Pre-steady-state kinetic analysis of the three Escherichia coli pseudouridine synthases TruB, TruA, and RluA reveals uniformly slow catalysis

Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Steady state kinetic analysis of ATP hydrolysis.

10.1016/s0021-9258(19)68922-2 ◽

1981 ◽

Vol 256 (16) ◽

pp. 8845-8849 ◽

Cited By ~ 8

Author(s):

G.M. Weinstock ◽

K. McEntee ◽

I.R. Lehman

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Analysis ◽

Atp Hydrolysis ◽

Reca Protein ◽

Steady State Kinetic ◽

Nucleoside Triphosphates ◽

Hydrolysis Of ◽

Anabolic Ornithine Carbamoyltransferase of Escherichia coli and Catabolic Ornithine Carbamoyltransferase of Pseudomonas putida. Steady-State Kinetic Analysis

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1978.tb20914.x ◽

1978 ◽

Vol 89 (1) ◽

pp. 203-212 ◽

Cited By ~ 19

Author(s):

Brigitte WARGNIES ◽

Christiane LEGRAIN ◽

Victor STALON

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Pseudomonas Putida ◽

Kinetic Analysis ◽

Ornithine Carbamoyltransferase ◽

Steady State Kinetic ◽

Studies on translocation. 21. Steady state kinetic analysis of the mechanism of guanosine triphosphate hydrolysis catalyzed by Escherichia coli elongation factor G and the ribosome

Biochemistry ◽

10.1021/bi00666a003 ◽

1976 ◽

Vol 15 (21) ◽

pp. 4565-4569 ◽

Cited By ~ 26

Author(s):

Michael S. Rohrbach ◽

James W. Bodley

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Analysis ◽

Elongation Factor ◽

Guanosine Triphosphate ◽

Elongation Factor G ◽

Steady State Kinetic ◽

State Kinetic ◽

Factor G

Ornithine Carbamoyltransferase from Escherichia coli W. Purification, Structure and Steady-State Kinetic Analysis

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1976.tb10230.x ◽

1976 ◽

Vol 63 (1) ◽

pp. 289-301 ◽

Cited By ~ 64

Author(s):

Christiane LEGRAIN ◽

Victor STALON

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Analysis ◽

Ornithine Carbamoyltransferase ◽

Steady State Kinetic ◽

Insight into the activation mechanism of Escherichia coli octaprenyl pyrophosphate synthase derived from pre-steady-state kinetic analysis

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/s0167-4838(01)00283-7 ◽

2002 ◽

Vol 1594 (1) ◽

pp. 64-73 ◽

Cited By ~ 19

Author(s):

Jian-Jung Pan ◽

Tun-Hsun Kuo ◽

Yi-Kai Chen ◽

Lee-Wei Yang ◽

Po-Huang Liang

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Analysis ◽

Activation Mechanism ◽

Steady State Kinetic ◽

State Kinetic ◽

Insight Into

Fatty acid synthetase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from pigeon liver.

10.1016/s0021-9258(19)41660-8 ◽

1975 ◽

Vol 250 (7) ◽

pp. 2709-2717

Author(s):

SS Katiyar ◽

WW Cleland ◽

JW Porter

Keyword(s):

Steady State ◽

Fatty Acid ◽

Kinetic Analysis ◽

Fatty Acid Synthetase ◽

Steady State Kinetic ◽

State Kinetic ◽

Pigeon Liver

Mechanism of bovine liver S-adenosylhomocysteine hydrolase. Steady-state and pre-steady-state kinetic analysis.

10.1016/s0021-9258(18)54682-2 ◽

1991 ◽

Vol 266 (32) ◽

pp. 21616-21625

Author(s):

D.J. Porter ◽

F.L. Boyd

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Bovine Liver ◽

Adenosylhomocysteine Hydrolase ◽

Steady State Kinetic ◽

Acetyl coenzyme A carboxylase. Rapid purification of the chick liver enzyme and steady state kinetic analysis of the carboxylase-catalyzed reaction.

10.1016/s0021-9258(19)68288-8 ◽

1982 ◽

Vol 257 (2) ◽

pp. 924-929 ◽

Cited By ~ 3

Author(s):

N.B. Beaty ◽

M.D. Lane

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Liver Enzyme ◽

Coenzyme A ◽

Acetyl Coenzyme A ◽

Acetyl Coenzyme ◽

Steady State Kinetic ◽

Rapid Purification ◽

Acetyl Coenzyme A Carboxylase ◽

Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart

10.1016/s0021-9258(18)52325-5 ◽

1991 ◽

Vol 266 (3) ◽

pp. 1516-1525 ◽

Cited By ~ 6

Author(s):

Z Y Zhang ◽

R L VanEtten

Keyword(s):

Molecular Weight ◽

Steady State ◽

Kinetic Analysis ◽

Protein Phosphatase ◽

Low Molecular Weight ◽

Bovine Heart ◽

Steady State Kinetic ◽

Concurrent Reduction of Iodine and Oxidation of EDTA at the Active Site of Horseradish Peroxidase: Probing the Iodine Binding Site by Optical Difference Spectroscopy and Steady State Kinetic Analysis for the Formation of Active Enzyme-I+-EDTA Ternary Complex and for Iodine Reductase Activity

Biochemistry ◽

10.1021/bi00040a010 ◽

1995 ◽

Vol 34 (40) ◽

pp. 12998-13006 ◽

Cited By ~ 7

Author(s):

Subrata Adak ◽

Dipak Kr. Bhattacharyya ◽

Abhijit Mazumder ◽

Uday Bandyopadhyay ◽

Ranajit K. Banerjee

Keyword(s):

Steady State ◽

Horseradish Peroxidase ◽

Kinetic Analysis ◽

Active Site ◽

Ternary Complex ◽

Reductase Activity ◽

Difference Spectroscopy ◽

Steady State Kinetic ◽

State Kinetic ◽

Enzyme I