메뉴 건너뛰기




Volumn 40, Issue 1, 2005, Pages 1-20

Relating structure to mechanism in creatine kinase

Author keywords

Energy homeostasis; Guanidino kinase; Myocardial infarction; Phosphagen kinase; Phosphoryl group transfer; Transition state analogue complex; X ray structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE KINASE; CREATINE; CREATINE KINASE; CREATINE KINASE ISOENZYME; CREATINE PHOSPHATE; CYTOPLASM PROTEIN; DIMER; FUNCTIONAL GROUP; MITOCHONDRIAL ENZYME; NITRATE; NUCLEOTIDE; OLIGOMER; PHOSPHORYL GROUP; UNCLASSIFIED DRUG;

EID: 15944400625     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409230590918577     Document Type: Review
Times cited : (170)

References (152)
  • 1
    • 1342331873 scopus 로고    scopus 로고
    • The role of phosphagen specificity loops in arginine kinase
    • Azzi, A., Clark, S.A., Ellington, W.R., and Chapman, M.S. 2004. The role of phosphagen specificity loops in arginine kinase. Protein Sci 13:575-585.
    • (2004) Protein Sci , vol.13 , pp. 575-585
    • Azzi, A.1    Clark, S.A.2    Ellington, W.R.3    Chapman, M.S.4
  • 2
    • 0017903526 scopus 로고
    • Creatine kinase: A review of some recent work on the mechanism and subunit behavior of the enzyme
    • Bickerstaff, G.F. and Price, N.C. 1978. Creatine kinase: A review of some recent work on the mechanism and subunit behavior of the enzyme. Int J Biochem 9:1-8.
    • (1978) Int J Biochem , vol.9 , pp. 1-8
    • Bickerstaff, G.F.1    Price, N.C.2
  • 3
    • 0030010987 scopus 로고    scopus 로고
    • The utilisation of creatine and its analogues by cytosolic and mitochondrial creatine kinase
    • Boehm, E.A., Radda, G.K., Tomlin, H., and Clark, J.F. 1996. The utilisation of creatine and its analogues by cytosolic and mitochondrial creatine kinase. Biochim Biophys Acta 1274:119-128.
    • (1996) Biochim Biophys Acta , vol.1274 , pp. 119-128
    • Boehm, E.A.1    Radda, G.K.2    Tomlin, H.3    Clark, J.F.4
  • 4
    • 0016717899 scopus 로고
    • An essential arginyl residue at the nucleotide binding site of creatine kinase
    • Borders, C.L., Jr. and Riordan, J.F. 1975. An essential arginyl residue at the nucleotide binding site of creatine kinase. Biochemistry 4:4699-4704.
    • (1975) Biochemistry , vol.4 , pp. 4699-4704
    • Borders Jr., C.L.1    Riordan, J.F.2
  • 5
    • 0037018947 scopus 로고    scopus 로고
    • Determination of the affinity of each component of a composite quaternary transition-state analogue complex of creatine kinase
    • Borders, C.L., Jr., Snider, M.J., Wolfenden, R., and Edmiston, P.L. 2002. Determination of the affinity of each component of a composite quaternary transition-state analogue complex of creatine kinase. Biochemistry 41:6995-7000.
    • (2002) Biochemistry , vol.41 , pp. 6995-7000
    • Borders Jr., C.L.1    Snider, M.J.2    Wolfenden, R.3    Edmiston, P.L.4
  • 7
    • 0023655789 scopus 로고
    • Compartmented coupling of chicken heart mitochondria creatine kinase to the nucleotide translocase requires the outer mitochondrial membrane
    • Brooks, S.P. and Suelter, C.H. 1987. Compartmented coupling of chicken heart mitochondria creatine kinase to the nucleotide translocase requires the outer mitochondrial membrane. Arch Biochem Biophys 257:144-153.
    • (1987) Arch Biochem Biophys , vol.257 , pp. 144-153
    • Brooks, S.P.1    Suelter, C.H.2
  • 8
    • 0026793939 scopus 로고
    • The active site of creatine kinase. Affinity labeling of cysteine 282 with N-(2,3-epoxypropyl)-N-amidinoglycine
    • Buechter, D.D., Medzihradszky, K.F., Burlingame, A.L., and Kenyon, G.L. 1992. The active site of creatine kinase. Affinity labeling of cysteine 282 with N-(2,3-epoxypropyl)-N-amidinoglycine. J Biol Chem 267:2173-2178.
    • (1992) J Biol Chem , vol.267 , pp. 2173-2178
    • Buechter, D.D.1    Medzihradszky, K.F.2    Burlingame, A.L.3    Kenyon, G.L.4
  • 9
    • 0019321490 scopus 로고
    • Structure of metal x nucleotide complex in the creatine kinase reaction. A study with diastereomeric phosphorothioate analogs of adenosine di- and triphosphate
    • Burgers, P.M. and Eckstein, F. 1980. Structure of metal x nucleotide complex in the creatine kinase reaction. A study with diastereomeric phosphorothioate analogs of adenosine di- and triphosphate. J Biol Chem 255:8229-8233.
    • (1980) J Biol Chem , vol.255 , pp. 8229-8233
    • Burgers, P.M.1    Eckstein, F.2
  • 10
    • 0018276787 scopus 로고
    • Creatine kinase. A new crystal form providing evidence of subunit structural homogeneity
    • Burgess, A.N., Liddell, J.M., Cook, W., Tweedlie, R.M., and Swan, I.D. 1978. Creatine kinase. A new crystal form providing evidence of subunit structural homogeneity. J Mol Biol 123:691-695.
    • (1978) J Mol Biol , vol.123 , pp. 691-695
    • Burgess, A.N.1    Liddell, J.M.2    Cook, W.3    Tweedlie, R.M.4    Swan, I.D.5
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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 Prot Chem 19:59-66.
    • (2000) J Prot 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
  • 14
    • 0024825977 scopus 로고
    • A spin-label electron spin resonance study of the binding of mitochondrial creatine kinase to cardiolipin
    • Cheneval, D., Carafoli, E., Powell, G.L., and Marsh, D. 1989. A spin-label electron spin resonance study of the binding of mitochondrial creatine kinase to cardiolipin. Eur J Biochem 186:415-419.
    • (1989) Eur J Biochem , vol.186 , pp. 415-419
    • Cheneval, D.1    Carafoli, E.2    Powell, G.L.3    Marsh, D.4
  • 15
    • 0018509713 scopus 로고
    • The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate
    • Clarke, D.E. and Price, N.C. 1979. The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate. Biochem J 181:467-475.
    • (1979) Biochem J , vol.181 , pp. 467-475
    • Clarke, D.E.1    Price, N.C.2
  • 16
  • 17
    • 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
  • 19
    • 0037465512 scopus 로고    scopus 로고
    • Generation of an active monomer of rabbit muscle creatine kinase by site-directed mutagenesis: The effect of quaternary structure on catalysis and stability
    • Cox, J.M., Davis, C.A., Chan, C., Jourden, M.J., Jorjorian, A.D., Brym, M.J., Snider, M.J., Borders, C.L., Jr., and Edmiston, P.L. 2003. Generation of an active monomer of rabbit muscle creatine kinase by site-directed mutagenesis: the effect of quaternary structure on catalysis and stability. Biochemistry 42:1863-1871.
    • (2003) Biochemistry , vol.42 , pp. 1863-1871
    • Cox, J.M.1    Davis, C.A.2    Chan, C.3    Jourden, M.J.4    Jorjorian, A.D.5    Brym, M.J.6    Snider, M.J.7    Borders Jr., C.L.8    Edmiston, P.L.9
  • 20
    • 0018801583 scopus 로고
    • Subunit-selective chemical modifications of creatine kinase. Evidence for asymmetrical association of the subunits
    • Degani, Y. and Degani, C. 1979. Subunit-selective chemical modifications of creatine kinase. Evidence for asymmetrical association of the subunits. Biochemistry 18:5917-5923.
    • (1979) Biochemistry , vol.18 , pp. 5917-5923
    • Degani, Y.1    Degani, C.2
  • 21
    • 0014640009 scopus 로고
    • Comparative structural studies of the active site of ATP-guanidine phosphotransferases. The essential cysteine tryptic peptide of arginine kinase from Homarus vulgaris muscle
    • Der Terrossian, E., Pradel, L.A., Kassab, R., and Thoai, N.V. 1969. Comparative structural studies of the active site of ATP-guanidine phosphotransferases. The essential cysteine tryptic peptide of arginine kinase from Homarus vulgaris muscle. Eur J Biochem 11:482-490.
    • (1969) Eur J Biochem , vol.11 , pp. 482-490
    • Der Terrossian, E.1    Pradel, L.A.2    Kassab, R.3    Thoai, N.V.4
  • 22
    • 0017124718 scopus 로고
    • Preparation and properties of S-cyano derivatives of creatine kinase
    • Der Terrossian, E. and Kassab, R. 1976. Preparation and properties of S-cyano derivatives of creatine kinase. Eur J Biochem 70:623-628.
    • (1976) Eur J Biochem , vol.70 , pp. 623-628
    • Der Terrossian, E.1    Kassab, R.2
  • 23
    • 0000219480 scopus 로고
    • Conformational changes in arginine kinase upon ligand binding seen by small-angle x-ray scattering
    • Dumas, C. and Janin, J. 1983. Conformational changes in arginine kinase upon ligand binding seen by small-angle x-ray scattering. FEBS Lett 153:128-130.
    • (1983) FEBS Lett , vol.153 , pp. 128-130
    • Dumas, C.1    Janin, J.2
  • 24
    • 0019003286 scopus 로고
    • Preparation and properties of chromium(III) adenosine 5′-triphosphate, chromium(III) adenosine 5′-diphosphate, and related chromium(III) complexes
    • Dunaway-Mariano, D. and Cleland, W.W. 1980. Preparation and properties of chromium(III) adenosine 5′-triphosphate, chromium(III) adenosine 5′-diphosphate, and related chromium(III) complexes. Biochemistry 19:1496-1505.
    • (1980) Biochemistry , vol.19 , pp. 1496-1505
    • Dunaway-Mariano, D.1    Cleland, W.W.2
  • 26
    • 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. 2000a. 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
  • 27
    • 0034282672 scopus 로고    scopus 로고
    • A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity
    • Eder, M., Stolz, M., Wallimann, T., and Schlattner, U. 2000b. A conserved negatively charged cluster in the active site of creatine kinase is critical for enzymatic activity. J Biol Chem 275:27094-27099.
    • (2000) J Biol Chem , vol.275 , pp. 27094-27099
    • Eder, M.1    Stolz, M.2    Wallimann, T.3    Schlattner, U.4
  • 28
    • 84944495722 scopus 로고
    • Further observations of phosphagens
    • Eggleton, P. and Eggleton, G.P. 1928. Further observations of phosphagens. J Physiol 65:15-24.
    • (1928) J Physiol , vol.65 , pp. 15-24
    • Eggleton, P.1    Eggleton, G.P.2
  • 29
    • 0000258498 scopus 로고
    • The estimation of creatine and of diacetyl
    • Eggleton, P., Elsden, S.R., and Gough, N. 1943. The estimation of creatine and of diacetyl. Biochem J 37:526-529.
    • (1943) Biochem J , vol.37 , pp. 526-529
    • Eggleton, P.1    Elsden, S.R.2    Gough, N.3
  • 30
    • 0035052706 scopus 로고    scopus 로고
    • Evolution and physiological roles of phosphagen systems
    • Ellington, W.R. 2001. Evolution and physiological roles of phosphagen systems. Annu Rev Physiol 63:289-325.
    • (2001) Annu Rev Physiol , vol.63 , pp. 289-325
    • Ellington, W.R.1
  • 31
    • 0016802401 scopus 로고
    • A quenched-flow study of the reaction catalysed by creatine kinase
    • Engelborghs, Y., Marsh, A., and Gutfreund, H. 1975. A quenched-flow study of the reaction catalysed by creatine kinase. Biochem J 151:47-50.
    • (1975) Biochem J , vol.151 , pp. 47-50
    • Engelborghs, Y.1    Marsh, A.2    Gutfreund, H.3
  • 32
    • 15944375598 scopus 로고
    • Specificity of creatine phosphokinase
    • Ennor, A.M., Rosenberg, H., and Armstrong, M.D. 1955. Specificity of creatine phosphokinase. Nature 175:120.
    • (1955) Nature , vol.175 , pp. 120
    • Ennor, A.M.1    Rosenberg, H.2    Armstrong, M.D.3
  • 33
    • 0014216037 scopus 로고
    • The comparative enzymology of creatine kinases. I. Isolation and characterization from chicken and rabbit tissues
    • Eppenberger, H.M., Dawson, D.M., and Kaplan, N.O. 1967. The comparative enzymology of creatine kinases. I. Isolation and characterization from chicken and rabbit tissues. J Biol Chem 242:204-209.
    • (1967) J Biol Chem , vol.242 , pp. 204-209
    • Eppenberger, H.M.1    Dawson, D.M.2    Kaplan, N.O.3
  • 34
    • 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
  • 35
    • 0030606976 scopus 로고    scopus 로고
    • Changes in creatine kinase structure upon ligand binding as seen by small-angle scattering
    • Forstner, M., Kriechbaum, M., Laggner, P., and Wallimann, T. 1996. Changes in creatine kinase structure upon ligand binding as seen by small-angle scattering. J Mol Struct 383:217-222.
    • (1996) J Mol Struct , vol.383 , pp. 217-222
    • Forstner, M.1    Kriechbaum, M.2    Laggner, P.3    Wallimann, T.4
  • 36
    • 0342460542 scopus 로고    scopus 로고
    • The active site histidines of creatine kinase. A critical role of His 61 situated on a flexible loop
    • Forstner, M., Muller, A., Stolz, M., and Wallimann, T. 1997. The active site histidines of creatine kinase. A critical role of His 61 situated on a flexible loop. Protein Sci 6:331-339.
    • (1997) Protein Sci , vol.6 , pp. 331-339
    • Forstner, M.1    Muller, A.2    Stolz, M.3    Wallimann, T.4
  • 37
    • 0031848225 scopus 로고    scopus 로고
    • Structural changes of creatine kinase upon substrate binding
    • Forstner, M., Kriechbaum, M., Laggner, P., and Wallimann, T. 1998. Structural changes of creatine kinase upon substrate binding. Biophys J 75:1016-1023.
    • (1998) Biophys J , vol.75 , pp. 1016-1023
    • Forstner, M.1    Kriechbaum, M.2    Laggner, P.3    Wallimann, T.4
  • 39
    • 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
  • 40
    • 3042856467 scopus 로고    scopus 로고
    • The active site cysteine of arginine kinase: Structural and functional analysis of partially active mutants
    • Gattis, J.L., Ruben, E., Fenley, M.O., Ellington, W.R., and Chapman, M.S. 2004. The active site cysteine of arginine kinase: structural and functional analysis of partially active mutants. Biochemistry 43:8680-8689.
    • (2004) Biochemistry , vol.43 , pp. 8680-8689
    • Gattis, J.L.1    Ruben, E.2    Fenley, M.O.3    Ellington, W.R.4    Chapman, M.S.5
  • 41
    • 0021095858 scopus 로고
    • Crystallization and preliminary X-ray diffraction data of two crystal forms of bovine heart creatine kinase
    • Gilliland, G.L., Sjolin, L., and Olsson, G. 1983. Crystallization and preliminary X-ray diffraction data of two crystal forms of bovine heart creatine kinase. J Mol Biol 170:791-793.
    • (1983) J Mol Biol , vol.170 , pp. 791-793
    • Gilliland, G.L.1    Sjolin, L.2    Olsson, G.3
  • 42
    • 0035814912 scopus 로고    scopus 로고
    • Structural changes of mitochondrial creatine kinase upon binding of ADP, ATP, or Pi, observed by reaction-induced infrared difference spectra
    • Granjon, T., Vacheron, M.J., Vial, C., and Buchet, R. 2001. Structural changes of mitochondrial creatine kinase upon binding of ADP, ATP, or Pi, observed by reaction-induced infrared difference spectra. Biochemistry 40:2988-2994.
    • (2001) Biochemistry , vol.40 , pp. 2988-2994
    • Granjon, T.1    Vacheron, M.J.2    Vial, C.3    Buchet, R.4
  • 43
    • 0027724210 scopus 로고
    • Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study
    • Gross, M. and Wallimann, T. 1993. Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study. Biochemistry 32:13933-13940.
    • (1993) Biochemistry , vol.32 , pp. 13933-13940
    • Gross, M.1    Wallimann, T.2
  • 44
    • 0028246759 scopus 로고
    • The tryptophan residues of mitochondrial creatine kinase: Roles of Trp-223, Trp-206, and Trp-264 in active-site and quaternary structure formation
    • Gross, M., Furter-Graves, E.M., Wallimann, T., Eppenberger, H.M., and Furter, R. 1994. The tryptophan residues of mitochondrial creatine kinase: roles of Trp-223, Trp-206, and Trp-264 in active-site and quaternary structure formation. Protein Sci 3:1058-1068.
    • (1994) Protein Sci , vol.3 , pp. 1058-1068
    • Gross, M.1    Furter-Graves, E.M.2    Wallimann, T.3    Eppenberger, H.M.4    Furter, R.5
  • 45
    • 0019888151 scopus 로고
    • The stereochemical course of the reaction catalyzed by creatine kinase
    • Hansen, D. E. and Knowles, J. R. 1981. The stereochemical course of the reaction catalyzed by creatine kinase. J Biol Chem 256:5967-5969.
    • (1981) J Biol Chem , vol.256 , pp. 5967-5969
    • Hansen, D.E.1    Knowles, J.R.2
  • 46
    • 0022974985 scopus 로고
    • Purification and crystallization of creatine kinase from rabbit skeletal muscle
    • Hershenson, S., Helmers, N., Desmueles, P., and Stroud, R. 1986. Purification and crystallization of creatine kinase from rabbit skeletal muscle. J Biol Chem 261:3732-3736.
    • (1986) J Biol Chem , vol.261 , pp. 3732-3736
    • Hershenson, S.1    Helmers, N.2    Desmueles, P.3    Stroud, R.4
  • 47
    • 0034647651 scopus 로고    scopus 로고
    • Why is creatine kinase a dimer? Evidence for cooperativity between the two subunits
    • Hornemann, T., Rutishauser, D., and Wallimann, T. 2000a. Why is creatine kinase a dimer? Evidence for cooperativity between the two subunits. Biochim Biophys Acta 1480:365-373.
    • (2000) Biochim Biophys Acta , vol.1480 , pp. 365-373
    • Hornemann, T.1    Rutishauser, D.2    Wallimann, T.3
  • 49
    • 85013517833 scopus 로고
    • Selective detection of Thr-, Ser-, and Tyr-phosphopeptides in complex digests by electrospray LC-MS
    • Crabb, J.W., Ed., Academic Press, San Diego, CA
    • Huddleston, M.J., Annan, R.S., Bean, M.F., and Carr, S.A. 1994. Selective detection of Thr-, Ser-, and Tyr-phosphopeptides in complex digests by electrospray LC-MS. In: Techniques in Protein Chemistry Vol. 5. pp. 123-130. Crabb, J.W., Ed., Academic Press, San Diego, CA.
    • (1994) Techniques in Protein Chemistry , vol.5 , pp. 123-130
    • Huddleston, M.J.1    Annan, R.S.2    Bean, M.F.3    Carr, S.A.4
  • 50
    • 0014028030 scopus 로고
    • The reaction of nucleotide substrate analogues with adenosine triphosphate-creatine phosphotransferase
    • James, E. and Morrison, J. F. 1966. The reaction of nucleotide substrate analogues with adenosine triphosphate-creatine phosphotransferase. J Biol Chem 241:4758-4770.
    • (1966) J Biol Chem , vol.241 , pp. 4758-4770
    • James, E.1    Morrison, J.F.2
  • 51
    • 0017199256 scopus 로고
    • Binding of adenosine 5′-diphosphate to creatine kinase. An investigation using intermolecular nuclear Overhauser effect measurements
    • James, T.L. 1976. Binding of adenosine 5′-diphosphate to creatine kinase. An investigation using intermolecular nuclear Overhauser effect measurements. Biochemistry. 15:4724-4730.
    • (1976) Biochemistry , vol.15 , pp. 4724-4730
    • James, T.L.1
  • 52
    • 0031469493 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase - A square protein
    • Kabsch, W. and Fritz-Wolf, K. 1997. Mitochondrial creatine kinase-a square protein. Curr Opin Struct Biol 7:811-818.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 811-818
    • Kabsch, W.1    Fritz-Wolf, K.2
  • 53
    • 15944390701 scopus 로고
    • A short N-terminal domain of mitochondrial creatine kinase is involved in octamer formation but not in membrane binding
    • Wirtz, K.W.A., Ed., Plenum Press, Berlin, Germany
    • Kaldis, P., Eppenberger, H.M., and Wallimann, T. 1993. A short N-terminal domain of mitochondrial creatine kinase is involved in octamer formation but not in membrane binding. In: New Developments in Lipid-Protein Interactions and Receptor Function, pp. 199-211. Wirtz, K.W.A., Ed., Plenum Press, Berlin, Germany.
    • (1993) New Developments in Lipid-Protein Interactions and Receptor Function , pp. 199-211
    • Kaldis, P.1    Eppenberger, H.M.2    Wallimann, T.3
  • 54
    • 0027979405 scopus 로고
    • The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization
    • Kaldis, P., Furter, R., and Wallimann, T. 1994. The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization. Biochemistry 33:952-959.
    • (1994) Biochemistry , vol.33 , pp. 952-959
    • Kaldis, P.1    Furter, R.2    Wallimann, T.3
  • 55
    • 2142859139 scopus 로고    scopus 로고
    • Calcium ion coordination: A comparison with that of beryllium, magnesium, and zinc
    • Katz, A.K., Glusker, J.P., Beebe, S.A., and Bock, C.W. 1996. Calcium ion coordination: a comparison with that of beryllium, magnesium, and zinc J Am Chem Soc 118:5752-5763.
    • (1996) J Am Chem Soc , vol.118 , pp. 5752-5763
    • Katz, A.K.1    Glusker, J.P.2    Beebe, S.A.3    Bock, C.W.4
  • 56
    • 0020654939 scopus 로고
    • Creatine kinase: Structure-activity relationships
    • Kenyon, G.L. and Reed, G.H. 1983. Creatine kinase: structure-activity relationships. Adv Enzymol Relat Areas Mol Biol 54:367-426.
    • (1983) Adv Enzymol Relat Areas Mol Biol , vol.54 , pp. 367-426
    • Kenyon, G.L.1    Reed, G.H.2
  • 57
    • 0015358337 scopus 로고
    • Studies on adenosine triphosphate transphosphorylases: XI. Isolation of the crystalline adenosine-triphosphate-creatine transphosphorylases from the muscle and brain of man, calf, and rabbit; and a preparation of their enzymatically active hybrids
    • Keutel, H.J., Okabe, K., Jacobs, H.K., Ziter, F., Maland, L., and Kuby, S.A. 1972. Studies on adenosine triphosphate transphosphorylases: XI. Isolation of the crystalline adenosine-triphosphate-creatine transphosphorylases from the muscle and brain of man, calf, and rabbit; and a preparation of their enzymatically active hybrids. Arch Biochem Biophys 150:648-678.
    • (1972) Arch Biochem Biophys , vol.150 , pp. 648-678
    • Keutel, H.J.1    Okabe, K.2    Jacobs, H.K.3    Ziter, F.4    Maland, L.5    Kuby, S.A.6
  • 58
    • 0002046465 scopus 로고
    • Adenosinetriphosphate-creatine transphosphorylase: I. Isolation of the crystalline enzyme from rabbit muscle
    • Kuby, S.A., Noda, L., and Lardy, H.A. 1954. Adenosinetriphosphate- creatine transphosphorylase: I. Isolation of the crystalline enzyme from rabbit muscle. J Biol Chem 209:191-201.
    • (1954) J Biol Chem , vol.209 , pp. 191-201
    • Kuby, S.A.1    Noda, L.2    Lardy, H.A.3
  • 59
    • 0010360162 scopus 로고
    • ATP-creatine transphosphorylase
    • Boyer, P.D., Ed., Academic Press, New York
    • Kuby, S.A. and Noltmann, E.A. 1962. ATP-creatine transphosphorylase. In: The Enzymes 2 ed. Vol. 6. pp. 515-603. Boyer, P.D., Ed., Academic Press, New York.
    • (1962) The Enzymes 2 Ed. , vol.6 , pp. 515-603
    • Kuby, S.A.1    Noltmann, E.A.2
  • 60
    • 0014774689 scopus 로고
    • Properties and reaction with iodoacetamide of adenosine 5′-triphosphate-creatine phosphotransferase from human skeletal muscle. Further evidence about the role of the essential thiol group in relation to the mechanism of action
    • Kumudavalli, I., Moreland, B.H., and Watts, D.C. 1970. Properties and reaction with iodoacetamide of adenosine 5′-triphosphate-creatine phosphotransferase from human skeletal muscle. Further evidence about the role of the essential thiol group in relation to the mechanism of action. Biochem. J. 117:513-523.
    • (1970) Biochem J , vol.117 , pp. 513-523
    • Kumudavalli, I.1    Moreland, B.H.2    Watts, D.C.3
  • 63
    • 0018696222 scopus 로고
    • eq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions
    • eq of the creatine kinase reaction and other phosphate hydrolyses and phosphate transfer reactions. J Biol Chem 254:6528-6537.
    • (1979) J Biol Chem , vol.254 , pp. 6528-6537
    • Lawson, J.W.1    Veech, R.L.2
  • 64
    • 0039058404 scopus 로고
    • Über die umesterung des adenylsäuresystems mit phosphagenen
    • Lehmann, H. 1936. Über die umesterung des adenylsäuresystems mit phosphagenen. Biochem Z 286:336-343.
    • (1936) Biochem Z , vol.286 , pp. 336-343
    • Lehmann, H.1
  • 65
    • 0019332954 scopus 로고
    • 31P NMR quantitation of the displacement of equilibria of arginine, creatine, pyruvate, and 3-P-glycerate kinase reactions by substitution of sulfur for oxygen in the beta phosphate of ATP
    • 31P NMR quantitation of the displacement of equilibria of arginine, creatine, pyruvate, and 3-P-glycerate kinase reactions by substitution of sulfur for oxygen in the beta phosphate of ATP. J Biol Chem 255:8756-8760.
    • (1980) J Biol Chem , vol.255 , pp. 8756-8760
    • Lerman, C.L.1    Cohn, M.2
  • 67
    • 0021923785 scopus 로고
    • Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: Electron paramagnetic resonance studies with oxygen-17-labeled ligands
    • Leyh, T.S., Goodhart, P.J., Nguyen, A.C., Kenyon, G.L., and Reed, G.H. 1985. Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: electron paramagnetic resonance studies with oxygen-17-labeled ligands. Biochemistry 24:308-316.
    • (1985) Biochemistry , vol.24 , pp. 308-316
    • Leyh, T.S.1    Goodhart, P.J.2    Nguyen, A.C.3    Kenyon, G.L.4    Reed, G.H.5
  • 68
    • 0009502136 scopus 로고
    • Über die enzymatische aufspaltung der kreatinphosphorsaure; zugleich ein beitrag zum Chemismus der muskelkontraktion
    • Lohman, K. 1934. Über die enzymatische aufspaltung der kreatinphosphorsaure; zugleich ein beitrag zum Chemismus der muskelkontraktion. Biochem Z 271:264-277.
    • (1934) Biochem Z , vol.271 , pp. 264-277
    • Lohman, K.1
  • 69
    • 0019321011 scopus 로고
    • Evidence for an associative mechanism in the phosphoryl transfer step catalyzed by rabbit muscle creatine kinase
    • Lowe, G. and Sproat, B.S. 1980. Evidence for an associative mechanism in the phosphoryl transfer step catalyzed by rabbit muscle creatine kinase. J Biol Chem 255:3944-3951.
    • (1980) J Biol Chem , vol.255 , pp. 3944-3951
    • Lowe, G.1    Sproat, B.S.2
  • 70
    • 0017367678 scopus 로고
    • 3-blocked creatine kinase with altered catalytic activity. Kinetic consequences of the presence of the blocking group
    • 3-blocked creatine kinase with altered catalytic activity. Kinetic consequences of the presence of the blocking group. J Biol Chem 252:1202-1207.
    • (1977) J Biol Chem , vol.252 , pp. 1202-1207
    • Maggio, E.T.1    Kenyon, G.L.2    Markham, G.D.3    Reed, G.H.4
  • 71
    • 0000636916 scopus 로고
    • Studies on adenosine triphosphatetransphosphorylases: III. Inhibition reactions
    • Mahowald, T.A., Noltmann, E.A., and Kuby, S.A. 1962. Studies on adenosine triphosphatetransphosphorylases: III. Inhibition reactions. J Biol Chem 237:1535-1548.
    • (1962) J Biol Chem , vol.237 , pp. 1535-1548
    • Mahowald, T.A.1    Noltmann, E.A.2    Kuby, S.A.3
  • 72
    • 0018800396 scopus 로고
    • Affinity labeling of creatine kinase by N-(2,3-epoxypropyl)-N- amidinoglycine
    • Marletta, M.A., and Kenyon, G.L. 1979. Affinity labeling of creatine kinase by N-(2,3-epoxypropyl)-N-amidinoglycine. J Biol Chem 254: 1879.
    • (1979) J Biol Chem , vol.254 , pp. 1879
    • Marletta, M.A.1    Kenyon, G.L.2
  • 73
    • 0344391933 scopus 로고    scopus 로고
    • --creatine transition state analogue complex as detected by hydrogen/deuterium exchange
    • --creatine transition state analogue complex as detected by hydrogen/deuterium exchange. Biochemistry 42:13595-13604.
    • (2003) Biochemistry , vol.42 , pp. 13595-13604
    • Mazon, H.1    Marcillat, O.2    Forest, E.3    Vial, C.4
  • 74
    • 0015501464 scopus 로고
    • Specificity of creatine kinase for guanidino substrates. Kinetic and proton nuclear magnetic relaxation rate studies
    • McLaughlin, A.C., Cohn, M., and Kenyon, G.L. 1972. Specificity of creatine kinase for guanidino substrates. Kinetic and proton nuclear magnetic relaxation rate studies. J Biol Chem 247:4382-4388.
    • (1972) J Biol Chem , vol.247 , pp. 4382-4388
    • McLaughlin, A.C.1    Cohn, M.2    Kenyon, G.L.3
  • 75
    • 0017180105 scopus 로고
    • Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. Implications for substrate specificity and catalytic mechanism
    • McLaughlin, A.C., Leigh, J.S., Jr., and Cohn, M. 1976. Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. Implications for substrate specificity and catalytic mechanism. J Biol Chem 251:2777-2787.
    • (1976) J Biol Chem , vol.251 , pp. 2777-2787
    • McLaughlin, A.C.1    Leigh Jr., J.S.2    Cohn, M.3
  • 76
    • 0015805738 scopus 로고
    • A preliminary crystallographic investigation of rabbit muscle creatine kinase
    • McPherson, A., Jr. 1973. A preliminary crystallographic investigation of rabbit muscle creatine kinase. J Mol Biol 81:83-86.
    • (1973) J Mol Biol , vol.81 , pp. 83-86
    • McPherson Jr., A.1
  • 77
    • 0022336833 scopus 로고
    • Tryptophan residues of creatine kinase: A fluorescence study
    • Messmer, C.H. and Kagi, J.H. 1985. Tryptophan residues of creatine kinase: a fluorescence study. Biochemistry 24:7172-7178.
    • (1985) Biochemistry , vol.24 , pp. 7172-7178
    • Messmer, C.H.1    Kagi, J.H.2
  • 78
    • 0015052797 scopus 로고
    • Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate anion complexes
    • Milner-White, E.J. and Watts, D.C. 1971. Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate anion complexes. Biochem J 122:727-740.
    • (1971) Biochem J , vol.122 , pp. 727-740
    • Milner-White, E.J.1    Watts, D.C.2
  • 79
    • 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
  • 80
    • 0014010187 scopus 로고
    • Isotope exchange studies of the mechanism of the reaction catalyzed by adenosine triphosphate: Creatine phosphotransferase
    • Morrison, J.F. and Cleland, W.W. 1966. Isotope exchange studies of the mechanism of the reaction catalyzed by adenosine triphosphate: creatine phosphotransferase. J Biol Chem 241:673-683.
    • (1966) J Biol Chem , vol.241 , pp. 673-683
    • Morrison, J.F.1    Cleland, W.W.2
  • 81
    • 0014180427 scopus 로고
    • Isotope exchange studies of the reaction catalyzed by ATP: Creatine phosphotransferase
    • Morrison, J.F. and White, A. 1967. Isotope exchange studies of the reaction catalyzed by ATP: creatine phosphotransferase. Eur J Biochem 3:145-152.
    • (1967) Eur J Biochem , vol.3 , pp. 145-152
    • Morrison, J.F.1    White, A.2
  • 82
    • 77956932220 scopus 로고
    • Arginine kinase and other invertebrate guanidino kinases
    • Boyer, P.D., Ed., Academic Press, New York., NY
    • Morrison, J. F. 1973. Arginine kinase and other invertebrate guanidino kinases. In: The Enzymes. Vol. 8. pp. 457-486. Boyer, P.D., Ed., Academic Press, New York., NY.
    • (1973) The Enzymes , vol.8 , pp. 457-486
    • Morrison, J.F.1
  • 83
    • 0034625687 scopus 로고    scopus 로고
    • Creatine kinase isoenzymes specificities: Histidine 65 in human CK-BB, a role in protein stability, not in catalysis
    • Mourad-Terzian, T., Steghens, J.P., Min, K.L., Collombel, C., and Bozon, D. 2000. Creatine kinase isoenzymes specificities: histidine 65 in human CK-BB, a role in protein stability, not in catalysis. FEBS Lett 475:22-26.
    • (2000) FEBS Lett , vol.475 , pp. 22-26
    • Mourad-Terzian, T.1    Steghens, J.P.2    Min, K.L.3    Collombel, C.4    Bozon, D.5
  • 85
    • 0029664419 scopus 로고    scopus 로고
    • Evolution of the creatine kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene
    • Mühlebach, S.M., Wirz, T., Brandle, U., and Perriard, J.C. 1996. Evolution of the creatine kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene. J Biol Chem 271:11920-11929.
    • (1996) J Biol Chem , vol.271 , pp. 11920-11929
    • Mühlebach, S.M.1    Wirz, T.2    Brandle, U.3    Perriard, J.C.4
  • 88
    • 0012533250 scopus 로고
    • Kinetic properties and equilibrium constant of the adenosine triphosphate-creatine transphosphorylase-catalyzed reaction
    • Nihei, T., Noda, L., and Morales, M.F. 1961. Kinetic properties and equilibrium constant of the adenosine triphosphate-creatine transphosphorylase- catalyzed reaction. J Biol Chem 236:3203-3209.
    • (1961) J Biol Chem , vol.236 , pp. 3203-3209
    • Nihei, T.1    Noda, L.2    Morales, M.F.3
  • 89
    • 15944367163 scopus 로고
    • The enzymatic activity and inhibition of adenosine 5′-triphosphate- creatine transphosphorylase
    • Noda, L., Nihei, T., and Morales, M.F. 1960. The enzymatic activity and inhibition of adenosine 5′-triphosphate-creatine transphosphorylase. J Biol Chem 235:2830-2834.
    • (1960) J Biol Chem , vol.235 , pp. 2830-2834
    • Noda, L.1    Nihei, T.2    Morales, M.F.3
  • 90
    • 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
  • 91
    • 0000479830 scopus 로고
    • A spectrophotometric method for the determination of creatine phosphokinase and myokinase
    • Oliver, I.T. 1955. A spectrophotometric method for the determination of creatine phosphokinase and myokinase. Biochem J 61:116-122.
    • (1955) Biochem J , vol.61 , pp. 116-122
    • Oliver, I.T.1
  • 92
    • 0014967206 scopus 로고
    • Le dichroism circulaire de diverses phosphagène phosphotransférases
    • Oriol, C. and Landon, M.F. 1970. Le dichroism circulaire de diverses phosphagène phosphotransférases. Biochim Biophys Acta 214:455-462.
    • (1970) Biochim Biophys Acta , vol.214 , pp. 455-462
    • Oriol, C.1    Landon, M.F.2
  • 93
    • 15944363203 scopus 로고
    • The effect of trace metal contaminants and EDTA on the velocity of enzyme-catalysed reactions. Studies on ATP:creatine phosphotransferase
    • O'Sullivan, W.J., and Morrison, L.F. 1963. The effect of trace metal contaminants and EDTA on the velocity of enzyme-catalysed reactions. Studies on ATP:creatine phosphotransferase. Biochim Biophys Acta 77:142-144.
    • (1963) Biochim Biophys Acta , vol.77 , pp. 142-144
    • O'Sullivan, W.J.1    Morrison, L.F.2
  • 94
    • 0042127916 scopus 로고
    • The effect of magnesium on the reactivity of the essential sulphydryl groups in creatine kinase-substrate complexes
    • O'Sullivan, W.J., Diefenbach, H., and Cohn, M. 1966. The effect of magnesium on the reactivity of the essential sulphydryl groups in creatine kinase-substrate complexes. Biochemistry 5:2666-2673.
    • (1966) Biochemistry , vol.5 , pp. 2666-2673
    • O'Sullivan, W.J.1    Diefenbach, H.2    Cohn, M.3
  • 95
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner, N. and Geissler, A. 2001. Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2:339-349.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 96
    • 0001146990 scopus 로고
    • Stereospecificity of creatine kinase, crystal structure of 1-carboxymethyl-2-imino-3-phosphonoimidazolidine
    • Phillips, G.N., Jr., Thomas, J.W., Annesley, T.M., and Quiocho, F.A. 1979. Stereospecificity of creatine kinase, crystal structure of 1-carboxymethyl-2-imino-3-phosphonoimidazolidine. J Am Chem Soc 101:7120-7121.
    • (1979) J Am Chem Soc , vol.101 , pp. 7120-7121
    • Phillips Jr., G.N.1    Thomas, J.W.2    Annesley, T.M.3    Quiocho, F.A.4
  • 97
    • 2642583778 scopus 로고    scopus 로고
    • Structural and functional implications of the amino acid sequences of dimeric, cytoplasmic and octameric mitochondrial creatine kinases from a protostome invertebrate
    • Pineda, A.O., Jr., and Ellington, W.R. 1999. Structural and functional implications of the amino acid sequences of dimeric, cytoplasmic and octameric mitochondrial creatine kinases from a protostome invertebrate. Eur J Biochem 264:67-73.
    • (1999) Eur J Biochem , vol.264 , pp. 67-73
    • Pineda Jr., A.O.1    Ellington, W.R.2
  • 98
    • 0014406934 scopus 로고
    • The active site of ATP:guadinine phosphotransferases.II. Evidence for a critical histidine residue through use of a specific reagent, diethylpyrocarbonate
    • Pradel, L.-A., and Kassab, R. 1968. The active site of ATP:guadinine phosphotransferases.II. Evidence for a critical histidine residue through use of a specific reagent, diethylpyrocarbonate. Biochim Biophys Acta 167:317-325.
    • (1968) Biochim Biophys Acta , vol.167 , pp. 317-325
    • Pradel, L.-A.1    Kassab, R.2
  • 99
    • 0017089507 scopus 로고
    • Non-identical behaviour of the subunits of rabbit muscule creatine kinase
    • Price, N.C. and Hunter, M.G. 1976. Non-identical behaviour of the subunits of rabbit muscule creatine kinase. Biochim Biophys Acta 445:364-376.
    • (1976) Biochim Biophys Acta , vol.445 , pp. 364-376
    • Price, N.C.1    Hunter, M.G.2
  • 101
    • 0031656509 scopus 로고    scopus 로고
    • Molecular characterization of the creatine kinases and some historical perspectives
    • Qin, W., Khuchua, Z., Cheng, J., Boero, J., Payne, R.M., and Strauss, A.W. 1998. Molecular characterization of the creatine kinases and some historical perspectives. Mol Cell Biochem 184:153-167.
    • (1998) Mol Cell Biochem , vol.184 , pp. 153-167
    • Qin, W.1    Khuchua, Z.2    Cheng, J.3    Boero, J.4    Payne, R.M.5    Strauss, A.W.6
  • 102
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao, J.K., Bujacz, G., and Wiodawer, 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    Wiodawer, A.3
  • 103
    • 0015523053 scopus 로고
    • Structural changes induced by substrates and anions at the active site of creatine kinase. Electron paramagnetic resonance and nuclear magnetic relaxation rate studies of the manganous complexes
    • Reed, G.H. and Cohn, M. 1972. Structural changes induced by substrates and anions at the active site of creatine kinase. Electron paramagnetic resonance and nuclear magnetic relaxation rate studies of the manganous complexes. J Biol Chem 247:3073-3081.
    • (1972) J Biol Chem , vol.247 , pp. 3073-3081
    • Reed, G.H.1    Cohn, M.2
  • 104
    • 0015693270 scopus 로고
    • Structural studies of transition state analog complexes of creatine kinase
    • Reed, G.H. and McLaughlin, A.C. 1973. Structural studies of transition state analog complexes of creatine kinase. Ann NY Acad Sci 222:118-129.
    • (1973) Ann NY Acad Sci , vol.222 , pp. 118-129
    • Reed, G.H.1    McLaughlin, A.C.2
  • 105
    • 0017898552 scopus 로고
    • Investigations of anion binding sites in transition state analogue complexes of creatine kinase by infrared spectroscopy
    • Reed, G.H., Barlow, C.H., and Burns, R.A., Jr. 1978. Investigations of anion binding sites in transition state analogue complexes of creatine kinase by infrared spectroscopy. J Biol Chem 253:4153-4158.
    • (1978) J Biol Chem , vol.253 , pp. 4153-4158
    • Reed, G.H.1    Barlow, C.H.2    Burns Jr., R.A.3
  • 106
    • 0019333224 scopus 로고
    • Identification of the six ligands to manganese(II) in transition-state-analogue complexes of creatine kinase: Oxygen-17 superhyperfine coupling from selectively labeled ligands
    • Reed, G.H., and Leyh, T.S. 1980. Identification of the six ligands to manganese(II) in transition-state-analogue complexes of creatine kinase: oxygen-17 superhyperfine coupling from selectively labeled ligands. Biochemistry 19:5472-5480.
    • (1980) Biochemistry , vol.19 , pp. 5472-5480
    • Reed, G.H.1    Leyh, T.S.2
  • 107
    • 0005114932 scopus 로고
    • Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens
    • Robin, Y. 1964. Biological distribution of guanidines and phosphagens in marine annelida and related phyla from California, with a note on pluriphosphagens. Comp Biochem Physiol 12:347-367.
    • (1964) Comp Biochem Physiol , vol.12 , pp. 347-367
    • Robin, Y.1
  • 108
    • 0026035373 scopus 로고
    • Interaction of mitochondrial creatine kinase with model membranes. A monolayer study
    • Rojo, M., Hovius, R., Demel, R., Wallimann, T., Eppenberger, H. M., and Nicolay, K. 1991. Interaction of mitochondrial creatine kinase with model membranes. A monolayer study. FEBS Lett 281:123-129.
    • (1991) FEBS Lett , vol.281 , pp. 123-129
    • Rojo, M.1    Hovius, R.2    Demel, R.3    Wallimann, T.4    Eppenberger, H.M.5    Nicolay, K.6
  • 109
    • 0014077032 scopus 로고
    • An improved procedure for serum creatine phosphokinase determination
    • Rosalki, S.B. 1967. An improved procedure for serum creatine phosphokinase determination. J Lab Clin Med 696-705.
    • (1967) J Lab Clin Med , pp. 696-705
    • Rosalki, S.B.1
  • 110
    • 0019879376 scopus 로고
    • Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase
    • Rosevear, P.R., Desmeules, P., Kenyon, G.L., and Mildvan, A.S. 1981. Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase. Biochemistry 20:6155-6164.
    • (1981) Biochemistry , vol.20 , pp. 6155-6164
    • Rosevear, P.R.1    Desmeules, P.2    Kenyon, G.L.3    Mildvan, A.S.4
  • 111
    • 0015234223 scopus 로고
    • On the specificity of creatine kinase. New glycocyamines and glycocyamine analogs related to creatine
    • Rowley, G.L., Greenleaf, A.L., and Kenyon, G.L. 1971. On the specificity of creatine kinase. New glycocyamines and glycocyamine analogs related to creatine. J Am Chem Soc 93:5542-5551.
    • (1971) J Am Chem Soc , vol.93 , pp. 5542-5551
    • Rowley, G.L.1    Greenleaf, A.L.2    Kenyon, G.L.3
  • 112
    • 0003675548 scopus 로고
    • Cellular bioenergetics; role of coupled creatine kinases
    • Saks, V.A. and Ventura-Clapier, R. 1994. Cellular bioenergetics; Role of coupled creatine kinases. Mol Cell Biochem 133/134.
    • (1994) Mol Cell Biochem , vol.133-134
    • Saks, V.A.1    Ventura-Clapier, R.2
  • 113
    • 0015743403 scopus 로고
    • Inhibition of creatine kinase by chromium nucleotides
    • Schimerlik, M.I. and Cleland, W.W. 1973. Inhibition of creatine kinase by chromium nucleotides. J Biol Chem. 248:8418-8423.
    • (1973) J Biol Chem , vol.248 , pp. 8418-8423
    • Schimerlik, M.I.1    Cleland, W.W.2
  • 114
    • 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
  • 115
    • 0034536628 scopus 로고    scopus 로고
    • Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes
    • Schlattner, U., Eder, M., Dolder, M., Khuchua, Z.A., Strauss, A.W., and Wallimann, T. 2000. Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes. Biol Chem 381:1063-1070.
    • (2000) Biol Chem , vol.381 , pp. 1063-1070
    • Schlattner, U.1    Eder, M.2    Dolder, M.3    Khuchua, Z.A.4    Strauss, A.W.5    Wallimann, T.6
  • 117
    • 0025687007 scopus 로고
    • Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle
    • Schnyder, T., Sargent, D.F., Richmond, T.J., Eppenberger, H.M., and Wallimann, T. 1990. Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle. J Mol Biol 216:809-812.
    • (1990) J Mol Biol , vol.216 , pp. 809-812
    • Schnyder, T.1    Sargent, D.F.2    Richmond, T.J.3    Eppenberger, H.M.4    Wallimann, T.5
  • 118
    • 0025754308 scopus 로고
    • Crystallization of mitochondrial creatine kinase. Growing of large protein crystals and electron microscopic investigation of microcrystals consisting of octamers
    • Schnyder, T., Winkler, H., Gross, H., Eppenberger, H.M., and Wallimann, T. 1991. Crystallization of mitochondrial creatine kinase. Growing of large protein crystals and electron microscopic investigation of microcrystals consisting of octamers. J Biol Chem 266:5318-5322.
    • (1991) J Biol Chem , vol.266 , pp. 5318-5322
    • Schnyder, T.1    Winkler, H.2    Gross, H.3    Eppenberger, H.M.4    Wallimann, T.5
  • 121
    • 0016243367 scopus 로고
    • Nonessentiality of the active sulfhydryl group of rabbit muscle creatine kinase
    • Smith, D.J. and Kenyon, G.I. 1974. Nonessentiality of the active sulfhydryl group of rabbit muscle creatine kinase J Biol Chem 249:3317-3318.
    • (1974) J Biol Chem , vol.249 , pp. 3317-3318
    • Smith, D.J.1    Kenyon, G.I.2
  • 122
    • 1942439849 scopus 로고    scopus 로고
    • Cloning and expression of mitochondrial and protoflagellar creatine kinases from a marine sponge: Implications for the origin of intracellular energy transport systems
    • Sona, S., Suzuki, T., and Ellington, W.R. 2004. Cloning and expression of mitochondrial and protoflagellar creatine kinases from a marine sponge: implications for the origin of intracellular energy transport systems. Biochem. Biophys Res Commun 317:1207-1214.
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 1207-1214
    • Sona, S.1    Suzuki, T.2    Ellington, W.R.3
  • 123
    • 0029888809 scopus 로고    scopus 로고
    • Expression of horseshoe crab arginine kinase in Escherichia coli and site-directed mutations of the reactive cysteine peptide
    • Strong, S.J., and Ellington, W.R. 1996. Expression of horseshoe crab arginine kinase in Escherichia coli and site-directed mutations of the reactive cysteine peptide. Comp. Biochem. Physiol. B Biochem Mol Biol 113:809-816.
    • (1996) Comp Biochem Physiol B Biochem Mol Biol , vol.113 , pp. 809-816
    • Strong, S.J.1    Ellington, W.R.2
  • 124
    • 0029992890 scopus 로고    scopus 로고
    • Balancing ATP in the cell
    • Stroud, R.M. 1996. Balancing ATP in the cell. Nat Struct Biol. 3:567-569.
    • (1996) Nat Struct Biol , vol.3 , pp. 567-569
    • Stroud, R.M.1
  • 125
    • 0000516638 scopus 로고
    • Synthesis of and structural assignments for some N-phosphono-2- iminoimidazolidines (cyclic guanidines)
    • Struve, G.E., Gazzola, C., and Kenyon, G.L. 1977. Synthesis of and structural assignments for some N-phosphono-2-iminoimidazolidines (cyclic guanidines). J Org Chem 42:4035-4040.
    • (1977) J Org Chem , vol.42 , pp. 4035-4040
    • Struve, G.E.1    Gazzola, C.2    Kenyon, G.L.3
  • 126
    • 0031555335 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
    • Suzuki, T., Kawasaki, Y., Furukohri, T., and Ellington, W.R. 1997. Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site. Biochim. Biophys Acta 1343:152-159.
    • (1997) Biochim Biophys Acta , vol.1343 , pp. 152-159
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3    Ellington, W.R.4
  • 127
    • 0032517306 scopus 로고    scopus 로고
    • Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases: A two-domain arginine kinase from the clam Pseudocardium sachalinensis
    • Suzuki, T., Kawasaki, Y., Unemi, Y., Nishimura, Y., Soga, T., Kamidochi, M., Yazawa, Y., and Furukohri, T. 1998. Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases: a two-domain arginine kinase from the clam Pseudocardium sachalinensis. Biochim Biophys Acta 1388:253-259.
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 253-259
    • Suzuki, T.1    Kawasaki, Y.2    Unemi, Y.3    Nishimura, Y.4    Soga, T.5    Kamidochi, M.6    Yazawa, Y.7    Furukohri, T.8
  • 128
    • 4344597786 scopus 로고    scopus 로고
    • Evolution and divergence of the genes for cytoplasmic, mitochondrial, and flagellar creatine kinases
    • Suzuki, T., Mizuta, C., Uda, K., Ishida, K., Mizuta, K., Sona, S., Compaan, D.M., and Ellington, W.R. 2004. Evolution and divergence of the genes for cytoplasmic, mitochondrial, and flagellar creatine kinases. J Mol Evol 59:218-226.
    • (2004) J Mol Evol , vol.59 , pp. 218-226
    • Suzuki, T.1    Mizuta, C.2    Uda, K.3    Ishida, K.4    Mizuta, K.5    Sona, S.6    Compaan, D.M.7    Ellington, W.R.8
  • 129
    • 0019561269 scopus 로고
    • Crystallization and properties of creatine kinase from equine skeletal muscle
    • Takasawa, T., Fukushi, K., and Shiokawa, H. 1981. Crystallization and properties of creatine kinase from equine skeletal muscle. J Biochem 89:1619-1631.
    • (1981) J Biochem , vol.89 , pp. 1619-1631
    • Takasawa, T.1    Fukushi, K.2    Shiokawa, H.3
  • 130
    • 0000185297 scopus 로고
    • Creatine and creatine kinase measurement
    • Tanzer, M.L. and Gilvarg, C.J. 1959. Creatine and creatine kinase measurement. J Biol Chem 234:3201-3204.
    • (1959) J Biol Chem , vol.234 , pp. 3201-3204
    • Tanzer, M.L.1    Gilvarg, C.J.2
  • 131
    • 0035121731 scopus 로고    scopus 로고
    • The three-dimensional structure of cytosolic bovine retinal creatine kinase
    • Tisi, D., Bax, B., and Loew, A. 2001. The three-dimensional structure of cytosolic bovine retinal creatine kinase. Acta Crystallogr D Biol Crystallogr 57:187-193.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 187-193
    • Tisi, D.1    Bax, B.2    Loew, A.3
  • 132
    • 4344563957 scopus 로고    scopus 로고
    • Role of amino acid residues on the GS region of Stichopus arginine kinase and Danio creatine kinase
    • Uda, K. and Suzuki, T. 2004. Role of amino acid residues on the GS region of Stichopus arginine kinase and Danio creatine kinase. Protein J 23:53-64.
    • (2004) Protein J , vol.23 , pp. 53-64
    • Uda, K.1    Suzuki, T.2
  • 133
    • 0031571603 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase interaction with phospholipid vesicles
    • Vacheron, M.J., Glottes, E., Chautard, C., and Vial, C. 1997. Mitochondrial creatine kinase interaction with phospholipid vesicles. Arch Biochem Biophys 344:316-324.
    • (1997) Arch Biochem Biophys , vol.344 , pp. 316-324
    • Vacheron, M.J.1    Glottes, E.2    Chautard, C.3    Vial, C.4
  • 134
    • 0018789695 scopus 로고
    • Creatine kinase. Nuclear magnetic resonance and fluorescence evidence for interaction of adenosine 5′-diphosphate with aromatic residues
    • Vasák, M., Nagayama, K., Wüthrich, K., Mertens, M., and Kägi, J.H.R. 1979. Creatine kinase. Nuclear magnetic resonance and fluorescence evidence for interaction of adenosine 5′-diphosphate with aromatic residues. Biochemistry 18:5050-5055.
    • (1979) Biochemistry , vol.18 , pp. 5050-5055
    • Vasák, M.1    Nagayama, K.2    Wüthrich, K.3    Mertens, M.4    Kägi, J.H.R.5
  • 135
    • 0026585611 scopus 로고
    • Intracellularcompartmentation, 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. Intracellularcompartmentation, 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
  • 136
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pKa for Cys282 in the active site of human muscle creatine kinase
    • Wang, P.F., McLeish, M.J., Kneen, M.M., Lee, G., and Kenyon, G.L. 2001. An unusually low pKa for Cys282 in the active site of human muscle creatine kinase. Biochemistry 40:11698-11705.
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 137
    • 0025701673 scopus 로고
    • Is the subunit the minimal functional unit of creatine kinase?
    • Wang, X.C., Zhou, H.M., Wang, Z.X., and Tsou, C.L. 1990. Is the subunit the minimal functional unit of creatine kinase? Biochim Biophys Acta 1039:313-317.
    • (1990) Biochim Biophys Acta , vol.1039 , pp. 313-317
    • Wang, X.C.1    Zhou, H.M.2    Wang, Z.X.3    Tsou, C.L.4
  • 138
    • 0029894582 scopus 로고    scopus 로고
    • Kinetic differentiation between ligand-induced and pre-existent asymmetric models
    • Wang, Z.X. and Pan, X.M. 1996. Kinetic differentiation between ligand-induced and pre-existent asymmetric models. FEBS Lett 388:73-75.
    • (1996) FEBS Lett , vol.388 , pp. 73-75
    • Wang, Z.X.1    Pan, X.M.2
  • 139
    • 0000833663 scopus 로고
    • A study of the 'reactive' sulphydryl groups of adenosine 5′-triophosphate-creatine phosphotransferase
    • Watts, D.C. and Rabin, B.R. 1962. A study of the 'reactive' sulphydryl groups of adenosine 5′-triophosphate-creatine phosphotransferase. Biochem J 85:507-516.
    • (1962) Biochem J , vol.85 , pp. 507-516
    • Watts, D.C.1    Rabin, B.R.2
  • 140
    • 0002052737 scopus 로고
    • The origin and evolution of the phosphagen phosphotransferases
    • van Thoai, N. and Roche, J., Eds., Gordon & Breach, New York, NY
    • Watts, D.C. 1968. The origin and evolution of the phosphagen phosphotransferases. In: Homologous Enzymes and Biochemical Evolution pp. 279-296. van Thoai, N. and Roche, J., Eds., Gordon & Breach, New York, NY.
    • (1968) Homologous Enzymes and Biochemical Evolution , pp. 279-296
    • Watts, D.C.1
  • 141
    • 0002640823 scopus 로고
    • Evolution of phosphagen kinases
    • Schoffeneils, E., Ed., North-Holland Publishing Co., Amsterdam, The Netherlands
    • Watts, D.C. 1971. Evolution of phosphagen kinases. In: Biochemical Evolution and the Origin of Life. pp. 150-173. Schoffeneils, E., Ed., North-Holland Publishing Co., Amsterdam, The Netherlands.
    • (1971) Biochemical Evolution and the Origin of Life , pp. 150-173
    • Watts, D.C.1
  • 142
    • 77956904558 scopus 로고
    • Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase)
    • Boyer, P.D., Ed., Academic Press, New York, NY
    • Watts, D.C. 1973. Creatine kinase (adenosine 5′-triphosphate- creatine phosphotransferase). In: The Enzymes. Vol. 8. pp. 383-455. Boyer, P.D., Ed., Academic Press, New York, NY.
    • (1973) The Enzymes , vol.8 , pp. 383-455
    • Watts, D.C.1
  • 143
    • 0001684572 scopus 로고
    • Evolution of phosphagen kinases in the chordate line
    • Watts, D.C. 1975. Evolution of phosphagen kinases in the chordate line. Symp Zool Soc Lond 36:105-127.
    • (1975) Symp Zool Soc Lond , vol.36 , pp. 105-127
    • Watts, D.C.1
  • 144
    • 0025287976 scopus 로고
    • The phosphocreatine shuttle of sea urchin sperm: Flagellar creatine kinase resulted from gene triplication
    • Wothe, D.D., Charbonneau, H., and Shapiro, B.M. 1990. The phosphocreatine shuttle of sea urchin sperm: Flagellar creatine kinase resulted from gene triplication. Proc Natl Acad Sci. USA 87:5203-5207.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5203-5207
    • Wothe, D.D.1    Charbonneau, H.2    Shapiro, B.M.3
  • 145
    • 0024410068 scopus 로고
    • Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation
    • Wu, H., Yao, Q.Z., and Tsou, C.L. 1989. Creatine kinase is modified by 2-chloromercuri-4-nitrophenol at the active site thiols with complete inactivation. Biochim Biophys Acta 997:78-92.
    • (1989) Biochim Biophys Acta , vol.997 , pp. 78-92
    • Wu, H.1    Yao, Q.Z.2    Tsou, C.L.3
  • 146
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: A key enzyme of aerobic energy metabolism
    • Wyss, M., Smeitink, J., Wevers, R.A., and Wallimann, T. 1992. Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism. Biochim Biophys Acta 1102:119-166.
    • (1992) Biochim Biophys Acta , vol.1102 , pp. 119-166
    • Wyss, M.1    Smeitink, J.2    Wevers, R.A.3    Wallimann, T.4
  • 147
    • 0027255880 scopus 로고
    • Selective labelling and inactivation of creatine kinase isoenzymes by the thyroid hormone derivative N-bromoacetyl-3,3′,5-tri-iodo-L- thyronine
    • Wyss, M., Wallimann, T., and Kohrle, J. 1993. Selective labelling and inactivation of creatine kinase isoenzymes by the thyroid hormone derivative N-bromoacetyl-3,3′,5-tri-iodo-L- thyronine Biochem J 291:463-472.
    • (1993) Biochem J , vol.291 , pp. 463-472
    • Wyss, M.1    Wallimann, T.2    Kohrle, J.3
  • 148
    • 0036898567 scopus 로고    scopus 로고
    • Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: Mechanistic insights
    • Yousef, M.S., Fabiola, F., Gattis, J.L., Somasundaram, T., and Chapman, M.S. 2002. Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights. Acta Crystallogr D Biol Crystallogr 58:2009-2017.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 2009-2017
    • Yousef, M.S.1    Fabiola, F.2    Gattis, J.L.3    Somasundaram, T.4    Chapman, M.S.5
  • 149
    • 12244270354 scopus 로고    scopus 로고
    • Induced fit in guanidino kinases-comparison of substrate-free and transition state analog structures of arginine kinase
    • Yousef, M.S., Clark, S.A., Pruett, P.K., Somasundaram, T., Ellington, W.R., and Chapman, M.S. 2003. Induced fit in guanidino kinases-comparison of substrate-free and transition state analog structures of arginine kinase. Protein Sci 12:103-111.
    • (2003) Protein Sci , vol.12 , pp. 103-111
    • Yousef, M.S.1    Clark, S.A.2    Pruett, P.K.3    Somasundaram, T.4    Ellington, W.R.5    Chapman, M.S.6
  • 151
    • 0034054987 scopus 로고    scopus 로고
    • Induced fit in arginine kinase
    • Zhou, G., Ellington, W.R., and Chapman, M.S. 2000. Induced fit in arginine kinase. Biophys J 78:1541-1550.
    • (2000) Biophys J , vol.78 , pp. 1541-1550
    • Zhou, G.1    Ellington, W.R.2    Chapman, M.S.3
  • 152
    • 0023065318 scopus 로고
    • The presence of reactive SH groups in enzymatically active dicyano derivative of creatine kinase
    • Zhou, H.M. and Tsou, C.L. 1987. The presence of reactive SH groups in enzymatically active dicyano derivative of creatine kinase. Biochim Biophys Acta 911:136-143.
    • (1987) Biochim Biophys Acta , vol.911 , pp. 136-143
    • Zhou, H.M.1    Tsou, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.