Acetate kinase: a triple-displacement enzyme. | Zendy

Leonard B. Spector | Zendy

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Acetate kinase: a triple-displacement enzyme.

Author(s) -

Leonard B. Spector

Publication year - 1980

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.77.5.2626

Subject(s) - acetate kinase , chemistry , steric effects , kinase , phosphotransferase , enzyme , stereochemistry , phosphorylation , biochemistry , escherichia coli , gene

Facts relating to the mechanism of phosphoryl transfer by acetate kinase (ATP:acetate phosphotransferase, EC 2.7.2.1) are reviewed. They point to the existence of at least one experimentally established phosphoenzyme (E-P) intermediate on the reaction pathway. Sterically, the phosphoryl transfer occurs with a net inversion of the configuration of the phosphorus atom. These facts are best in accord with a triple-displacement mode of action for acetate kinase, with two E-P intermediates and three steric inversions on phosphorus. It follows that a second E-P for acetate kinase must exist.

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