Document Detail


The cellulolytic system of Streptomyces reticuli.
MedLine Citation:
PMID:  8789339     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The bacterium Streptomyces reticuli produces an unusual mycelia-associated cellulase (Avicelase, Cel1) which is solely sufficient to degrade crystalline cellulose to cellobiose. The enzyme consists of a binding domain, one adjoining region with unknown function, and a catalytic domain belonging to the cellulase family E. During cultivation, the strain produces a specific protease which processes the Avicelase to a truncated enzyme lacking the binding domain. The cellulase synthesis is regulated by induction (Avicel) and repression (metabolizable sugars and glycerol).
Authors:
H Schrempf; S Walter
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  17     ISSN:  0141-8130     ISO Abbreviation:  Int. J. Biol. Macromol.     Publication Date:  1995 Dec 
Date Detail:
Created Date:  1996-10-21     Completed Date:  1996-10-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  353-5     Citation Subset:  IM    
Affiliation:
FB Biologie/Chemie, Universitat Osnabrück, Germany.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / genetics,  metabolism*
Base Sequence
Binding Sites
Cellobiose / metabolism
Cellulase / genetics,  metabolism*
Cellulose / metabolism*
Cellulose 1,4-beta-Cellobiosidase
Endopeptidases / metabolism
Enzyme Induction
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic
Genes, Bacterial
Molecular Sequence Data
Protein Processing, Post-Translational
Sequence Homology, Amino Acid
Streptomyces / enzymology*,  genetics
beta-Glucosidase / metabolism
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 16462-44-5/Cellobiose; 9004-34-6/Cellulose; EC 3.2.1.21/beta-Glucosidase; EC 3.2.1.4/Cellulase; EC 3.2.1.91/Cellulose 1,4-beta-Cellobiosidase; EC 3.4.-/Endopeptidases

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


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