| Literature DB >> 2825652 |
M Kretschmer1, W Schellenberger, A Otto, R Kessler, E Hofmann.
Abstract
Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.Entities:
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Year: 1987 PMID: 2825652 PMCID: PMC1148341 DOI: 10.1042/bj2460755
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857