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Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coli.

Biochemistry - 14 Aug 1990

Reinstein J, Schlichting I, Wittinghofer A

Abstract excerpt

Amino acids in the phosphate binding loop of adenylate kinase of Escherichia coli were mutated by site-directed mutagenesis. The mutant proteins with a Pro-9----Gly (P9G) and with a Lys-13----Gln (K13Q) exchange were overexpressed and purified. They were characterized by steady-state kinetics, fluorescence binding, and structural studies, together with the phosphate binding loop mutants P9L and G10V prepared...

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PMID: 2223776
DOI: 10.1021/bi00484a014

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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