Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.

Literature DB >> 5820641

The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.

Abstract

The analysis and interpretation of initial-rate data for reactions involving three substrates, obtained in suitably designed experiments, are discussed. Possible mechanisms for such reactions are classified, the rate equations are compared and the extent to which they can be distinguished experimentally is considered.

Mesh：

Substances：

Year: 1969 PMID： 5820641 PMCID： PMC1184927 DOI： 10.1042/bj1140547

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

9 in total

Review 1. THE METABOLISM OF PROPIONIC ACID.

Authors: Y KAZIRO; S OCHOA
Journal: Adv Enzymol Relat Subj Biochem Date: 1964

2. EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF LIVER AND YEAST ALCOHOL DEHYDROGENASE.

Authors: E SILVERSTEIN; P D BOYER
Journal: J Biol Chem Date: 1964-11 Impact factor: 5.157

3. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.

Authors: W W CLELAND
Journal: Biochim Biophys Acta Date: 1963-01-08

4. Kinetic studies of liver alcohol dehydrogenase.

Authors: K DALZIEL
Journal: Biochem J Date: 1962-08 Impact factor: 3.857

5. [Research on monocarbon compounds. I. The tetrahydrofolate formylase from pigeon liver. Purification and mechanism].

Authors: L JAENICKE; E BRODE
Journal: Biochem Z Date: 1961

6. Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction.

Authors: C FRIEDEN
Journal: J Biol Chem Date: 1959-11 Impact factor: 5.157

7. Acyl adenylates; an enzymatic mechanism of acetate activation.

Authors: P BERG
Journal: J Biol Chem Date: 1956-10 Impact factor: 5.157

8. Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme.

Authors: S KAUFMAN
Journal: J Biol Chem Date: 1955-09 Impact factor: 5.157

9. The kinetics and mechanism of liver alcohol dehydrogenase with primary and secondary alcohols as substrates.

Authors: K Dalziel; F M Dickinson
Journal: Biochem J Date: 1966-07 Impact factor: 3.857

9 in total

21 in total

1. Steady-state kinetic analysis of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath).

Authors: J Green; H Dalton
Journal: Biochem J Date: 1986-05-15 Impact factor: 3.857

2. A steady-state kinetic study of the reaction catalysed by the secondary-amine mono-oxygenase of Pseudomonas aminovorans.

Authors: D F Brook; P J Large
Journal: Biochem J Date: 1976-07-01 Impact factor: 3.857

3. Gene cloning, sequence analysis, and expression of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase.

Authors: P Chaiyen; D P Ballou; V Massey
Journal: Proc Natl Acad Sci U S A Date: 1997-07-08 Impact factor: 11.205

4. Kinetic studies of dogfish liver glutamate dehydrogenase.

Authors: A H Electricwala; F M Dickinson
Journal: Biochem J Date: 1979-02-01 Impact factor: 3.857

5. Biochemical characterization of selenium-containing catalytic antibody as a cytosolic glutathione peroxidase mimic.

Authors: L Ding; Z Liu; Z Zhu; G Luo; D Zhao; J Ni
Journal: Biochem J Date: 1998-05-15 Impact factor: 3.857

6. The lactose synthase acceptor site: a structural map derived from acceptor studies.

Authors: L J Berliner; M E Davis; K E Ebner; T A Beyer; J E Bell
Journal: Mol Cell Biochem Date: 1984-04 Impact factor: 3.396

7. [On the mechanism of action of glutamate dehydrogenase from pea seedlings and the regulation of the activity by adenosine phosphates, the energy charge and ions].

Authors: E Pahlich; J Hoffmann
Journal: Planta Date: 1975-01 Impact factor: 4.116