Pre-steady-state kinetic analysis of damage recognition by human single-strand selective monofunctional uracil-DNA glycosylase SMUG1

Alexandra A. Kuznetsova; Danila A. Iakovlev; Inna V. Misovets; Alexander A. Ishchenko; Murat K. Saparbaev; Nikita A. Kuznetsov; Olga S. Fedorova

doi:10.1039/c7mb00457e

Pre-steady-state kinetic analysis of damage recognition by human single-strand selective monofunctional uracil-DNA glycosylase SMUG1

Molecular BioSystems ◽

10.1039/c7mb00457e ◽

2017 ◽

Vol 13 (12) ◽

pp. 2638-2649 ◽

Cited By ~ 13

Author(s):

Alexandra A. Kuznetsova ◽

Danila A. Iakovlev ◽

Inna V. Misovets ◽

Alexander A. Ishchenko ◽

Murat K. Saparbaev ◽

...

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Kinetic Data ◽

Single Strand ◽

Dna Glycosylase ◽

Uracil Dna Glycosylase ◽

Damage Recognition ◽

Steady State Kinetic ◽

State Kinetic

The mechanism of damaged base recognition by hSMUG1 was elucidated using comparison of pre-steady state kinetic data obtained by Trp and aPu fluorescence and FRET detection.

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

Journal of Biological Chemistry ◽

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

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

Journal of Biological Chemistry ◽

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 ◽

State Kinetic

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

Journal of Biological Chemistry ◽

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 ◽

State Kinetic

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

Journal of Biological Chemistry ◽

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 ◽

State Kinetic

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

Journal of Biological Chemistry ◽

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 ◽

State Kinetic

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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

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Deuterium isotope effects in the fermentation of hexoses to ethanol by Saccharomyces cerevisiae. II. A steady-state kinetic analysis of the methyl group of ethanol in an isotopic mirror fermentation experiment

Biochemistry ◽

10.1021/bi00850a031 ◽

1968 ◽

Vol 7 (10) ◽

pp. 3537-3546 ◽

Cited By ~ 8

Author(s):

Wolfgang K. Saur ◽

Daniel T. Peterson ◽

E. A. Halevi ◽

Henry L. Crespi ◽

Joseph J. Katz

Keyword(s):

Saccharomyces Cerevisiae ◽

Steady State ◽

Kinetic Analysis ◽

Isotope Effects ◽

Methyl Group ◽

Steady State Kinetic ◽

Deuterium Isotope Effects ◽

State Kinetic

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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 ◽

State Kinetic

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Steady-State Kinetic Analysis of Chemiosmotic Proton Circuits in Microorganisms*

Physiological Models in Microbiology ◽

10.1201/9781351075657-3 ◽

2018 ◽

pp. 49-74

Author(s):

Dale Sanders

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Steady State Kinetic ◽

State Kinetic

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DNA Polymerase β: Pre-Steady-State Kinetic Analysis and Roles of Arginine-283 in Catalysis and Fidelity†

Biochemistry ◽

10.1021/bi9527202 ◽

1996 ◽

Vol 35 (22) ◽

pp. 7041-7050 ◽

Cited By ~ 77

Author(s):

Brian G. Werneburg ◽

Jinwoo Ahn ◽

Xuejun Zhong ◽

Robert J. Hondal ◽

Vadim S. Kraynov ◽

...

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Dna Polymerase ◽

Dna Polymerase Β ◽

Steady State Kinetic ◽

State Kinetic

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