Abstract A nonspecific cellobiose phosphorylase from Clostridium thermocellum, which has been purified over 100-fold, is active on 10 different glucosyl acceptors, d-glucose, 2-deoxyglucose, 6-deoxyglucose, d-glucosamine, d-mannose, d-altrose, l-galactose, l-fucose, d-arabinose, and d-xylose. Following electrophoresis on polyacrylamide gels, the activity with various acceptors occurs at the location of the major protein component, indicating that a single enzyme catalyzes these reactions. The pH optimum is about 6.5 with d-xylose as an acceptor. The relative Vmax and apparent Km values are 202 and 9.2 mm for 6-deoxyglucose, 100 and 35 mm for d-xylose, 53 and 73 mm for 2-deoxyglucose, 31 and 9.5 mm for d-glucosamine, 22 and 85 mm for d-mannose, 9 and 240 mm for d-arabinose and 8 and 160 mm for l-fucose. The Ki for d-glucose is 1.2 mm. The apparent Km value is 7.3 mm for cellobiose and 2.9 mm for Pi.
Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum.
Published 1968 in Journal of Biological Chemistry
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- Publication year
1968
- Venue
Journal of Biological Chemistry
- Publication date
1968-06-10
- Fields of study
Biology, Medicine, Chemistry
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Semantic Scholar, PubMed
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