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

Dynamic Asymmetry and the Role of the Conserved Active-Site Thiol in Rabbit Muscle Creatine Kinase

Biochemistry ◽  
2014 ◽  
Vol 54 (1) ◽  
pp. 83-95 ◽  
Author(s):  
Casey H. Londergan ◽  
Rachel Baskin ◽  
Connor G. Bischak ◽  
Kevin W. Hoffman ◽  
David M. Snead ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Active Site ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

scholarly journals Asymmetry in Rabbit Muscle Creatine Kinase from the Perspective of Active Site Cysteines

2011 ◽  
Vol 100 (3) ◽  
pp. 224a
Author(s):  
Kevin W. Hoffman ◽  
Connor G. Bischak ◽  
David M. Snead ◽  
Stephen Griffiths ◽  
Christopher Reynoso ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Active Site ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

Rabbit Muscle Creatine Kinase:  Consequences of the Mutagenesis of Conserved Histidine Residues†

Biochemistry ◽  
1996 ◽  
Vol 35 (24) ◽  
pp. 7895-7902 ◽  
Author(s):  
Lorenzo H. Chen ◽  
Charles L. Borders, ◽  
John R. Vásquez ◽  
George L. Kenyon
Keyword(s):  
Creatine Kinase ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Histidine Residues ◽  
Muscle Creatine

scholarly journals A study of the role of the reactive thiol group of rabbit muscle creatine kinase with a chromophoric reporter group

1978 ◽  
Vol 171 (1) ◽  
pp. 269-272 ◽  
Author(s):  
M A Keighren ◽  
N C Price
Keyword(s):  
Creatine Kinase ◽  
Conformational Changes ◽  
Thiol Group ◽  
Enzymic Activity ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Transition State Analogue ◽  
Muscle Creatine ◽  
Reporter Group

Substrate- and ligand-induced conformational changes were studied in a series of thiol-modified derivatives of rabbit muscle creatine kinase that retained different amounts of enzymic activity. The results indicate that the ‘reactive’ thiol group of the enzyme is required for the conformational changes associated with formation of a ‘transition-state analogue’ complex.

scholarly journals Exploring the Role of the Active Site Cysteine in Human Muscle Creatine Kinase†

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11464-11472 ◽  
Author(s):  
Pan-Fen Wang ◽  
Allen J. Flynn ◽  
Mor M. Naor ◽  
Jan H. Jensen ◽  
Guanglei Cui ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Active Site ◽  
Human Muscle ◽  
Muscle Creatine Kinase ◽  
Active Site Cysteine ◽  
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.

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