Article: A study of the role of the reactive thiol group of rabbit muscle creatine kinase with a chromophoric 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.

Citing Articles

The effect of limited proteolysis on rabbit muscle creatine kinase.

Price N, Murray S Biochem J. 1981; 199(1):239-44.

PMID: 7039617 PMC: 1163356. DOI: 10.1042/bj1990239.

The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate.

Clarke D, Price N Biochem J. 1979; 181(2):467-75.

PMID: 496894 PMC: 1161179. DOI: 10.1042/bj1810467.

The reaction of rabbit muscle creatine kinase with some derivatives of iodoacetamide.

Price N Biochem J. 1979; 177(2):603-12.

PMID: 435254 PMC: 1186411. DOI: 10.1042/bj1770603.

References

1.

Markham G, Reed G . Magnetic resonance studies of three forms of creatine kinase. Comparison of the properties of native, CH-S-blocked, and H2NCOCH-blocked enzymes. J Biol Chem. 1977; 252(4):1197-201. View

2.

Laue M, Quiocho F . Spectrochemical and ligand-binding studies of an active mercurinitrophenol-labeled creatine kinase. Biochemistry. 1977; 16(17):3838-45. DOI: 10.1021/bi00636a019. View

3.

Maggio E, Kenyon G . Properties of a CH3-blocked creatine kinase with altered catalytic activity. Kinetic consequences of the presence of the blocking group. J Biol Chem. 1977; 252(4):1202-7. View

4.

der Terrossian E, Kassab R . Preparation and properties of S-cyano derivatives of creatine kinase. Eur J Biochem. 1976; 70(2):623-8. DOI: 10.1111/j.1432-1033.1976.tb11053.x. View

5.

James T, Cohn M . The role of the lysyl residue at the active site of creatine kinase. Nuclear Overhauser effect studies. J Biol Chem. 1974; 249(8):2599-604. View

6.

Price N, Hunter M . Non-identical behaviour of the subunits of rabbit muscule creatine kinase. Biochim Biophys Acta. 1976; 445(2):364-76. DOI: 10.1016/0005-2744(76)90090-5. View

7.

Smith D, Maggio E, Kenyon G . Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes. Biochemistry. 1975; 14(4):766-71. DOI: 10.1021/bi00675a019. View

8.

Quiocho F, Thomson J . Substrate binding to an active creatine kinase with a thiol-bound mercurinitrophenol chromophoric probe. Proc Natl Acad Sci U S A. 1973; 70(10):2858-62. PMC: 427125. DOI: 10.1073/pnas.70.10.2858. View

9.

Mclaughlin A . The interaction of 8-anilino-1-naphthalenesulfonate with creatine kinase. Evidence for cooperativitiy of nucleotide binding. J Biol Chem. 1974; 249(5):1445-52. View

10.

Kelly I . Creatine kinase. Modification of the working enzyme. Biochem J. 1976; 157(1):23-31. PMC: 1163814. DOI: 10.1042/bj1570023. View

11.

Haugland R . Conformational flexibility and structure of creatine kinase. J Supramol Struct. 1975; 3(2):192-9. DOI: 10.1002/jss.400030213. View

12.

Watts D . Inhibition of adenosine 5'-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organization of the catalytic site. Biochem J. 1971; 122(5):727-40. PMC: 1176842. DOI: 10.1042/bj1220727. View

A Study of the Role of the Reactive Thiol Group of Rabbit Muscle Creatine Kinase with a Chromophoric Reporter Group