus / enzymology* |
| Chemical | |
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 1.1.1.85/3-Isopropylmalate Dehydrogenase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Phosphatidylinositol 4,5-bisphosphate stimulates phosphorylation of the adaptor protein Shc by c-Src...
Next Document: HIV-1 protein Vpr causes gross mitochondrial dysfunction in the yeast Saccharomyces cerevisiae.