Ostrich fructose-1,6-bisphosphatase: Kinetic characterization of the liver isoenzyme |
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Institution: | 1. Department of Biochemistry, University of Zululand, Private Bag X1001, Kwa-Dlangezwa 3886 Republic of South Africa |
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Abstract: | - 1.1. Purified ostrich (Struthio camelus) liver fructose-1,6-bisphosphatase exhibited an absolute requirement for Mg2+.
- 2.2. The enzyme catalyzed the hydrolysis of fructose-1,6-bisphosphate, sedoheptulose-l,7-bisphosphate and ribulose-l,5-bisphosphate.
- 3.3. S0.5 for substrate was 1.4 μM.
- 4.4. AMP was a potent non-competitive inhibitor with respect to substrate (Ki of 25 μM).
- 5.5. Fructose-2,6-bisphosphate was a potent competitive inhibitor of the enzyme (Ki of 4.8 μM).
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