Kinetic consequences of a slow substrate binding step in group transferases Interpretation of product inhibition experiments-Reference-Cited by-同舟云学术

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Kinetic consequences of a slow substrate binding step in group transferases Interpretation of product inhibition experiments

Published:1976-05 Issue:3 Volume:429 Page:720-741
ISSN:0005-2744
Container-title:Biochimica et Biophysica Acta (BBA) - Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Enzymology

Author:

Himoe Albert

Publisher

Elsevier BV

Reference66 articles.

1. The kinetics of enzyme-catalyzed reactions with two or more substrates or products

2. Kinetic Study of Yeast Hexokinase. 1. Steady-State Kinetics

3. Comments on the Kinetics and Mechanism of Yeast Hexokinase Action. Is the Binding Sequence of Substrates to the Enzyme Ordered or Random?

4. Computer Simulation Studies with Yeast Hexokinase and Additional Evidence for the Random Bi Bi Mechanism

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Protonation of arginine 57 of Escherichia coli ornithine transcarbamoylase regulates substrate binding and turnover.;Journal of Biological Chemistry;1993-09

2. Substrate binding sites on arginine phosphokinase (Homarus vulgaris);Biochimie;1979-09

3. Anabolic Ornithine Carbamoyltransferase of Escherichia coli and Catabolic Ornithine Carbamoyltransferase of Pseudomonas putida. Steady-State Kinetic Analysis;European Journal of Biochemistry;1978-08

4. Choline sulfokinase of penicillium chrysogenum: Partial purification and kinetic mechanism;Archives of Biochemistry and Biophysics;1977-04

5. Serine transhydroxymethylase: evidence for a sequential random mechanism;Biochemistry;1977-02-08

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