Anomeric Specificity of the Alkaline Form of Fructose 1,6-Diphosphatase from Rabbit Liver

Anomeric Specificity of the Alkaline Form of Fructose 1,6-Diphosphatase from Rabbit Liver

The preferred configuration of the active substrate for rabbit liver fructose 1,6-diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose-1,6-P 2 . Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5-...

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Veröffentlicht in:The Journal of biological chemistry 1974-02, Vol.249 (3), p.930-931
Hauptverfasser: Benkovic, P A, Bullard, W P, De Maine, M, Fishbein, R, Schray, K J, Steffens, J J, Benkovic, S J
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Fructose-Bisphosphatase - metabolism
Fructosephosphates
Isomerism
Kinetics
Liver - enzymology
Molecular Conformation
Rabbits
Time Factors
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Zusammenfassung:The preferred configuration of the active substrate for rabbit liver fructose 1,6-diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose-1,6-P 2 . Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5- to 10-fold less than that for the α anomer.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)43020-2