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

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 ◽

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

RNA ◽

10.1261/rna.2905811 ◽

2011 ◽

Vol 17 (12) ◽

pp. 2074-2084 ◽

Cited By ~ 18

Author(s):

J. R. Wright ◽

L. C. Keffer-Wilkes ◽

S. R. Dobing ◽

U. Kothe

Keyword(s):

Escherichia Coli ◽

Steady State ◽

Kinetic Analysis ◽

Steady State Kinetic ◽

Pseudouridine Synthases ◽

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 ◽

Promotion mechanism of CeO2addition on the low temperature SCR reaction over MnOx/TiO2: a new insight from the kinetic study

RSC Advances ◽

10.1039/c5ra01767j ◽

2015 ◽

Vol 5 (35) ◽

pp. 27785-27793 ◽

Cited By ~ 17

Author(s):

Shangchao Xiong ◽

Yong Liao ◽

Hao Dang ◽

Feihong Qi ◽

Shijian Yang

Keyword(s):

Steady State ◽

Low Temperature ◽

Kinetic Study ◽

Kinetic Analysis ◽

Steady State Kinetic ◽

Low Temperature Scr ◽

Promotion Mechanism ◽

State Kinetic ◽

Insight Into

A new insight into CeO2addition on the SCR reaction over MnOx/TiO2was drawn according to steady-state kinetic analysis.

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 ◽