Multiple Forms of Xylose Reductase inCandida intermedia:  Comparison of Their Functional Properties Using Quantitative Structure−Activity Relationships, Steady-State Kinetic Analysis, and pH Studies

Bernd Nidetzky; Kaspar Brüggler; Regina Kratzer; Peter Mayr

doi:10.1021/jf034426j

Multiple Forms of Xylose Reductase inCandida intermedia: Comparison of Their Functional Properties Using Quantitative Structure−Activity Relationships, Steady-State Kinetic Analysis, and pH Studies

Journal of Agricultural and Food Chemistry ◽

10.1021/jf034426j ◽

2003 ◽

Vol 51 (27) ◽

pp. 7930-7935 ◽

Cited By ~ 16

Author(s):

Bernd Nidetzky ◽

Kaspar Brüggler ◽

Regina Kratzer ◽

Peter Mayr

Keyword(s):

Steady State ◽

Kinetic Analysis ◽

Functional Properties ◽

Xylose Reductase ◽

Quantitative Structure ◽

Multiple Forms ◽

Structure Activity ◽

Steady State Kinetic ◽

Quantitative Structure Activity Relationships ◽

State Kinetic

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Application of the linear free energy principle for derivation of nonlinear quantitative structure-activity relationships. A steady-state kinetic model

Journal of Mathematical Chemistry ◽

10.1007/bf01165558 ◽

1993 ◽

Vol 13 (1) ◽

pp. 115-132

Author(s):

Art?ras K. Dubickas ◽

A. A. Petraaskas

Keyword(s):

Free Energy ◽

Steady State ◽

Quantitative Structure ◽

Energy Principle ◽

Free Energy Principle ◽

Linear Free Energy ◽

Structure Activity ◽

Steady State Kinetic ◽

Quantitative Structure Activity Relationships ◽

State Kinetic

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Xylose Reductase from the Basidiomycete Fungus Cryptococcus flavus: Purification, Steady-State Kinetic Characterization, and Detailed Analysis of the Substrate Binding Pocket Using Structure-Activity Relationships

The Journal of Biochemistry ◽

10.1093/jb/mvg071 ◽

2003 ◽

Vol 133 (4) ◽

pp. 553-562 ◽

Cited By ~ 8

Author(s):

P. Mayr

Keyword(s):

Steady State ◽

Detailed Analysis ◽

Xylose Reductase ◽

Binding Pocket ◽

Kinetic Characterization ◽

Substrate Binding Pocket ◽

Structure Activity ◽

Steady State Kinetic ◽

State Kinetic ◽

Basidiomycete Fungus

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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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