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Kinetic parameters of human and rabbit liver D-fructose 1,6-diphosphate 1-phosphohydrolase determined at 25 and 37 degrees C.

作者信息

Dziewulska-Szwajkowska D, Skałecki K, Dzugaj A

机构信息

Department of Animal Physiology, University of Wrocław, Poland.

出版信息

Comp Biochem Physiol B. 1993 Jun;105(2):395-400. doi: 10.1016/0305-0491(93)90247-3.

DOI:10.1016/0305-0491(93)90247-3
PMID:8395376
Abstract
  1. Kinetic parameters of human and rabbit liver D-fructose 1,6-diphosphate 1-phosphohydrolase (EC 3.1.3.11) (FDP-ase) at 25 and 37 degrees C have been determined. 2. Km determined at 25 degrees C were 1.4 microM for human and 1.6 microM for rabbit enzyme; at 37 degrees C, corresponding values were 1.7 and 1.8 microM. 3. Both enzymes are allosterically inhibited by AMP. Respective values of I0.5 were 7.2 microM for human and 13.2 microM for rabbit at 25 degrees C, and 16.6 microM for human and 27.3 microM for rabbit at 37 degrees C. 4. Fructose 2,6-diphosphate, a potent regulator of gluconeogenesis, is more effective at 25 than at 37 degrees C. Ki determined at 25 degrees C was 0.07 microM for human and 0.035 microM for rabbit in comparison with 0.17 microM for human and 0.09 microM for rabbit at 37 degrees C. 5. Affinity of FDP-ase for magnesium is also dependent on temperature. For the human enzyme, Km at 25 degrees C was 226 microM and at 37 degrees C, 176 microM. For the rabbit enzyme, corresponding values were 256 and 240 microM. 6. Both enzymes are activated by KCl. Determined values of A0.5 were 91 mM for human, and 50 mM for rabbit enzyme at 25 degrees C, and 129 mM for human and 100 mM for rabbit enzyme at 37 degrees C.
摘要

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引用本文的文献

1
Kinetic properties of D-fructose-1,6-bisphosphate 1-phosphohydrolase isolated from human muscle.从人体肌肉中分离出的D-果糖-1,6-二磷酸1-磷酸水解酶的动力学特性。
Biochem J. 1995 Sep 15;310 ( Pt 3)(Pt 3):1029-35. doi: 10.1042/bj3101029.