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An enzyme synthesizing fructose 2,6‐bisphosphate occurs in leaves and is regulated by metabolite effectors
Author(s) -
Cséke Csaba,
Buchanan Bob B.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80226-9
Subject(s) - biochemistry , fructose , metabolite , glycolysis , enzyme , effector , fructose 2,6 bisphosphate , fructose 1,6 bisphosphatase , pentose phosphate pathway , phosphoenolpyruvate carboxykinase , biology , phosphorylation , enzyme activator , chemistry , phosphofructokinase
An enzyme catalyzing the ATP and fructose 6‐phosphate‐dependent synthesis of fructose 2,6‐bisphosphate, a regulator of glycolysis and gluconeogenesis, has been identified and partially purified from plants, specifically the cytoplasmic fraction of spinach leaf parenchyma cells. The enzyme, designated fructose 6‐phosphate, 2‐kinase, showed no response to a protein phosphorylation system known to inhibit the corresponding enzyme in mammalian cells, but it responded strikingly to metabolite effectors (P i , an activator/PGA, an inhibitor) through changes in substrate affinity and maximal velocity. The observed pattern of regulation suggests a role for chloroplasts in controlling cytoplasmic carbon processing.