Document Detail


Exploring amino acids responsible for the temperature profile of glycoside hydrolase family 45 endoglucanase EGL3 from Humicola grisea.
MedLine Citation:
PMID:  16960377     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
EGL3 and RCE1 are glycoside hydrolase family 45 endoglucanases isolated from Humicola grisea and Rhizopus oryzae respectively. The amino acid sequences of the two endoglucanases are homologous; on the other hand, the optimum temperature of EGL3 is higher than that of RCE1. In this study, four chimeric endoglucanases, named ER1, ER2, ER3 and ER4, in which one of four sequential amino acid regions of the EGL3 catalytic domain (CAD) was replaced by the corresponding RCE1 amino acids, were constructed to explore the region responsible for the EGL3 temperature profile. Then their temperature profiles were compared with that of the recombinant EGL3. Replacement of the N-terminal region of EGL3 with that of RCE1 caused the EGL3 temperature profile to shift to a lower temperature. These results suggest that the N-terminal amino acids of the EGL3 are responsible for the EGL3 temperature profile.
Authors:
Koichiro Murashima; Atsushi Shimonaka; Tomoko Nishimura; Yuko Baba; Jinichiro Koga; Hidetoshi Kubota; Toshiaki Kono
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Publication Detail:
Type:  Comparative Study; Journal Article     Date:  2006-09-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  70     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-09-27     Completed Date:  2006-11-21     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  2205-12     Citation Subset:  IM    
Affiliation:
Food and Health R & D Laboratories, Meiji Seika Kaisha, Ltd., Sakado-shi, Saitama, Japan. koichiro_murashima@meiji.co.jp
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / chemistry*,  genetics,  metabolism
Ascomycota / enzymology*,  genetics
Carboxymethylcellulose / metabolism
Cellulase / chemistry*,  genetics,  metabolism
DNA, Fungal / chemistry,  genetics
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Hydrogen-Ion Concentration
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutant Chimeric Proteins / genetics,  metabolism
Protein Conformation
Sequence Alignment
Structure-Activity Relationship
Temperature
Chemical
Reg. No./Substance:
0/Amino Acids; 0/DNA, Fungal; 0/Mutant Chimeric Proteins; 9004-32-4/Carboxymethylcellulose; EC 3.2.1.4/Cellulase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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