FEBS Letters | |
Characterization of yeast fructose‐2,6‐bisphosphate 6‐phosphatase | |
Purwin, Claudio1  Plankert, Uwe2  Holzer, Helmut2  | |
[1] Medizinische Universitätsklinik, Hugstetter Str. 55, 7800 Freiburg Germany;Biochemisches Institut, Universität Freiburg, Hermann-Herder-Str. 7, 7800 Freiburg, Germany | |
关键词: Yeast; Fructose-2; 6-bisphosphate 6-phosphatase; Kinetic parameter; Inhibitor; Fru(2; 6)P2; fructose 2; 6-bisphosphate; Fru(2; 6)P2 6-Pase; fructose-2; 6-bisphosphate-6-phosphatase; | |
DOI : 10.1016/0014-5793(88)80547-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
To obtain information on the biological significance of yeast fructose-2,6-bisphosphate 6-phosphatase, kinetic data of the purified enzyme [(1987) Eur. J. Biochem. 164, 27–30] have been measured. Maximal activity was found between Ph 6 and 7, the apparent Michaelis constant with fructose 2,6-bisphosphate was 7.2 μM at Ph 6.0 and 79 μm at Ph 7.0. Concentrations required for 50% inhibition of the enzyme at Ph 6.0 were 8 μm Fru2P, 45 μm G1c6P, 80 μm Fru6P and 200 μm inorganic phosphate. The known intracellular steady-state level of about 10 μm fructose 2,6-bisphosphate in the presence of glucose is likely to be the result of a balance between the rapid synthesis of fructose 2,6-bisphosphate catalyzed by 6-phosphofructose 2-kinase and a fructose 2,6-bisphosphate degrading activity. The biological function of fructose-2,6-bisphosphate 6-phosphatase with an apparent Michaelis constant between 7 and 79 μm fructose 2,6-bisphosphate at Ph 6–7 is therefore suggested to participate in the maintenance of a steady-state level of fructose 2,6-bisphosphate in a concentration range that fits well with the Michaelis constant of the enzyme.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020291199ZK.pdf | 337KB | download |