Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme

F. W. Dahlquist; D. L. Purich

doi:10.1021/bi00680a028

Regulation of Escherichia coli glutamine synthetase. Evidence for the action of some feedback modifiers at the active site of the unadenylylated enzyme

Biochemistry ◽

10.1021/bi00680a028 ◽

1975 ◽

Vol 14 (9) ◽

pp. 1980-1989 ◽

Cited By ~ 16

Author(s):

F. W. Dahlquist ◽

D. L. Purich

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Active Site

Download Full-text

Active site ligand stabilization of quaternary structures of glutamine synthetase from Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)34563-0 ◽

1982 ◽

Vol 257 (12) ◽

pp. 7246-7251 ◽

Cited By ~ 5

Author(s):

M R Maurizi ◽

A Ginsburg

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Active Site ◽

Ligand Stabilization ◽

Quaternary Structures

Download Full-text

Distances between active site probes in glutamine synthetase from Escherichia coli: fluorescence energy transfer in free and in stacked dodecamers

Biochemistry ◽

10.1021/bi00349a021 ◽

1986 ◽

Vol 25 (1) ◽

pp. 141-151 ◽

Cited By ~ 8

Author(s):

Michael R. Maurizi ◽

Philip G. Kasprzyk ◽

Ann Ginsburg

Keyword(s):

Escherichia Coli ◽

Energy Transfer ◽

Glutamine Synthetase ◽

Active Site ◽

Fluorescence Energy Transfer ◽

Fluorescence Energy

Download Full-text

Thermodynamic effects of active-site ligands on the reversible, partial unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric studies

Biochemistry ◽

10.1021/bi00163a006 ◽

1992 ◽

Vol 31 (48) ◽

pp. 11991-12000 ◽

Cited By ~ 11

Author(s):

Michal Zolkiewski ◽

Ann Ginsburg

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Active Site ◽

Partial Unfolding ◽

Thermodynamic Effects ◽

Calorimetric Studies

Download Full-text

Kinetic and mutagenic studies of the role of the active site residues Asp-50 and Glu-327 of Escherichia coli glutamine synthetase

Biochemistry ◽

10.1021/bi00169a008 ◽

1994 ◽

Vol 33 (3) ◽

pp. 682-686 ◽

Cited By ~ 30

Author(s):

Murtaza Alibhai ◽

Joseph J. Villafranca

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Active Site ◽

Active Site Residues

Download Full-text

Oxidative modification of Escherichia coli glutamine synthetase. Decreases in the thermodynamic stability of protein structure and specific changes in the active site conformation.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)46028-0 ◽

1992 ◽

Vol 267 (3) ◽

pp. 1872-1880

Author(s):

M T Fisher ◽

E R Stadtman

Keyword(s):

Escherichia Coli ◽

Protein Structure ◽

Glutamine Synthetase ◽

Thermodynamic Stability ◽

Active Site ◽

Oxidative Modification ◽

Active Site Conformation

Download Full-text

Active-Site Ligand Binding and Subunit Interactions in Glutamine Synthetase from Escherichia coli

Modulation by Molecular Interactions - Current Topics in Cellular Regulation - Current Topics in Cellular Regulation ◽

10.1016/b978-0-12-152826-3.50022-x ◽

1985 ◽

pp. 191-206 ◽

Cited By ~ 6

Author(s):

Michael R. Maurizi ◽

Ann Ginsburg

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Ligand Binding ◽

Active Site ◽

Subunit Interactions

Download Full-text

Thermodynamics of active-site ligand binding to Escherichia coli glutamine synthetase

Biochemistry ◽

10.1021/bi00393a007 ◽

1987 ◽

Vol 26 (19) ◽

pp. 5989-5996 ◽

Cited By ~ 11

Author(s):

Ann Ginsburg ◽

Eileen G. Gorman ◽

Sue H. Neece ◽

Marlana B. Blackburn

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Ligand Binding ◽

Active Site

Download Full-text

Affinity labeling of the active site of Escherichia coli glutamine synthetase by 5'-p-fluorosulfonylbenzoyladenosine.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70061-1 ◽

1981 ◽

Vol 256 (2) ◽

pp. 882-886

Author(s):

W.B. Foster ◽

M.J. Griffith ◽

H.S. Kingdon

Keyword(s):

Escherichia Coli ◽

Glutamine Synthetase ◽

Active Site ◽

Affinity Labeling

Download Full-text

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

European Journal of Biochemistry ◽

10.1046/j.1432-1033.2001.02035.x ◽

2001 ◽

Vol 268 (6) ◽

pp. 1640-1645

Author(s):

Annelise Matharu ◽

Hideyuki Hayashi ◽

Hiroyuki Kagamiyama ◽

Bruno Maras ◽

Robert A. John

Keyword(s):

Escherichia Coli ◽

Active Site ◽

Aspartate Aminotransferase ◽

Substrate Binding ◽

Arginine Residues

Download Full-text

Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype

Nucleic Acids Research ◽

10.1093/nar/gkm926 ◽

2007 ◽

Vol 36 (1) ◽

pp. 41-50 ◽

Cited By ~ 29

Author(s):

L. M. S. Elles ◽

O. C. Uhlenbeck

Keyword(s):

Escherichia Coli ◽

Active Site ◽

Slow Growth ◽

Helicase Activity ◽

Growth Phenotype ◽

Arginine Finger ◽

Slow Growth Phenotype

Download Full-text