Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase

Biochemistry ◽  
1981 ◽  
Vol 20 (5) ◽  
pp. 1204-1210 ◽  
Author(s):  
Paul F. Cook ◽  
George L. Kenyon ◽  
W. Wallace Cleland
Keyword(s):  
Creatine Kinase ◽  
Catalytic Mechanism ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

Sodium barbital is a slow reversible inactivator of rabbit-muscle creatine kinase

2006 ◽  
Vol 84 (2) ◽  
pp. 142-147
Author(s):  
Feng Shi ◽  
Tong-Jin Zhao ◽  
Hua-Wei He ◽  
Jie Li ◽  
Xian-Gang Zeng ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Energy Homeostasis ◽  
Inactivation Kinetics ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Reversible Inactivation ◽  
Inhibition Effect ◽  
Sodium Barbital ◽  
Muscle Creatine ◽  
Detailed Kinetics

As a depressant of the central nervous system, the clinical effect of sodium barbital has been extensively studied. Here we report on sodium barbital as an inhibitor of rabbit-muscle creatine kinase (CK), which plays a significant role in energy homeostasis in the muscles. Although sodium barbital gradually inhibits the activity of CK with increased concentration, the inhibition effect can be completely reversed by dilution, indicating that the inactivation process is reversible. Detailed kinetics analysis, according to a previously presented theory, indicates that sodium barbital functions as a non complexing inhibitor, and its inhibition effect on CK is a slow reversible inactivation. In this study, a kinetic model of the substrate reaction is presented, and the microscopic rate constants for the reaction of sodium barbital with the free enzyme and the enzyme–substrate complexes are determined. Kinetic analysis reveals that sodium barbital might compete with both creatine and ATP, but mainly with creatine, to inhibit the activity of CK. The results suggest that CK might be a target for sodium barbital in vivo.Key words: creatine kinase; inactivation; kinetics; sodium barbital.

Mutagenesis of Two Acidic Active Site Residues in Human Muscle Creatine Kinase:  Implications for the Catalytic Mechanism†

Biochemistry ◽  
2001 ◽  
Vol 40 (10) ◽  
pp. 3056-3061 ◽  
Author(s):  
John S. Cantwell ◽  
Walter R. Novak ◽  
Pan-Fen Wang ◽  
Michael J. McLeish ◽  
George L. Kenyon ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Active Site ◽  
Catalytic Mechanism ◽  
Human Muscle ◽  
Active Site Residues ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

Mixed Macromolecular Crowding Accelerates the Refolding of Rabbit Muscle Creatine Kinase: Implications for Protein Folding in Physiological Environments

2006 ◽  
Vol 364 (3) ◽  
pp. 469-482 ◽  
Author(s):  
Fen Du ◽  
Zheng Zhou ◽  
Zhong-Ying Mo ◽  
Jun-Zhi Shi ◽  
Jie Chen ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Protein Folding ◽  
Macromolecular Crowding ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

scholarly journals Chaperone-Like Effect of the Linker on the Isolated C-Terminal Domain of Rabbit Muscle Creatine Kinase

2012 ◽  
Vol 103 (3) ◽  
pp. 558-566 ◽  
Author(s):  
Zhe Chen ◽  
Xiang-Jun Chen ◽  
Mengdie Xia ◽  
Hua-Wei He ◽  
Sha Wang ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Terminal Domain ◽  
Muscle Creatine

Non-identical behaviour of the subunits of rabbit muscle creatine kinase

1976 ◽  
Vol 445 (2) ◽  
pp. 364-376 ◽  
Author(s):  
Nicholas C. Price ◽  
Morag G. Hunter
Keyword(s):  
Creatine Kinase ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine ◽  
Identical Behaviour

Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase

Biochemistry ◽  
1981 ◽  
Vol 20 (21) ◽  
pp. 6155-6164 ◽  
Author(s):  
Paul R. Rosevear ◽  
Peter Desmeules ◽  
George L. Kenyon ◽  
Albert S. Mildvan
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Creatine Kinase ◽  
Magnetic Resonance ◽  
Active Site ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Magnetic Resonance Studies ◽  
Histidine Residues ◽  
Muscle Creatine
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