The mechanism of the pyruvate, phosphate dikinase reaction.
نویسندگان
چکیده
منابع مشابه
The Pyruvate-Phosphate Dikinase Reaction
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 ...
متن کاملSwiveling domain mechanism in pyruvate phosphate dikinase.
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...
متن کاملThe pyruvate-phosphate dikinase reaction. The fate of phosphate and the equilibrium.
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 ...
متن کاملCrystalline Pyruvate, Phosphate Dikinase from Bacteroides symbiosus
Pyruvate, phosphate dikinase was purified and crystallized from Bacteroides symbiosus. The function of histidyl and cysteinyl residues of the enzyme were investigated by chemical modification with diethylpyrocarbonate and bromopyruvate. Diethylpyrocarbonate rapidly inactivated the enzyme by combination with histidyl residues. The modified enzyme loses the ability to form phosphoryl enzyme and e...
متن کاملPyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis.
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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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1968
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.61.4.1448