Cellulose 1,4-beta-cellobiosidase
Cellulose 1,4-beta-cellobiosidase (non-reducing end) (EC 3.2.1.91, 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) is an enzyme with systematic name 4-beta-D-glucan cellobiohydrolase (non-reducing end).[1][2][3][4] This enzyme catalyses the following chemical reaction
- Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing [cellobiose] from the non-reducing ends of the chains
References
- ↑ Berghem, L.E.R. and Pettersson, L.G. (1973). "The mechanism of enzymatic cellulose degradation. Purification of a cellulolytic enzyme from Trichoderma viride active on highly ordered cellulose". Eur. J. Biochem. 37: 21–30. doi:10.1111/j.1432-1033.1973.tb02952.x. PMID 4738092.
- ↑ Eriksson, K.E. and Pettersson, B. (1975). "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-β-glucanase". Eur. J. Biochem. 51: 213–218. doi:10.1111/j.1432-1033.1975.tb03921.x. PMID 235428.
- ↑ Halliwell, G., Griffin, M. and Vincent, R. (1972). "The role of component C1 in cellulolytic systems". Biochem. J. 127: 43P–43P. PMID 5076675.
- ↑ Zverlov V., Velikodvorskaya G., Schwarz W., Bronnenmeier K., Kellermann J., Staudenbauer W. (1998) Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA. J. Bacteriol. 180, 3091-3099.
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