Inactivation and proteolysis of heat-sensitive adenylate kinase of Escherichia coli CR341 T28.

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Substitution of a serine residue for proline-87 reduces catalytic activity and increases susceptibility to proteolysis of Escherichia coli adenylate kinase.

Amino acid analysis, HPLC separation of trypsin digests, and sequence analysis showed that the thermosensitivity of the adenylate kinase (EC 2.7.4.3) from Escherichia coli K-12 strain CR341 T28 results from substitution of a serine residue for proline-87 in the wild-type enzyme. This mutation is accompanied by decreased affinity for nucleotide substrates and decreased catalysis. Circular dichro...

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Circular dichroism investigation of Escherichia coli adenylate kinase.

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Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli.

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1984

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)47210-3