Pyruvate, phosphate dikinase. Metal cation requirements and inactivation of the enzyme by sulfhydryl agents
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چکیده
منابع مشابه
Pyruvate, phosphate dikinase. Metal cation requirements and inactivation of the enzyme by sulfhydryl agents.
The metal cation requirements of pyruvate, phosphate dikinase from Bacteroides symbiosus have been examined with respect to both the overall reaction and the three partial reactions. The overall reaction and all three partial reactions require a divalent cation (M$‘, Mn’+, or Co’+). Although Mn2+ and Co’+ are very effective activators at low concentrations in two of the three partial reactions,...
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was obtained from Bacteroides symbiosus cell extracts and was purified from interfering enzyme activities. It was strongly stimulated by ammonium ion. In this respect and in other physical properties the bacterial enzyme differed from that previously obtained from Entamoeba histolytica. In a complete reaction system the enzyme transferred label from orthophosphate to pyrophosphate and to the y ...
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Crystals of pyruvate phosphate dikinase in complex with a substrate analogue inhibitor, phosphonopyruvate (K(i) = 3 microM), have been obtained in the presence of Mg(2+). The structure has been determined and refined at 2.2 A resolution, revealing that the Mg(2+)-bound phosphonopyruvate binds in the alpha/beta-barrel's central channel, at the C-termini of the beta-strands. The mode of binding r...
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Pyruvate phosphate dikinase (PPDK) catalyzes the reversible conversion of phosphoenolpyruvate (PEP), AMP, and Pi to pyruvate and ATP. The enzyme contains two remotely located reaction centers: the nucleotide partial reaction takes place at the N-terminal domain, and the PEP/pyruvate partial reaction takes place at the C-terminal domain. A central domain, tethered to the N- and C-terminal domain...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34421-6