Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli

Jochen Reinstein; Martin Brune; Alfred Wittinghofer

doi:10.1021/bi00413a020

Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli

Biochemistry ◽

10.1021/bi00413a020 ◽

1988 ◽

Vol 27 (13) ◽

pp. 4712-4720 ◽

Cited By ~ 88

Author(s):

Jochen Reinstein ◽

Martin Brune ◽

Alfred Wittinghofer

Keyword(s):

Escherichia Coli ◽

Adenylate Kinase ◽

Nucleotide Binding ◽

Binding Loop

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

Biochemistry ◽

10.1021/bi00484a014 ◽

1990 ◽

Vol 29 (32) ◽

pp. 7451-7459 ◽

Cited By ~ 71

Author(s):

Jochen Reinstein ◽

Ilme Schlichting ◽

Alfred Wittinghofer

Keyword(s):

Escherichia Coli ◽

Adenylate Kinase ◽

Phosphate Binding ◽

Binding Loop

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Nucleotide-binding properties of adenylate kinase from Escherichia coli: A molecular dynamics study in aqueous and vacuum environments

Journal of Computer-Aided Molecular Design ◽

10.1007/bf00125373 ◽

1994 ◽

Vol 8 (4) ◽

pp. 367-388 ◽

Cited By ~ 13

Author(s):

Petra Kern ◽

Roger M. Brunne ◽

Gerd Folkers

Keyword(s):

Escherichia Coli ◽

Molecular Dynamics ◽

Adenylate Kinase ◽

Nucleotide Binding ◽

Binding Properties

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Faculty Opinions recommendation of The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1027346.328490 ◽

2005 ◽

Author(s):

Miguel Valvano

Keyword(s):

Escherichia Coli ◽

Substrate Specificity ◽

Nucleotide Binding ◽

Binding Domain ◽

Atp Binding ◽

Nucleotide Binding Domain ◽

Terminal Domain ◽

Atp Binding Cassette Transporter ◽

Domain Protein ◽

O Antigens

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Identification and purification of an adenylate kinase-associated protein that influences the thermolability of adenylate kinase from a temperature-sensitive adk mutant of Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)44126-3 ◽

1983 ◽

Vol 258 (21) ◽

pp. 13370-13376

Author(s):

R J Huss ◽

M Glaser

Keyword(s):

Escherichia Coli ◽

Adenylate Kinase ◽

Temperature Sensitive

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The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase

Archives of Biochemistry and Biophysics ◽

10.1016/j.abb.2021.108899 ◽

2021 ◽

pp. 108899

Author(s):

Yunxiang Li ◽

Neydy A. Valdez ◽

Nelli Mnatsakanyan ◽

Joachim Weber

Keyword(s):

Escherichia Coli ◽

Atp Synthase ◽

Nucleotide Binding ◽

Binding Affinities

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Differentiation of nucleotide binding sites and role of metal ion in the adenylate kinase reaction by 31P NMR. Equilibria, interconversion rates, and NMR parameters of bound substrates

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38123-1 ◽

1978 ◽

Vol 253 (4) ◽

pp. 1149-1158 ◽

Cited By ~ 3

Author(s):

B.D. Nageswara Rao ◽

M. Cohn ◽

L. Noda

Keyword(s):

Binding Sites ◽

Adenylate Kinase ◽

Metal Ion ◽

31P Nmr ◽

Nucleotide Binding ◽

Nucleotide Binding Sites ◽

Nmr Parameters ◽

Kinase Reaction

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A mutation in Escherichia coli tRNA nucleotidyltransferase that affects only AMP incorporation is in a sequence often associated with nucleotide-binding proteins.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)66797-3 ◽

1986 ◽

Vol 261 (32) ◽

pp. 14875-14877

Author(s):

L Q Zhu ◽

H Cudny ◽

M P Deutscher

Keyword(s):

Escherichia Coli ◽

Binding Proteins ◽

Nucleotide Binding ◽

Nucleotide Binding Proteins

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Circular dichroism investigation of Escherichia coli adenylate kinase.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)61532-7 ◽

1987 ◽

Vol 262 (6) ◽

pp. 2502-2506

Author(s):

M. Monnot ◽

A.M. Gilles ◽

I.S. Girons ◽

S. Michelson ◽

O. Bârzu ◽

...

Keyword(s):

Escherichia Coli ◽

Circular Dichroism ◽

Adenylate Kinase ◽

Circular Dichroïsm

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Purification and Characterization of Adenylate Kinase as an Apparent Adenosine Triphosphate-dependent Inhibitor of Ribonuclease II in Escherichia coli

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)44180-x ◽

1973 ◽

Vol 248 (6) ◽

pp. 2014-2021

Author(s):

Randall K. Holmes ◽

Maxine F. Singer

Keyword(s):

Escherichia Coli ◽

Adenosine Triphosphate ◽

Adenylate Kinase ◽

Purification And Characterization

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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.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.83.16.5798 ◽

1986 ◽

Vol 83 (16) ◽

pp. 5798-5802 ◽

Cited By ~ 28

Author(s):

A. M. Gilles ◽

I. Saint-Girons ◽

M. Monnot ◽

S. Fermandjian ◽

S. Michelson ◽

...

Keyword(s):

Escherichia Coli ◽

Catalytic Activity ◽

Adenylate Kinase ◽

Serine Residue

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