Document Detail

Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum.
MedLine Citation:
PMID:  20229062     Owner:  NLM     Status:  MEDLINE    
To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10-25th and C-terminal 1-9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1-7th and C-terminal 1-3rd residues were not necessary to maintain enzymatic activity.
Dong Niu; Xu-Xia Zhou; Tao-Yan Yuan; Zhi-Wei Lin; Hui Ruan; Wei-Fen Li
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-03-13
Journal Detail:
Title:  Biotechnology letters     Volume:  32     ISSN:  1573-6776     ISO Abbreviation:  Biotechnol. Lett.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-06-17     Completed Date:  2010-09-15     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  963-7     Citation Subset:  IM    
College of Animal Sciences, Zhejiang University, 310029, Hangzhou, China.
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MeSH Terms
Bacterial Proteins / chemistry*,  genetics,  metabolism*
Catalytic Domain
Clostridium thermocellum / enzymology*
Enzyme Stability
Escherichia coli / genetics
Gene Expression
Glycoside Hydrolases / chemistry*,  genetics,  metabolism*
Mutant Proteins / chemistry,  genetics,  metabolism
Protein Stability
Sequence Deletion
Reg. No./Substance:
0/Bacterial Proteins; 0/Mutant Proteins; EC 3.2.1.-/Glycoside Hydrolases; EC

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

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