KEGG   ENZYME: 3.2.1.91Help
Entry
EC 3.2.1.91                 Enzyme                                 

Name cellulose 1,4-beta-cellobiosidase;
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
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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Pathway ec00500  Starch and sucrose metabolism
Orthology K01225  cellulose 1,4-beta-cellobiosidase
Genes ANG: An01g11660(cbhB)
RSO: RS03897(RSp0583)
CTH: Cthe_0040 Cthe_0071 Cthe_1235
CSC: Csac_1078 Csac_1079 Csac_2410
MUL: MUL_0371
TFU: Tfu_0620 Tfu_1627 Tfu_1959
STP: Strop_2951
Taxonomy
Reference
  Authors
  Title


  Journal
  Organism
1  [PMID:4738092]
Berghem LE, Pettersson LG.
The mechanism of enzymatic cellulose degradation. Purification of a
cellulolytic enzyme from Trichoderma viride active on highly ordered
cellulose.
Eur. J. Biochem. 37 (1973) 21-30.
Trichoderma viride
Reference
  Authors
  Title



  Journal
  Organism
2  [PMID:235428]
Eriksson KE, Pettersson B.
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.
Eur. J. Biochem. 51 (1975) 213-8.
Sporotrichum pulverulentum
Reference
  Authors
  Title
  Journal
3  [PMID:5076675]
Halliwell G, Griffin M, Vincent R.
The role of component C 1  in cellulolytic systems.
Biochem. J. 127 (1972) 43P.
Other DBs ExplorEnz - The Enzyme Database: 3.2.1.91
IUBMB Enzyme Nomenclature: 3.2.1.91
ExPASy - ENZYME nomenclature database: 3.2.1.91
BRENDA, the Enzyme Database: 3.2.1.91
CAS: 37329-65-0

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