메뉴 건너뛰기




Volumn 45, Issue 38, 2006, Pages 11464-11472

Exploring the role of the active site cysteine in human muscle creatine kinase

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; ENZYME KINETICS; HYDROGEN BONDS; MUSCLE; MUTAGENESIS; PH EFFECTS;

EID: 33749011194     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0607002     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann, T., Wyss, M., Brdiczka, D., Nicolay, K., and Eppenberger, H. M. (1992) Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis, Biochem. J. 281, 21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 2
    • 0031712655 scopus 로고    scopus 로고
    • Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach
    • Schlattner, U., Forstner, M., Eder, M., Stachowiak, O., Fritz-Wolf, K., and Wallimann, T. (1998) Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach, Mol. Cell. Biochem. 184, 125-140.
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 125-140
    • Schlattner, U.1    Forstner, M.2    Eder, M.3    Stachowiak, O.4    Fritz-Wolf, K.5    Wallimann, T.6
  • 3
    • 0033935979 scopus 로고    scopus 로고
    • Creatine and creatinine metabolism
    • Wyss, M., and Kaddurah-Daouk, R. (2000) Creatine and creatinine metabolism, Physiol. Rev. 80, 1107-1213.
    • (2000) Physiol. Rev. , vol.80 , pp. 1107-1213
    • Wyss, M.1    Kaddurah-Daouk, R.2
  • 4
    • 0024852674 scopus 로고
    • Diagnostic use of CK-MM and CK-MB isoforms for detecting myocardial infarction
    • Apple, F. S. (1989) Diagnostic use of CK-MM and CK-MB isoforms for detecting myocardial infarction, Clin. Lab. Med. 9, 643-654.
    • (1989) Clin. Lab. Med. , vol.9 , pp. 643-654
    • Apple, F.S.1
  • 5
    • 0033013566 scopus 로고    scopus 로고
    • Creatine kinase isoforms and myoglobin: Early detection of myocardial infarction and reperfusion
    • Apple, F. S. (1999) Creatine kinase isoforms and myoglobin: early detection of myocardial infarction and reperfusion, Coron. Art. Dis. 10, 75-79.
    • (1999) Coron. Art. Dis. , vol.10 , pp. 75-79
    • Apple, F.S.1
  • 7
    • 0032030854 scopus 로고    scopus 로고
    • Abnormal properties of creatine kinase in Alzheimer's disease brain: Correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning
    • David, S., Shoemaker, M., and Haley, B. E. (1998) Abnormal properties of creatine kinase in Alzheimer's disease brain: correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning, Brain Res. Mol. Brain Res. 54, 276-287.
    • (1998) Brain Res. Mol. Brain Res. , vol.54 , pp. 276-287
    • David, S.1    Shoemaker, M.2    Haley, B.E.3
  • 8
    • 0032969798 scopus 로고    scopus 로고
    • Creatine kinase, cell membrane and Duchenne muscular dystrophy
    • Ozawa, E., Hagiwara, Y., and Yoshida, M. (1999) Creatine kinase, cell membrane and Duchenne muscular dystrophy, Mol. Cell. Biochem. 190, 143-151.
    • (1999) Mol. Cell. Biochem. , vol.190 , pp. 143-151
    • Ozawa, E.1    Hagiwara, Y.2    Yoshida, M.3
  • 10
    • 0034849927 scopus 로고    scopus 로고
    • Serum creatine kinase levels parallel the clinical course for rhabdomyomatous Wilms tumor
    • Delahunt, B., Lewis, M. E., Pringle, K. C., Wiltshire, E. J., and Crooke, M. J. (2001) Serum creatine kinase levels parallel the clinical course for rhabdomyomatous Wilms tumor, Am. J. Clin. Pathol. 116, 354-359.
    • (2001) Am. J. Clin. Pathol. , vol.116 , pp. 354-359
    • Delahunt, B.1    Lewis, M.E.2    Pringle, K.C.3    Wiltshire, E.J.4    Crooke, M.J.5
  • 11
    • 10044231671 scopus 로고    scopus 로고
    • Clinical applications of microarray technology: Creatine kinase B is an up-regulated gene in epithelial ovarian cancer and shows promise as a serum marker
    • Huddleston, H. G., Wong, K. K., Welch, W. R., Berkowitz, R. S., and Mok, S. C. (2005) Clinical applications of microarray technology: creatine kinase B is an up-regulated gene in epithelial ovarian cancer and shows promise as a serum marker, Gynecol. Oncol. 96, 77-83.
    • (2005) Gynecol. Oncol. , vol.96 , pp. 77-83
    • Huddleston, H.G.1    Wong, K.K.2    Welch, W.R.3    Berkowitz, R.S.4    Mok, S.C.5
  • 13
  • 14
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao, J. K., Bujacz, G., and Wlodawer, A. (1998) Crystal structure of rabbit muscle creatine kinase, FEBS Lett. 439, 133-137.
    • (1998) FEBS Lett. , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3
  • 16
    • 0027268548 scopus 로고
    • Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis
    • Furter, R., Furter-Graves, E. M., and Wallimann, T. (1993) Creatine kinase: the reactive cysteine is required for synergism but is nonessential for catalysis, Biochemistry 32, 7022-7029.
    • (1993) Biochemistry , vol.32 , pp. 7022-7029
    • Furter, R.1    Furter-Graves, E.M.2    Wallimann, T.3
  • 17
    • 0029894773 scopus 로고    scopus 로고
    • Rabbit muscle creatine kinase: Consequences of the mutagenesis of conserved histidine residues
    • Chen, L. H., Borders, C. L., Jr., Vasquez, J. R., and Kenyon, G. L. (1996) Rabbit muscle creatine kinase: consequences of the mutagenesis of conserved histidine residues, Biochemistry 35, 7895-7902.
    • (1996) Biochemistry , vol.35 , pp. 7895-7902
    • Chen, L.H.1    Borders Jr., C.L.2    Vasquez, J.R.3    Kenyon, G.L.4
  • 18
    • 0035852971 scopus 로고    scopus 로고
    • Mutagenesis of two acidic active site residues in human muscle creatine kinase: Implications for the catalytic mechanism
    • Cantwell, J. S., Novak, W. R., Wang, P. F., McLeish, M. J., Kenyon, G. L., and Babbitt, P. C. (2001) Mutagenesis of two acidic active site residues in human muscle creatine kinase: implications for the catalytic mechanism, Biochemistry 40, 3056-3061.
    • (2001) Biochemistry , vol.40 , pp. 3056-3061
    • Cantwell, J.S.1    Novak, W.R.2    Wang, P.F.3    McLeish, M.J.4    Kenyon, G.L.5    Babbitt, P.C.6
  • 20
    • 15944400625 scopus 로고    scopus 로고
    • Relating structure to mechanism in creatine kinase
    • McLeish, M. J., and Kenyon, G. L. (2005) Relating structure to mechanism in creatine kinase, Crit. Rev. Biochem. Mol. Biol. 40, 1-20.
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 1-20
    • McLeish, M.J.1    Kenyon, G.L.2
  • 21
    • 0000199735 scopus 로고
    • The amino acid sequence around the "reactive" sulfhydryl groups in adenosine triphosphocreatine phosphotransferase
    • Mahowald, T. A. (1965) The amino acid sequence around the "reactive" sulfhydryl groups in adenosine triphosphocreatine phosphotransferase, Biochemistry 4, 732-740.
    • (1965) Biochemistry , vol.4 , pp. 732-740
    • Mahowald, T.A.1
  • 22
    • 0344314134 scopus 로고
    • Effect of oligomerization on the properties of essential SH-groups of mitochondrial creatine kinase
    • Fedosov, S. N., and Belousova, L. V. (1988) Effect of oligomerization on the properties of essential SH-groups of mitochondrial creatine kinase, Biokhimiya 53, 550-564.
    • (1988) Biokhimiya , vol.53 , pp. 550-564
    • Fedosov, S.N.1    Belousova, L.V.2
  • 23
    • 0019509122 scopus 로고
    • Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase
    • Cook, P. F., Kenyon, G. L., and Cleland, W. W. (1981) Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase, Biochemistry 20, 1204-1210.
    • (1981) Biochemistry , vol.20 , pp. 1204-1210
    • Cook, P.F.1    Kenyon, G.L.2    Cleland, W.W.3
  • 24
    • 0036001159 scopus 로고    scopus 로고
    • Structural basis of perturbed pKa values of catalytic groups in enzyme active sites
    • Harris, T. K., and Turner, G. J. (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites, IUBMB Life 53, 85-98.
    • (2002) IUBMB Life , vol.53 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 26
    • 0033928160 scopus 로고    scopus 로고
    • A comparative study of human muscle and brain creatine kinases expressed in Escherichia coli
    • Chen, L. H., White, C. B., Babbitt, P. C., McLeish, M. J., and Kenyon, G. L. (2000) A comparative study of human muscle and brain creatine kinases expressed in Escherichia coli, J. Protein Chem. 19, 59-66.
    • (2000) J. Protein Chem. , vol.19 , pp. 59-66
    • Chen, L.H.1    White, C.B.2    Babbitt, P.C.3    McLeish, M.J.4    Kenyon, G.L.5
  • 30
    • 0034658257 scopus 로고    scopus 로고
    • Crystal structure of human ubiquitous mitochondrial creatine kinase
    • Eder, M., Fritz-Wolf, K., Kabsch, W., Wallimann, T., and Schlattner, U. (2000) Crystal structure of human ubiquitous mitochondrial creatine kinase, Proteins 39, 216-225.
    • (2000) Proteins , vol.39 , pp. 216-225
    • Eder, M.1    Fritz-Wolf, K.2    Kabsch, W.3    Wallimann, T.4    Schlattner, U.5
  • 32
    • 0036417674 scopus 로고    scopus 로고
    • Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies
    • Wang, P. F., Novak, W. R. P., Cantwell, J. S., Babbitt, P. C., McLeish, M. J., and Kenyon, G. L. (2002) Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies, Protein Expression Purif. 26, 89-95.
    • (2002) Protein Expression Purif. , vol.26 , pp. 89-95
    • Wang, P.F.1    Novak, W.R.P.2    Cantwell, J.S.3    Babbitt, P.C.4    McLeish, M.J.5    Kenyon, G.L.6
  • 33
    • 0001838147 scopus 로고
    • The mechanism of the reaction catalyzed by adenosine triphosphate- creatine phosphotransferase
    • Morrison, J. F., and James, E. (1965) The mechanism of the reaction catalyzed by adenosine triphosphate-creatine phosphotransferase, Biochem. J. 97, 37-52.
    • (1965) Biochem. J. , vol.97 , pp. 37-52
    • Morrison, J.F.1    James, E.2
  • 34
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying ph-dependent processes
    • Ellis, K. J., and Morrison, J. F. (1982) Buffers of constant ionic strength for studying ph-dependent processes, Methods Enzymol. 87, 405-426.
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 36
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J. M., Cieplak, P., and Kollman, P. A. (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?, J. Comput. Chem. 21, 1049-1074.
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 37
    • 0037495965 scopus 로고    scopus 로고
    • Development of polyphosphate parameters for use with the AMBER force field
    • Meagher, K., Redman, L., and Carlson, H. (2003) Development of polyphosphate parameters for use with the AMBER force field, J. Comput. Chem. 24, 1016-1025.
    • (2003) J. Comput. Chem. , vol.24 , pp. 1016-1025
    • Meagher, K.1    Redman, L.2    Carlson, H.3
  • 39
    • 84986516411 scopus 로고
    • Application of the multimolecule and multiconformational RESP methodology to biopolymers-charge derivation for DNA, RNA, and proteins
    • Cieplak, P., Cornell, W. D., Bayly, C., and Kollman, P. A. (1995) Application of the multimolecule and multiconformational RESP methodology to biopolymers-charge derivation for DNA, RNA, and proteins, J. Comput. Chem. 16, 1357-1377.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.3    Kollman, P.A.4
  • 40
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald-an N.log(N) method for Ewald sums in large systems, J. Chem. Phys. 98, 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 43
    • 29344458799 scopus 로고    scopus 로고
    • Computational studies of the farnesyltransferase ternary complex part I: Substrate binding
    • Cui, G., Wang, B., and Merz, K. M., Jr. (2005) Computational studies of the farnesyltransferase ternary complex part I: substrate binding, Biochemistry 44, 16513-16523.
    • (2005) Biochemistry , vol.44 , pp. 16513-16523
    • Cui, G.1    Wang, B.2    Merz Jr., K.M.3
  • 44
    • 0001496334 scopus 로고
    • Properties of thiolesters: Kinetics of hydrolysis in dilute aqueous media
    • Noda, L., Kuby, S. A., and Lardy, H. (1953) Properties of thiolesters: kinetics of hydrolysis in dilute aqueous media, J. Am. Chem. Soc. 75, 913-917.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 913-917
    • Noda, L.1    Kuby, S.A.2    Lardy, H.3
  • 45
    • 0015962432 scopus 로고
    • Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes
    • Polgár, L. (1974) Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes, FEBS Lett. 38, 187-190.
    • (1974) FEBS Lett. , vol.38 , pp. 187-190
    • Polgár, L.1
  • 47
    • 0027325607 scopus 로고
    • Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site
    • Lo Bello, M., Parker, M. W., Desideri, A., Polticelli, F., Falconi, M., Del Boccio, G., Pennelli, A., Federici, G., and Ricci, G. (1993) Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site, J. Biol. Chem. 268, 19033-19038.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19033-19038
    • Lo Bello, M.1    Parker, M.W.2    Desideri, A.3    Polticelli, F.4    Falconi, M.5    Del Boccio, G.6    Pennelli, A.7    Federici, G.8    Ricci, G.9
  • 50
    • 21344465414 scopus 로고    scopus 로고
    • Loop movement and catalysis in creatine kinase
    • Wang, P.-F., Flynn, A. D., McLeish, M. J., and Kenyon, G. L. (2005) Loop movement and catalysis in creatine kinase, IUBMB Life 57, 355-362.
    • (2005) IUBMB Life , vol.57 , pp. 355-362
    • Wang, P.-F.1    Flynn, A.D.2    McLeish, M.J.3    Kenyon, G.L.4
  • 51
    • 7244234097 scopus 로고    scopus 로고
    • Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase
    • Novak, W. R. P., Wang, P.-F., McLeish, M. J., Kenyon, G. L., and Babbitt, P. C. (2004) Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase, Biochemistry 43, 13766-13774.
    • (2004) Biochemistry , vol.43 , pp. 13766-13774
    • Novak, W.R.P.1    Wang, P.-F.2    McLeish, M.J.3    Kenyon, G.L.4    Babbitt, P.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.