KEGG   ENZYME: 3.2.1.91Help
Entry
EC 3.2.1.91                 Enzyme                                 

Name
cellulose 1,4-beta-cellobiosidase (non-reducing end);
exo-cellobiohydrolase;
beta-1,4-glucan cellobiohydrolase;
beta-1,4-glucan cellobiosylhydrolase;
1,4-beta-glucan cellobiosidase;
exoglucanase;
avicelase;
CBH 1;
C1 cellulase;
cellobiohydrolase I;
cellobiohydrolase;
exo-beta-1,4-glucan cellobiohydrolase;
1,4-beta-D-glucan cellobiohydrolase;
cellobiosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
4-beta-D-glucan cellobiohydrolase (non-reducing end)
Reaction(IUBMB)
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
Reaction(KEGG)
(other) R02886 R06200(G)
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History
EC 3.2.1.91 created 1976, modified 2011
Pathway
Starch and sucrose metabolism
Metabolic pathways
Orthology
K01225  
cellulose 1,4-beta-cellobiosidase
Genes
ANG: 
ANI_1_1574014(An01g11660)
RSO: 
RS03897(RSp0583)
CTH: 
TIT: 
TMT: 
CSC: 
TTM: 
TFU: 
STP: 
Taxonomy
Reference
1  [PMID:4738092]
  Authors
Berghem LE, Pettersson LG.
  Title
The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose.
  Journal
Eur. J. Biochem. 37 (1973) 21-30.
  Organism
Trichoderma viride
Reference
2  [PMID:235428]
  Authors
Eriksson KE, Pettersson B.
  Title
Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cellulose. 3. Purification and physico-chemical characterization of an exo-1,4-beta-glucanase.
  Journal
Eur. J. Biochem. 51 (1975) 213-8.
  Organism
Sporotrichum pulverulentum
Reference
3  [PMID:5076675]
  Authors
Halliwell G, Griffin M, Vincent R.
  Title
The role of component C 1  in cellulolytic systems.
  Journal
Biochem. J. 127 (1972) 43P.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37329-65-0

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