메뉴 건너뛰기




Volumn 6, Issue 2, 1997, Pages 331-339

The active site histidines of creatine kinase. A critical role of His 61 situated on a flexible loop

Author keywords

acid base catalysis; active site; creatine kinase; enzyme mechanism; guanidino kinases

Indexed keywords

CREATINE KINASE; HISTIDINE;

EID: 0342460542     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060208     Document Type: Article
Times cited : (27)

References (44)
  • 3
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon DJ, Anderson WF. 1988. A fast algorithm for rendering space-filling molecule pictures. J Mol Graphics 6:219-220.
    • (1988) J Mol Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000246042 scopus 로고
    • Simulated annealing in crystallography
    • Brünger AT. 1991. Simulated annealing in crystallography. Anna Rev Phys Chem 42:197-223.
    • (1991) Anna Rev Phys Chem , vol.42 , pp. 197-223
    • Brünger, A.T.1
  • 6
    • 0029894773 scopus 로고    scopus 로고
    • Rabbit muscle creatine kinase: Consequences of the mutagenesis of conserved histidine residues
    • Chen LH, Borders CL, Vásquez JR, Kenyon GL. 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, C.L.2    Vásquez, J.R.3    Kenyon, G.L.4
  • 7
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland WW. 1979. Statistical analysis of enzyme kinetic data. Methods Enzymol 63:103-138.
    • (1979) Methods Enzymol , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 8
    • 0019509122 scopus 로고
    • Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase
    • Cook PF, Kenyon GL, Cleland WW. 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
  • 9
    • 0028902065 scopus 로고
    • Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
    • First EA, Fersht AR. 1995. Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry 34: 5030-5043.
    • (1995) Biochemistry , vol.34 , pp. 5030-5043
    • First, E.A.1    Fersht, A.R.2
  • 10
    • 0030606976 scopus 로고    scopus 로고
    • Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering
    • Forstner M, Kriechbaum M, Laggner P, Wallimann T. 1996. Changes of 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
  • 13
    • 0027268548 scopus 로고
    • Creatine kinase: The reactive cysteine is required for synergism but is nonessential for catalysis
    • Furter R, Furter-Graves EM, 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
  • 14
    • 0024454018 scopus 로고
    • Aluminum-adenine nucleotides as alternate substrates for creatine kinase
    • Furumo NC, Viola RE. 1989. Aluminum-adenine nucleotides as alternate substrates for creatine kinase. Arch Biochem Biophys 275:33-39.
    • (1989) Arch Biochem Biophys , vol.275 , pp. 33-39
    • Furumo, N.C.1    Viola, R.E.2
  • 15
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter O. 1977. A new method for the evaluation of small-angle scattering data. J Appl Cryst 10:415-421.
    • (1977) J Appl Cryst , vol.10 , pp. 415-421
    • Glatter, O.1
  • 16
    • 0028246759 scopus 로고
    • The tryptophane residues of mitochondrial creatine kinase: Roles ot Trp-223, Trp-206, and Trp-264 in active-site and quaternary structure formation
    • Gross M, Furter-Graves EM, Wallimann T, Eppenberger HM, Furter R. 1994. The tryptophane residues of mitochondrial creatine kinase: Roles ot 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
  • 18
    • 0002417327 scopus 로고
    • Instrumentation. Experimental technique, slit collimation
    • Glatter O, Kratky O, eds. London, UK: Academic Press Inc.
    • Kratky O. 1982. Instrumentation. Experimental technique, slit collimation. In: Glatter O, Kratky O, eds. Small angle X-ray scattering. London, UK: Academic Press Inc. pp 53-83.
    • (1982) Small Angle X-ray Scattering , pp. 53-83
    • Kratky, O.1
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0025702022 scopus 로고
    • 31P-NMR magnetization transfer and radioisotope exchange methods for assessment of an enzyme reaction mechanism: Rate-determining steps of the creatine kinase reaction
    • 31P-NMR magnetization transfer and radioisotope exchange methods for assessment of an enzyme reaction mechanism: Rate-determining steps of the creatine kinase reaction. Biochim Biophys Acta 1020:290-304.
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 290-304
    • Kupriyanov, V.V.1    Balaban, R.S.2    Lyulina, N.V.3    Steinschneider, A.Y.4    Saks, V.A.5
  • 21
    • 0025068606 scopus 로고
    • Transition-state analogues in protein crystallography: Probes of the structural source of enzyme catalysis
    • Lolis E, Petsko GA. 1990. Transition-state analogues in protein crystallography: Probes of the structural source of enzyme catalysis. Anna Rev Biochem 59:597-630.
    • (1990) Anna Rev Biochem , vol.59 , pp. 597-630
    • Lolis, E.1    Petsko, G.A.2
  • 23
    • 0017180105 scopus 로고
    • Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes
    • McLaughlin AC, Leigh JS, Cohn M. 1976. Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. J Biol Chem 251:2777-2787.
    • (1976) J Biol Chem , vol.251 , pp. 2777-2787
    • McLaughlin, A.C.1    Leigh, J.S.2    Cohn, M.3
  • 24
    • 0028057108 scopus 로고
    • Raster3D Version 2.0 - A program for photorealistic molecular graphics
    • Merritt EA, Murphy MEP. 1994. Raster3D Version 2.0 - A program for photorealistic molecular graphics. Acta Cryst D50:869-873.
    • (1994) Acta Cryst , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 25
    • 0015052797 scopus 로고
    • Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion-complexes
    • Milner-White EJ, Watts DC. 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
  • 26
    • 0014010187 scopus 로고
    • Isotope exchange studies of the mechanism of the reaction catalyzed by ATP:creatine phosphotransferase
    • Morrison JF, Cleland WW. 1966. Isotope exchange studies of the mechanism of the reaction catalyzed by ATP:creatine phosphotransferase. J Biol Chem 241:637-683.
    • (1966) J Biol Chem , vol.241 , pp. 637-683
    • Morrison, J.F.1    Cleland, W.W.2
  • 28
    • 33947547892 scopus 로고
    • Molecular architecture and biological reactions
    • Pauling L. 1946. Molecular architecture and biological reactions. Chem Eng News 24:1375-1377.
    • (1946) Chem Eng News , vol.24 , pp. 1375-1377
    • Pauling, L.1
  • 29
    • 0019394535 scopus 로고
    • 31P NMR of enzyme-bound substrates of rabbit muscle creatine kinase. Equilibrium constants, interconversion rates, and NMR parameters of enzyme-bound complexes
    • 31P NMR of enzyme-bound substrates of rabbit muscle creatine kinase. Equilibrium constants, interconversion rates, and NMR parameters of enzyme-bound complexes. J Biol Chem 256:1716-1721.
    • (1981) J Biol Chem , vol.256 , pp. 1716-1721
    • Rao, B.D.N.1    Cohn, M.2
  • 30
    • 0019879376 scopus 로고
    • Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase
    • Rosevear PR, Desmeules P, Kenyon GL, Mildvan AS. 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
  • 31
    • 0022248941 scopus 로고
    • Calculations of electrostatic energies in proteins. The energetics of ionized groups in bovine pancreatic trypsin inhibitor
    • Russell ST, Warshel A. 1985. Calculations of electrostatic energies in proteins. The energetics of ionized groups in bovine pancreatic trypsin inhibitor. J Mol Biol 185:389-404.
    • (1985) J Mol Biol , vol.185 , pp. 389-404
    • Russell, S.T.1    Warshel, A.2
  • 33
    • 0015743403 scopus 로고
    • Inhibition of creatine kinase by chromium nucleotides
    • Schimerlick MI, Cleland WW. 1973. Inhibition of creatine kinase by chromium nucleotides. J Biol Chem 248:8418-8423.
    • (1973) J Biol Chem , vol.248 , pp. 8418-8423
    • Schimerlick, M.I.1    Cleland, W.W.2
  • 34
    • 0025687007 scopus 로고
    • Crystallization and preliminary X-ray analysis of two different forms of mitochondrial creatine kinase from chicken cardiac muscle
    • Schnyder T, Sargent DF, Richmond TJ, Eppenberger HM, 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
  • 35
    • 0028464366 scopus 로고
    • Why have mutagenesis studies not located the general base in ras p21
    • Schweins T, Langen R, Warshel A. 1994. Why have mutagenesis studies not located the general base in ras p21. Nat Struct Biol 1:476-484.
    • (1994) Nat Struct Biol , vol.1 , pp. 476-484
    • Schweins, T.1    Langen, R.2    Warshel, A.3
  • 38
    • 0029992890 scopus 로고    scopus 로고
    • Balancing ATP in the cell
    • Stroud RM. 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
  • 40
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • Tabor S, Richardson CC. 1987. DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc Natl Acad Sci USA 84:4767-4771.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 41
    • 0021351106 scopus 로고
    • Function of M-line bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphocreatine shuttle
    • Wallimann T, Schlösser T, Eppenberger HM. 1984. Function of M-line bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphocreatine shuttle. J Biol Chem 259:5238-5246.
    • (1984) J Biol Chem , vol.259 , pp. 5238-5246
    • Wallimann, T.1    Schlösser, T.2    Eppenberger, H.M.3
  • 42
    • 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, Eppenberger HM. 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
  • 43
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solution
    • Warshel A, Russell ST. 1984. Calculations of electrostatic interactions in biological systems and in solution. Q Rev Biophys 17:283-422.
    • (1984) Q Rev Biophys , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 44
    • 0026698727 scopus 로고
    • Mitochondrial creatine kinase: A key enzyme of aerobic energy metabolism
    • Wyss M, Smeitink J, Wevers RA, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.