Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity

Jesse Ybarra; A. R. S. Prasad; Jonathan S. Nishimura

doi:10.1021/bi00370a061

Chemical modification of tryptophan residues in Escherichia coli succinyl-CoA synthetase. Effect on structure and enzyme activity

Biochemistry ◽

10.1021/bi00370a061 ◽

1986 ◽

Vol 25 (22) ◽

pp. 7174-7178 ◽

Cited By ~ 7

Author(s):

Jesse Ybarra ◽

A. R. S. Prasad ◽

Jonathan S. Nishimura

Keyword(s):

Escherichia Coli ◽

Enzyme Activity ◽

Chemical Modification ◽

Tryptophan Residues ◽

Succinyl Coa Synthetase

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Chemical modification of Escherichia coli RNA polymerase by diethyl pyrocarbonate: evidence of histidine requirement for enzyme activity and intrinsic zinc binding

Biochemistry ◽

10.1021/bi00373a007 ◽

1986 ◽

Vol 25 (25) ◽

pp. 8167-8172 ◽

Cited By ~ 21

Author(s):

A. W. Abdulwajid ◽

Felicia Y. H. Wu

Keyword(s):

Escherichia Coli ◽

Enzyme Activity ◽

Chemical Modification ◽

Rna Polymerase ◽

Zinc Binding ◽

Diethyl Pyrocarbonate

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Reversible Chemical Modification of the Tryptophan Residues of Thioredoxin from Escherichia coli B

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1972.tb01795.x ◽

1972 ◽

Vol 26 (4) ◽

pp. 528-534 ◽

Cited By ~ 15

Author(s):

Arne Holmgren

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Tryptophan Residues ◽

Escherichia Coli B

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The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54766-9 ◽

1991 ◽

Vol 266 (31) ◽

pp. 20709-20713

Author(s):

L.J. Donald ◽

B.R. Crane ◽

D.H. Anderson ◽

H.W. Duckworth

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Citrate Synthase ◽

Site Directed Mutagenesis ◽

19F Nmr ◽

Directed Mutagenesis ◽

Allosteric Inhibition

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Adenosine 5'-O-(3-thio)triphosphate, a substrate and potent inhibitor of Escherichia coli succinyl-CoA synthetase. Additional evidence for a cooperative alternating-sites mechanism.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)42749-9 ◽

1984 ◽

Vol 259 (15) ◽

pp. 9642-9645 ◽

Cited By ~ 2

Author(s):

J S Nishimura ◽

T Mitchell

Keyword(s):

Escherichia Coli ◽

Potent Inhibitor ◽

Succinyl Coa Synthetase

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The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)34141-8 ◽

1994 ◽

Vol 269 (14) ◽

pp. 10883-10890 ◽

Cited By ~ 1

Author(s):

W.T. Wolodko ◽

M.E. Fraser ◽

M.N. James ◽

W.A. Bridger

Keyword(s):

Crystal Structure ◽

Escherichia Coli ◽

Succinyl Coa Synthetase

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Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein. Molecular topography of the enzyme.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)31702-2 ◽

1994 ◽

Vol 269 (50) ◽

pp. 31359-31371 ◽

Cited By ~ 1

Author(s):

W Bujalowski ◽

M M Klonowska

Keyword(s):

Escherichia Coli ◽

Binding Site ◽

Atp Binding ◽

Replicative Helicase ◽

Atp Binding Site ◽

Close Proximity ◽

Tryptophan Residues ◽

Helicase Dnab

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Structure-Function Studies of Escherichia coli Biotin Synthase via a Chemical Modification and Site-Directed Mutagenesis Approach

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a003028 ◽

2001 ◽

Vol 130 (5) ◽

pp. 627-635 ◽

Cited By ~ 7

Author(s):

L. Farh ◽

S.-Y. Hwang ◽

L. Steinrauf ◽

H.-J. Chiang ◽

D. Shiuan

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Structure Function ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Biotin Synthase

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Studies of Glutamate Dehydrogenase: Chemical Modification and Quantitative Determination of Tryptophan Residues

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1974.tb03415.x ◽

1974 ◽

Vol 43 (2) ◽

pp. 319-325 ◽

Cited By ~ 10

Author(s):

Veit Witzemann ◽

Rudolf Koberstein ◽

Horst Sund ◽

Ihab Rasched ◽

Hans Jornvall ◽

...

Keyword(s):

Chemical Modification ◽

Quantitative Determination ◽

Glutamate Dehydrogenase ◽

Tryptophan Residues

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Roles of tryptophan residues on the Rhizopus delemar lipase activity: Chemical modification in a water-olive oil emulsion

Biochimica et Biophysica Acta (BBA) - Enzymology ◽

10.1016/0005-2744(73)90421-x ◽

1973 ◽

Vol 327 (2) ◽

pp. 380-392 ◽

Cited By ~ 13

Author(s):

Hideo Chiba ◽

Masayoshi Hisatake ◽

Masaaki Hirose ◽

Etsuro Sugimoto

Keyword(s):

Chemical Modification ◽

Olive Oil ◽

Lipase Activity ◽

Rhizopus Delemar ◽

Oil Emulsion ◽

Tryptophan Residues ◽

Rhizopus Delemar Lipase

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Monoclonal antibodies to Escherichia coli F1-ATPase. Correlation of binding site location with interspecies cross-reactivity and effects on enzyme activity.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85099-8 ◽

1985 ◽

Vol 260 (19) ◽

pp. 10418-10425

Author(s):

S D Dunn ◽

R G Tozer ◽

D F Antczak ◽

L A Heppel

Keyword(s):

Escherichia Coli ◽

Enzyme Activity ◽

Monoclonal Antibodies ◽

Binding Site ◽

Cross Reactivity ◽

Site Location ◽

F1 Atpase

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