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

Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

4-beta-D-glucan cellobiohydrolase (non-reducing end)

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains

(other) R02886 R06200(G)

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

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

3  [PMID:5076675]

Halliwell G, Griffin M, Vincent R.

The role of component C 1  in cellulolytic systems.

Biochem. J. 127 (1972) 43P.