Myofibrillar creatine kinase activity inferred from a 3D model

Physiological Research

Volumn 51, Issue 1, 2002, Pages 35-41

  Mejsnar, Jiří A ^a   Sopko, B ^a   Gregor, M ^a  

^a CHARLES UNIVERSITY   (Czech Republic)

Author keywords

Energetics; Muscle; Myofibrillar creatine kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; CREATINE; CREATINE KINASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; MODEL; MUSCLE FIBRIL;

ACID-BASE EQUILIBRIUM; ADENOSINE TRIPHOSPHATE; CREATINE KINASE; ISOENZYMES; MODELS, BIOLOGICAL; MOLECULAR CONFORMATION; MYOFIBRILS; PHOSPHORYLATION; PROTEIN CONFORMATION;

EID: 0036197147     PISSN: 08628408     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (13)

1. Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase
2. Structural changes of creatine kinase upon substrate binding
3. Structure of mitochondrial creatine kinase
4. Fluorescence spectroscopy of creatine kinase molecule
5. Creatine kinase reaction in skinned rat psoas muscle fibers and their myofibrils
6. SWISS-MODEL protein modeling
7. Magnesium-adenosine diphosphate binding sites in wild-type creatine kinase and in mutants: Role of aromatic residues probed by Raman and infrared spectroscopies
8. Energetics of muscle contraction
9. Enzymatic reaction and the enzyme activity assessed at a subcellular level
10. Crystal structure of rabbit muscle creatine kinase
11. Inhibition of creatine kinase by chromium nucleotides
12. Balancing ATP in the cell
13. Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation