메뉴 건너뛰기




Volumn , Issue , 2005, Pages 811-835

Catalysis by alcohol dehydrogenases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85056378809     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420028027     Document Type: Chapter
Times cited : (12)

References (125)
  • 1
    • 0019516163 scopus 로고
    • Probes of mechanism and transition state structure in the alcohol dehydrogenase reaction
    • Klinman, J. P., Probes of mechanism and transition state structure in the alcohol dehydrogenase reaction, CRC Crit. Rev. Biochem., 10, 39-78, 1981.
    • (1981) CRC Crit. Rev. Biochem. , vol.10 , pp. 39-78
    • Klinman, J.P.1
  • 2
    • 0002233968 scopus 로고
    • Hydrogen tunneling and coupled motion in enzyme reactions
    • Cook, P. F., Ed., CRC Press, Boca Raton
    • Klinman, J. P., Hydrogen tunneling and coupled motion in enzyme reactions, In Enzyme Mechanism from Isotope Effects, Cook, P. F., Ed., CRC Press, Boca Raton, pp. 127-148, 1991.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 127-148
    • Klinman, J.P.1
  • 3
    • 0043101145 scopus 로고
    • Isotope effects on the transient kinetics of enzyme reactions
    • Cook, P. F., Ed., CRC Press, Boca Raton
    • McFarland, J. T., Isotope effects on the transient kinetics of enzyme reactions, In Enzyme Mechanism from Isotope Effects, Cook, P. F., Ed., CRC Press, Boca Raton, pp. 151-179, 1991.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 151-179
    • McFarland, J.T.1
  • 4
    • 0023071444 scopus 로고
    • Liver alcohol dehydrogenase
    • Pettersson, G., Liver alcohol dehydrogenase, CRC Crit. Rev. Biochem., 21, 349-389, 1987.
    • (1987) CRC Crit. Rev. Biochem. , vol.21 , pp. 349-389
    • Pettersson, G.1
  • 6
    • 0001667366 scopus 로고
    • Product inhibition studies on yeast and liver alcohol dehydrogenases
    • Wratten, C. C. and Cleland, W. W., Product inhibition studies on yeast and liver alcohol dehydrogenases, Biochemistry, 2, 935-941, 1963.
    • (1963) Biochemistry , vol.2 , pp. 935-941
    • Wratten, C.C.1    Cleland, W.W.2
  • 7
    • 2542464389 scopus 로고
    • Kinetic studies of liver alcohol dehydrogenase and pH effects with coenzyme preparations of high purity
    • Dalziel, K., Kinetic studies of liver alcohol dehydrogenase and pH effects with coenzyme preparations of high purity, J. Biol. Chem., 238, 2850-2858, 1963.
    • (1963) J. Biol. Chem. , vol.238 , pp. 2850-2858
    • Dalziel, K.1
  • 8
    • 0001211645 scopus 로고
    • Studies on liver alcohol dehydrogenase: II. The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide
    • Theorell, H. and Chance, B., Studies on liver alcohol dehydrogenase: II. The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide, Acta Chem. Scand., 5, 1127-1144, 1951.
    • (1951) Acta Chem. Scand. , vol.5 , pp. 1127-1144
    • Theorell, H.1    Chance, B.2
  • 9
    • 0023792892 scopus 로고
    • Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide
    • Sekhar, V. C. and Plapp, B. V., Mechanism of binding of horse liver alcohol dehydrogenase and nicotinamide adenine dinucleotide, Biochemistry, 27, 5082-5088, 1988.
    • (1988) Biochemistry , vol.27 , pp. 5082-5088
    • Sekhar, V.C.1    Plapp, B.V.2
  • 11
    • 0000152502 scopus 로고
    • Equilibrium reaction rates and the mechanisms of liver and yeast alcohol dehydrogenase
    • Silverstein, E. and Boyer, P. D., Equilibrium reaction rates and the mechanisms of liver and yeast alcohol dehydrogenase, J. Biol. Chem., 239, 3908-3914, 1964.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3908-3914
    • Silverstein, E.1    Boyer, P.D.2
  • 12
    • 0015500405 scopus 로고
    • Isotope exchange studies on liver alcohol dehydrogenase with cyclohexanol and cyclohexanone as reactants
    • Ainslie, G. R. and Cleland, W. W., Isotope exchange studies on liver alcohol dehydrogenase with cyclohexanol and cyclohexanone as reactants, J. Biol. Chem., 247, 946-951, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 946-951
    • Ainslie, G.R.1    Cleland, W.W.2
  • 13
    • 0010349979 scopus 로고
    • Kinetic studies with liver alcohol dehydrogenase
    • Wratten, C. C. and Cleland, W. W., Kinetic studies with liver alcohol dehydrogenase, Biochemistry, 4, 2442-2451, 1965.
    • (1965) Biochemistry , vol.4 , pp. 2442-2451
    • Wratten, C.C.1    Cleland, W.W.2
  • 14
    • 0013923844 scopus 로고
    • The kinetics and mechanism of liver alcohol dehydrogenase with primary and secondary alcohols as substrates
    • Dalziel, K. and Dickinson, F. M., The kinetics and mechanism of liver alcohol dehydrogenase with primary and secondary alcohols as substrates, Biochem. J., 100, 34-46, 1966.
    • (1966) Biochem. J. , vol.100 , pp. 34-46
    • Dalziel, K.1    Dickinson, F.M.2
  • 15
    • 0013937518 scopus 로고
    • Substrate activation and inhibition in coenzyme-substrate reactions: Cyclohexanol oxidation catalysed by liver alcohol dehydrogenase
    • Dalziel, K. and Dickinson, F. M., Substrate activation and inhibition in coenzyme-substrate reactions: cyclohexanol oxidation catalysed by liver alcohol dehydrogenase, Biochem. J., 100, 491-500, 1966.
    • (1966) Biochem. J. , vol.100 , pp. 491-500
    • Dalziel, K.1    Dickinson, F.M.2
  • 17
    • 0019891912 scopus 로고
    • Mechanistic deductions from isotope effects in multireactant enzyme mechanisms
    • Cook, P. F. and Cleland, W. W., Mechanistic deductions from isotope effects in multireactant enzyme mechanisms, Biochemistry, 20, 1790-1796, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1790-1796
    • Cook, P.F.1    Cleland, W.W.2
  • 18
    • 0015577980 scopus 로고
    • A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates
    • Dickinson, F. M. and Monger, G. P., A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates, Biochem. J., 131, 261-270, 1973.
    • (1973) Biochem. J. , vol.131 , pp. 261-270
    • Dickinson, F.M.1    Monger, G.P.2
  • 19
    • 0023892032 scopus 로고
    • Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase
    • Ganzhorn, A. J. and Plapp, B. V., Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase, J. Biol. Chem., 263, 5446-5454, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5446-5454
    • Ganzhorn, A.J.1    Plapp, B.V.2
  • 20
    • 0020345922 scopus 로고
    • Deuterium and tritium kinetic isotope effects on initial rates
    • Northrop, D. B., Deuterium and tritium kinetic isotope effects on initial rates, Methods Enzymol., 87, 607-625, 1982.
    • (1982) Methods Enzymol. , vol.87 , pp. 607-625
    • Northrop, D.B.1
  • 21
    • 0020435222 scopus 로고
    • The use of isotope effects to determine transition-state structure for enzymic reactions
    • Cleland, W. W., The use of isotope effects to determine transition-state structure for enzymic reactions, Methods Enzymol., 87, 625-641, 1982.
    • (1982) Methods Enzymol. , vol.87 , pp. 625-641
    • Cleland, W.W.1
  • 22
    • 0019524346 scopus 로고
    • pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope and pH-dependent steps the same
    • Cook, P. F. and Cleland, W. W., pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope and pH-dependent steps the same, Biochemistry, 20, 1797-1805, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1797-1805
    • Cook, P.F.1    Cleland, W.W.2
  • 23
    • 0019472074 scopus 로고
    • pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase
    • Cook, P. F. and Cleland, W. W., pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase, Biochemistry, 20, 1805-1816, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1805-1816
    • Cook, P.F.1    Cleland, W.W.2
  • 24
    • 0021756505 scopus 로고
    • Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehyde
    • Scharschmidt, M., Fisher, M. A., and Cleland, W. W., Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehyde, Biochemistry, 23, 5471-5478, 1984.
    • (1984) Biochemistry , vol.23 , pp. 5471-5478
    • Scharschmidt, M.1    Fisher, M.A.2    Cleland, W.W.3
  • 25
    • 0018977110 scopus 로고
    • Unified mechanism for proton-transfer reactions affecting the catalytic activity of liver alcohol dehydrogenase
    • Kvassman, J. and Pettersson, G., Unified mechanism for proton-transfer reactions affecting the catalytic activity of liver alcohol dehydrogenase, Eur. J. Biochem., 103, 565-575, 1980.
    • (1980) Eur. J. Biochem. , vol.103 , pp. 565-575
    • Kvassman, J.1    Pettersson, G.2
  • 26
    • 0020479867 scopus 로고
    • Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase
    • Eklund, H., Plapp, B. V., Samama, J. P., and Brändén, C.-I., Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase, J. Biol. Chem., 257, 14349-14358, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14349-14358
    • Eklund, H.1    Plapp, B.V.2    Samama, J.P.3    Brändén, C.-I.4
  • 28
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution
    • Eklund, H., Samama, J.-P., Wallén, L., Brändén, C.-I., Å keson, Å., and Jones, T. A., Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution, J. Mol. Biol., 146, 561-587, 1981.
    • (1981) J. Mol. Biol. , vol.146 , pp. 561-587
    • Eklund, H.1    Samama, J.-P.2    Wallén, L.3    Brändén, C.-I.4    Åkeson, Å.5    Jones, T.A.6
  • 29
    • 0031033967 scopus 로고    scopus 로고
    • Flexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides
    • Cho, H., Ramaswamy, S., and Plapp, B. V., Flexibility of liver alcohol dehydrogenase in stereoselective binding of 3-butylthiolane 1-oxides, Biochemistry, 36, 382-389, 1997.
    • (1997) Biochemistry , vol.36 , pp. 382-389
    • Cho, H.1    Ramaswamy, S.2    Plapp, B.V.3
  • 30
    • 0030999986 scopus 로고    scopus 로고
    • Binding of formamides to liver alcohol dehydrogenase
    • Ramaswamy, S., Scholze, M., and Plapp, B. V., Binding of formamides to liver alcohol dehydrogenase, Biochemistry, 36, 3522-3527, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3522-3527
    • Ramaswamy, S.1    Scholze, M.2    Plapp, B.V.3
  • 31
    • 0141703606 scopus 로고    scopus 로고
    • Formamides mimic aldehydes and inhibit liver alcohol dehydrogenases and ethanol metabolism
    • Venkataramaiah, T. H. and Plapp, B. V., Formamides mimic aldehydes and inhibit liver alcohol dehydrogenases and ethanol metabolism, J. Biol. Chem., 278, 36699-36706, 2003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36699-36706
    • Venkataramaiah, T.H.1    Plapp, B.V.2
  • 32
    • 0027196492 scopus 로고
    • Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis
    • Bahnson, B. J., Park, D.-H., Kim, K., Plapp, B. V., and Klinman, J. P., Unmasking of hydrogen tunneling in the horse liver alcohol dehydrogenase reaction by site-directed mutagenesis, Biochemistry, 32, 5503-5507, 1993.
    • (1993) Biochemistry , vol.32 , pp. 5503-5507
    • Bahnson, B.J.1    Park, D.-H.2    Kim, K.3    Plapp, B.V.4    Klinman, J.P.5
  • 33
    • 0035861065 scopus 로고    scopus 로고
    • Hydride transfer in liver alcohol dehydrogenase: Quantum dynamics, kinetic isotope effects, and role of enzyme motion
    • Billeter, S. R., Webb, S. P., Agarwal, P. K., Iordanov, T., and Hammes-Schiffer, S., Hydride transfer in liver alcohol dehydrogenase: quantum dynamics, kinetic isotope effects, and role of enzyme motion, J. Am. Chem. Soc., 123, 11262-11272, 2001.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11262-11272
    • Billeter, S.R.1    Webb, S.P.2    Agarwal, P.K.3    Iordanov, T.4    Hammes-Schiffer, S.5
  • 34
    • 0035940450 scopus 로고    scopus 로고
    • Contributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis
    • Rubach, J. K., Ramaswamy, S., and Plapp, B. V., Contributions of valine-292 in the nicotinamide binding site of liver alcohol dehydrogenase and dynamics to catalysis, Biochemistry, 40, 12686-12694, 2001.
    • (2001) Biochemistry , vol.40 , pp. 12686-12694
    • Rubach, J.K.1    Ramaswamy, S.2    Plapp, B.V.3
  • 36
    • 0037452898 scopus 로고    scopus 로고
    • Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase
    • Rubach, J. K. and Plapp, B. V., Amino acid residues in the nicotinamide binding site contribute to catalysis by horse liver alcohol dehydrogenase, Biochemistry, 42, 2907-2915, 2003.
    • (2003) Biochemistry , vol.42 , pp. 2907-2915
    • Rubach, J.K.1    Plapp, B.V.2
  • 37
    • 0025922529 scopus 로고
    • 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases
    • 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases, Biochemistry, 30, 4068-4071, 1991.
    • (1991) Biochemistry , vol.30 , pp. 4068-4071
    • Rotberg, N.S.1    Cleland, W.W.2
  • 38
    • 0001185405 scopus 로고    scopus 로고
    • Aromaticity of bent benzene rings: A VBSCF study
    • Dijkstra, F. and van Lenthe, J. H., Aromaticity of bent benzene rings: a VBSCF study, Int. J. Quantum Chem., 74, 213-221, 1999.
    • (1999) Int. J. Quantum Chem. , vol.74 , pp. 213-221
    • Dijkstra, F.1    van Lenthe, J.H.2
  • 39
    • 0028930478 scopus 로고
    • Site-directed mutagenesis: A tool for studying enzyme catalysis
    • Plapp, B. V., Site-directed mutagenesis: a tool for studying enzyme catalysis, Methods Enzymol., 249, 91-119, 1995.
    • (1995) Methods Enzymol. , vol.249 , pp. 91-119
    • Plapp, B.V.1
  • 40
    • 0033592324 scopus 로고    scopus 로고
    • Control of coenzyme binding to horse liver alcohol dehydrogenase
    • LeBrun, L. A. and Plapp, B. V., Control of coenzyme binding to horse liver alcohol dehydrogenase, Biochemistry, 38, 12387-12393, 1999.
    • (1999) Biochemistry , vol.38 , pp. 12387-12393
    • LeBrun, L.A.1    Plapp, B.V.2
  • 41
    • 1542743968 scopus 로고    scopus 로고
    • Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase
    • LeBrun, L. A., Park, D.-H., Ramaswamy, S., and Plapp, B. V., Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase, Biochemistry, 43, 3014-3026, 2004.
    • (2004) Biochemistry , vol.43 , pp. 3014-3026
    • LeBrun, L.A.1    Park, D.-H.2    Ramaswamy, S.3    Plapp, B.V.4
  • 42
    • 0034269897 scopus 로고    scopus 로고
    • Combining electronic structure methods with the calculation of hydrogen vibrational wave functions: Application to hydride transfer in liver alcohol dehydrogenase
    • Webb, S. P., Agarwal, P. K., and Hammes-Schiffer, S., Combining electronic structure methods with the calculation of hydrogen vibrational wave functions: application to hydride transfer in liver alcohol dehydrogenase, J. Phys. Chem. B, 104, 8884-8894, 2000.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 8884-8894
    • Webb, S.P.1    Agarwal, P.K.2    Hammes-Schiffer, S.3
  • 43
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products:I. Nomenclature and rate equations
    • Cleland, W. W., The kinetics of enzyme-catalyzed reactions with two or more substrates or products:I. Nomenclature and rate equations, Biochim. Biophys. Acta, 67, 104-137, 1963.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 44
    • 0014501232 scopus 로고
    • The rates of binding of reduced nicotinamide-adenine dinucleotide analogs to liver alcohol dehydrogenase
    • Shore, J. D., The rates of binding of reduced nicotinamide-adenine dinucleotide analogs to liver alcohol dehydrogenase, Biochemistry, 8, 1588-1590, 1969.
    • (1969) Biochemistry , vol.8 , pp. 1588-1590
    • Shore, J.D.1
  • 45
    • 0014961160 scopus 로고
    • Transients in the reactions of liver alcohol dehydrogenase
    • Shore, J. D. and Gutfreund, H., Transients in the reactions of liver alcohol dehydrogenase, Biochemistry, 9, 4655-4659, 1970.
    • (1970) Biochemistry , vol.9 , pp. 4655-4659
    • Shore, J.D.1    Gutfreund, H.2
  • 46
    • 0015522895 scopus 로고
    • The effects of pH and temperature on hydrogen transfer in the liver alcohol dehydrogenase mechanism
    • Brooks, R. L., Shore, J. D., and Gutfreund, H., The effects of pH and temperature on hydrogen transfer in the liver alcohol dehydrogenase mechanism, J. Biol. Chem., 247, 2382-2383, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2382-2383
    • Brooks, R.L.1    Shore, J.D.2    Gutfreund, H.3
  • 47
    • 77956918156 scopus 로고
    • Rapid reactions and transient states
    • Hammes, G. H. and Schimmel, P. R., Rapid reactions and transient states, Enzymes, 2, 67-114, 1970.
    • (1970) Enzymes , vol.2 , pp. 67-114
    • Hammes, G.H.1    Schimmel, P.R.2
  • 48
    • 0028673742 scopus 로고
    • Analysis of kinetic data: Practical applications of computer simulation and fitting programs
    • Frieden, C., Analysis of kinetic data: practical applications of computer simulation and fitting programs, Methods Enzymol., 240, 311-322, 1994.
    • (1994) Methods Enzymol. , vol.240 , pp. 311-322
    • Frieden, C.1
  • 49
    • 0025366693 scopus 로고
    • Rate constants for a mechanism including intermediates in the inter-conversion of ternary complexes by horse liver alcohol dehydrogenase
    • Sekhar, V. C. and Plapp, B. V., Rate constants for a mechanism including intermediates in the inter-conversion of ternary complexes by horse liver alcohol dehydrogenase, Biochemistry, 29, 4289-4295, 1990.
    • (1990) Biochemistry , vol.29 , pp. 4289-4295
    • Sekhar, V.C.1    Plapp, B.V.2
  • 50
    • 0017087921 scopus 로고
    • The transient-state kinetics of two-substrate enzyme systems operating by an ordered ternary-complex mechanism
    • Pettersson, G., The transient-state kinetics of two-substrate enzyme systems operating by an ordered ternary-complex mechanism, Eur. J. Biochem., 69, 273-278, 1976.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 273-278
    • Pettersson, G.1
  • 51
    • 84945061208 scopus 로고
    • Deuterium isotope effects on the presteady state burst of an enzymatic reaction
    • Cleland, W. W., Deuterium isotope effects on the presteady state burst of an enzymatic reaction, Z. Naturforsch., 44a, 445-449, 1988.
    • (1988) Z. Naturforsch. , vol.44 a , pp. 445-449
    • Cleland, W.W.1
  • 52
    • 0030049324 scopus 로고    scopus 로고
    • Interpretation of transient-state kinetic isotope effects
    • Fisher, H. F. and Saha, S. K., Interpretation of transient-state kinetic isotope effects, Biochemistry, 35, 83-88, 1996.
    • (1996) Biochemistry , vol.35 , pp. 83-88
    • Fisher, H.F.1    Saha, S.K.2
  • 53
    • 0019194597 scopus 로고
    • Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions
    • Cook, P. F., Blanchard, J. S., and Cleland, W. W., Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions, Biochemistry, 19, 4853-4858, 1980.
    • (1980) Biochemistry , vol.19 , pp. 4853-4858
    • Cook, P.F.1    Blanchard, J.S.2    Cleland, W.W.3
  • 54
    • 0015524179 scopus 로고
    • The mechanism of enzyme-catalyzed reduced nicotinamide adenine dinucleotidedependent reductions. Substituent and isotope effects in the yeast alcohol dehydrogenase reaction
    • Klinman, J. P., The mechanism of enzyme-catalyzed reduced nicotinamide adenine dinucleotidedependent reductions. Substituent and isotope effects in the yeast alcohol dehydrogenase reaction, J. Biol. Chem., 247, 7977-7987, 1972.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7977-7987
    • Klinman, J.P.1
  • 55
    • 0016823445 scopus 로고
    • Acid-base catalysis in the yeast alcohol dehydrogenase reaction
    • Klinman, J. P., Acid-base catalysis in the yeast alcohol dehydrogenase reaction, J. Biol. Chem., 250, 2569-2573, 1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2569-2573
    • Klinman, J.P.1
  • 56
    • 0017144165 scopus 로고
    • Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols
    • Klinman, J. P., Isotope effects and structure-reactivity correlations in the yeast alcohol dehydrogenase reaction. A study of the enzyme-catalyzed oxidation of aromatic alcohols, Biochemistry, 15, 2018-2026, 1976.
    • (1976) Biochemistry , vol.15 , pp. 2018-2026
    • Klinman, J.P.1
  • 57
    • 0015935520 scopus 로고
    • Horse liver alcohol dehydrogenase. Amino groups and rate-limiting steps in catalysis
    • Plapp, B. V., Brooks, R. L., and Shore, J. D., Horse liver alcohol dehydrogenase. Amino groups and rate-limiting steps in catalysis, J. Biol. Chem., 248, 3470-3475, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3470-3475
    • Plapp, B.V.1    Brooks, R.L.2    Shore, J.D.3
  • 58
    • 0017393626 scopus 로고
    • pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenase
    • Dworschack, R. T. and Plapp, B. V., pH, isotope, and substituent effects on the interconversion of aromatic substrates catalyzed by hydroxybutyrimidylated liver alcohol dehydrogenase, Biochemistry, 16, 2716-2725, 1977.
    • (1977) Biochemistry , vol.16 , pp. 2716-2725
    • Dworschack, R.T.1    Plapp, B.V.2
  • 59
    • 0037207116 scopus 로고    scopus 로고
    • Mobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and x-ray crystallographic studies
    • Rubach, J. K. and Plapp, B. V., Mobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and x-ray crystallographic studies, Biochemistry, 41, 15770-15779, 2002.
    • (2002) Biochemistry , vol.41 , pp. 15770-15779
    • Rubach, J.K.1    Plapp, B.V.2
  • 61
    • 0028927029 scopus 로고
    • Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenase
    • Fan, F. and Plapp, B. V., Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenase, Biochemistry, 34, 4709-4713, 1995.
    • (1995) Biochemistry , vol.34 , pp. 4709-4713
    • Fan, F.1    Plapp, B.V.2
  • 62
    • 0344631780 scopus 로고    scopus 로고
    • Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer
    • Ramaswamy, S., Park, D.-H., and Plapp, B. V., Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer, Biochemistry, 38, 13951-13959, 1999.
    • (1999) Biochemistry , vol.38 , pp. 13951-13959
    • Ramaswamy, S.1    Park, D.-H.2    Plapp, B.V.3
  • 63
    • 0024723235 scopus 로고
    • Quantum mechanical effects in enzyme-catalyzed hydrogen transfer reactions
    • Klinman, J. P., Quantum mechanical effects in enzyme-catalyzed hydrogen transfer reactions, Trends Biochem. Sci., 14, 368-373, 1989.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 368-373
    • Klinman, J.P.1
  • 64
    • 0028954039 scopus 로고
    • Hydrogen tunneling in enzyme catalysis
    • Bahnson, B. J. and Klinman, J. P., Hydrogen tunneling in enzyme catalysis, Methods Enzymol., 249, 373-397, 1995.
    • (1995) Methods Enzymol. , vol.249 , pp. 373-397
    • Bahnson, B.J.1    Klinman, J.P.2
  • 65
    • 0000809846 scopus 로고
    • Reaction-coordinate tunneling in hydride-transfer reactions
    • Huskey, W. P. and Schowen, R. L., Reaction-coordinate tunneling in hydride-transfer reactions, J. Am. Chem. Soc., 105, 5704-5706, 1983.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5704-5706
    • Huskey, W.P.1    Schowen, R.L.2
  • 66
    • 0037123292 scopus 로고    scopus 로고
    • Boundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling
    • Kohen, A. and Jensen, J. H., Boundary conditions for the Swain-Schaad relationship as a criterion for hydrogen tunneling, J. Am. Chem. Soc., 124, 3858-3864, 2002.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3858-3864
    • Kohen, A.1    Jensen, J.H.2
  • 67
    • 0024573393 scopus 로고
    • Hydrogen tunneling in enzyme reactions
    • Cha, Y., Murray, C. J., and Klinman, J. P., Hydrogen tunneling in enzyme reactions, Science, 243, 1325-1330, 1989.
    • (1989) Science , vol.243 , pp. 1325-1330
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 68
    • 0032580981 scopus 로고    scopus 로고
    • Active site modifications in a double mutant of liver alcohol dehydrogenase: Structural studies of two enzyme-ligand complexes
    • Colby, T. D., Bahnson, B. J., Chin, J. K., Klinman, J. P., and Goldstein, B. M., Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes, Biochemistry, 37, 9295-9304, 1998.
    • (1998) Biochemistry , vol.37 , pp. 9295-9304
    • Colby, T.D.1    Bahnson, B.J.2    Chin, J.K.3    Klinman, J.P.4    Goldstein, B.M.5
  • 69
    • 0032817216 scopus 로고    scopus 로고
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants
    • 2OH on the distance between reactants when catalyzed by horse liver alcohol dehydrogenase and 203 single point mutants, Bioorg. Chem., 27, 289-296, 1999.
    • (1999) Bioorg. Chem. , vol.27 , pp. 289-296
    • Luo, J.1    Kahn, K.2    Bruice, T.C.3
  • 70
    • 0037012441 scopus 로고    scopus 로고
    • Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase
    • Caratzoulas, S., Mincer, J. S., and Schwartz, S. D., Identification of a protein-promoting vibration in the reaction catalyzed by horse liver alcohol dehydrogenase, J. Am. Chem. Soc., 124, 3270-3276, 2002.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3270-3276
    • Caratzoulas, S.1    Mincer, J.S.2    Schwartz, S.D.3
  • 71
    • 0033168713 scopus 로고    scopus 로고
    • Hydrogen tunneling in biology
    • Kohen, A. and Klinman, J. P., Hydrogen tunneling in biology, Chem. Biol., 6, R191- R198, 1999.
    • (1999) Chem. Biol. , vol.6 , pp. R191-R198
    • Kohen, A.1    Klinman, J.P.2
  • 72
    • 0141828475 scopus 로고    scopus 로고
    • Kinetic isotope effects as probes for hydrogen tunneling, coupled motion and dynamics contributions to enzyme catalysis
    • Kohen, A., Kinetic isotope effects as probes for hydrogen tunneling, coupled motion and dynamics contributions to enzyme catalysis, Prog. React. Kinet. Mech., 28, 119-156, 2003.
    • (2003) Prog. React. Kinet. Mech. , vol.28 , pp. 119-156
    • Kohen, A.1
  • 74
    • 0033568523 scopus 로고    scopus 로고
    • New insights into enzyme catalysis. Ground state tunneling driven by protein dynamics
    • Scrutton, N. S., Basran, J., and Sutcliffe, M. J., New insights into enzyme catalysis. Ground state tunneling driven by protein dynamics, Eur. J. Biochem., 264, 666-671, 1999.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 666-671
    • Scrutton, N.S.1    Basran, J.2    Sutcliffe, M.J.3
  • 75
    • 0026733589 scopus 로고
    • Inter-conversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysis
    • Park, D.-H. and Plapp, B. V., Inter-conversion of E and S isoenzymes of horse liver alcohol dehydrogenase. Several residues contribute indirectly to catalysis, J. Biol. Chem., 267, 5527-5533, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5527-5533
    • Park, D.-H.1    Plapp, B.V.2
  • 76
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase
    • Kohen, A., Cannio, R., Bartolucci, S., and Klinman, J. P., Enzyme dynamics and hydrogen tunneling in a thermophilic alcohol dehydrogenase, Nature, 399, 496-499, 1999.
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 77
    • 0034327617 scopus 로고    scopus 로고
    • Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases
    • Kohen, A. and Klinman, J., Protein flexibility correlates with degree of hydrogen tunneling in thermophilic and mesophilic alcohol dehydrogenases, J. Am. Chem. Soc., 122, 10738-10739, 2000.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 10738-10739
    • Kohen, A.1    Klinman, J.2
  • 78
    • 0035916307 scopus 로고    scopus 로고
    • Probes of hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures
    • Tsai, S. and Klinman, J. P., Probes of hydrogen tunneling with horse liver alcohol dehydrogenase at subzero temperatures, Biochemistry, 40, 2303-2311, 2001.
    • (2001) Biochemistry , vol.40 , pp. 2303-2311
    • Tsai, S.1    Klinman, J.P.2
  • 79
    • 0035859446 scopus 로고    scopus 로고
    • Internal enzyme motions as a source of catalytic activity:Rate-promoting vibrations and hydrogen tunneling
    • Antoniou, D. and Schwartz, S. D., Internal enzyme motions as a source of catalytic activity:rate-promoting vibrations and hydrogen tunneling, J. Phys. Chem. B, 105, 5553-5558, 2001.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5553-5558
    • Antoniou, D.1    Schwartz, S.D.2
  • 80
    • 0035970089 scopus 로고    scopus 로고
    • Convex Arrhenius plots and their interpretation
    • Truhlar, D. G. and Kohen, A., Convex Arrhenius plots and their interpretation, Proc. Natl. Acad. Sci. U.S.A., 98, 848-851, 2001.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 848-851
    • Truhlar, D.G.1    Kohen, A.2
  • 81
    • 5544259571 scopus 로고
    • Molecular-dynamics simulation for a model nonadiabatic proton transfer reaction in solution
    • Borgis, D. and Hynes, J. T., Molecular-dynamics simulation for a model nonadiabatic proton transfer reaction in solution, J. Chem. Phys., 94, 3619-3628, 1991.
    • (1991) J. Chem. Phys. , vol.94 , pp. 3619-3628
    • Borgis, D.1    Hynes, J.T.2
  • 82
    • 0026707687 scopus 로고
    • Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer
    • Bruno, W. J. and Bialek, W., Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer, Biophys. J., 63, 689-699, 1992.
    • (1992) Biophys. J. , vol.63 , pp. 689-699
    • Bruno, W.J.1    Bialek, W.2
  • 83
    • 0347866726 scopus 로고    scopus 로고
    • Activated chemistry in the presence of a strongly symmetrically coupled vibration
    • Antoniou, D. and Schwartz, S. D., Activated chemistry in the presence of a strongly symmetrically coupled vibration, J. Chem. Phys., 108, 3620-3625, 1998.
    • (1998) J. Chem. Phys. , vol.108 , pp. 3620-3625
    • Antoniou, D.1    Schwartz, S.D.2
  • 84
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunneling in hydrolytic and redox enzyme catalysis
    • Kuznetsov, A. M. and Ulstrup, J., Proton and hydrogen atom tunneling in hydrolytic and redox enzyme catalysis, Canadian J. Chem. Revue Canadienne de Chimie, 77, 1085-1096, 1999.
    • (1999) Canadian J. Chem. Revue Canadienne de Chimie , vol.77 , pp. 1085-1096
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 85
    • 0036305396 scopus 로고    scopus 로고
    • A new conceptual framework for enzyme catalysis. Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes
    • Sutcliffe, M. J. and Scrutton, N. S., A new conceptual framework for enzyme catalysis. Hydrogen tunneling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes, Eur. J. Biochem., 269, 3096-3102, 2002.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3096-3102
    • Sutcliffe, M.J.1    Scrutton, N.S.2
  • 86
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics
    • Knapp, M. J. and Klinman, J. P., Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics, Eur. J. Biochem., 269, 3113-3121, 2002.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 87
    • 0037069410 scopus 로고    scopus 로고
    • Impact of enzyme motion on activity
    • Hammes-Schiffer, S., Impact of enzyme motion on activity, Biochemistry, 41, 13335-13343, 2002.
    • (2002) Biochemistry , vol.41 , pp. 13335-13343
    • Hammes-Schiffer, S.1
  • 88
    • 0037426823 scopus 로고    scopus 로고
    • A computational method to identify residues important in creating a protein promoting vibration in enzymes
    • Mincer, J. S. and Schwartz, S. D., A computational method to identify residues important in creating a protein promoting vibration in enzymes, J. Phys. Chem. B, 107, 366-371, 2003.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 366-371
    • Mincer, J.S.1    Schwartz, S.D.2
  • 89
    • 0043235788 scopus 로고    scopus 로고
    • Protein promoting vibrations in enzyme catalysis-a conserved evolutionary motif
    • Mincer, J. S. and Schwartz, S. D., Protein promoting vibrations in enzyme catalysis-a conserved evolutionary motif, J. Proteome Res., 2, 437-439, 2003.
    • (2003) J. Proteome Res. , vol.2 , pp. 437-439
    • Mincer, J.S.1    Schwartz, S.D.2
  • 90
    • 0035940264 scopus 로고    scopus 로고
    • Energetics and dynamics of enzymatic reactions
    • Villá, J. and Warshel, A., Energetics and dynamics of enzymatic reactions, J. Phys. Chem. B, 105, 7887-7907, 2001.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7887-7907
    • Villá, J.1    Warshel, A.2
  • 91
    • 0036285978 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biological reactions
    • Warshel, A., Molecular dynamics simulations of biological reactions, Acc. Chem. Res., 35, 385-395, 2002.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 385-395
    • Warshel, A.1
  • 92
    • 0034097153 scopus 로고    scopus 로고
    • Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: Evidence for mechanical models of catalysis
    • Northrop, D. B. and Cho, Y. K., Effect of pressure on deuterium isotope effects of yeast alcohol dehydrogenase: evidence for mechanical models of catalysis, Biochemistry, 39, 2406-2412, 2000.
    • (2000) Biochemistry , vol.39 , pp. 2406-2412
    • Northrop, D.B.1    Cho, Y.K.2
  • 93
    • 0033282014 scopus 로고    scopus 로고
    • Dynamics in alcohol dehydrogenase elucidated from crystallographic investigations
    • Weiner, H., Maser, E., Crabb, D. W., and Lindahl, R., Eds., Kluwer Academic, New York
    • Ramaswamy, S., Dynamics in alcohol dehydrogenase elucidated from crystallographic investigations, In Enzymology and Molecular Biology of Carbonyl Metabolism 7, Weiner, H., Maser, E., Crabb, D. W., and Lindahl, R., Eds., Kluwer Academic, New York, pp. 275-284, 1999.
    • (1999) Enzymology and Molecular Biology of Carbonyl Metabolism 7 , pp. 275-284
    • Ramaswamy, S.1
  • 94
    • 0037168602 scopus 로고    scopus 로고
    • Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase
    • Luo, J. and Bruice, T. C., Ten-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase, Proc. Natl Acad. Sci. U.S.A., 99, 16597-16600, 2002.
    • (2002) Proc. Natl Acad. Sci. U.S.A. , vol.99 , pp. 16597-16600
    • Luo, J.1    Bruice, T.C.2
  • 95
    • 0037159205 scopus 로고    scopus 로고
    • Coupling interactions of distal residues enhances dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates
    • Rajagopalan, P. T., Lutz, S., and Benkovic, S. J., Coupling interactions of distal residues enhances dihydrofolate reductase catalysis: mutational effects on hydride transfer rates, Biochemistry, 41, 12618-12628, 2002.
    • (2002) Biochemistry , vol.41 , pp. 12618-12628
    • Rajagopalan, P.T.1    Lutz, S.2    Benkovic, S.J.3
  • 97
    • 0034673157 scopus 로고    scopus 로고
    • Probes of a role for remote binding interactions on hydrogen tunneling in the horse liver alcohol dehydrogenase reaction
    • Chin, J. K. and Klinman, J. P., Probes of a role for remote binding interactions on hydrogen tunneling in the horse liver alcohol dehydrogenase reaction, Biochemistry, 39, 1278-1284, 2000.
    • (2000) Biochemistry , vol.39 , pp. 1278-1284
    • Chin, J.K.1    Klinman, J.P.2
  • 98
    • 0035892157 scopus 로고    scopus 로고
    • Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase
    • Alhambra, C., Corchado, J., Sanchez, M. L., Garcia-Viloca, M., Gao, J., and Truhlar, D. G., Canonical variational theory for enzyme kinetics with the protein mean force and multidimensional quantum mechanical tunneling dynamics. Theory and application to liver alcohol dehydrogenase, J. Phys. Chem. B, 105, 11326-11340, 2001.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11326-11340
    • Alhambra, C.1    Corchado, J.2    Sanchez, M.L.3    Garcia-Viloca, M.4    Gao, J.5    Truhlar, D.G.6
  • 99
    • 0037076062 scopus 로고    scopus 로고
    • A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH)
    • Cui, Q., Elstner, M., and Karplus, M., A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH), J. Phys. Chem. B, 106, 2721-2740, 2002.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2721-2740
    • Cui, Q.1    Elstner, M.2    Karplus, M.3
  • 101
    • 0036025446 scopus 로고    scopus 로고
    • Quantum mechanical methods for enzyme kinetics
    • Gao, J. and Truhlar, D. G., Quantum mechanical methods for enzyme kinetics, Annu. Rev. Phys. Chem., 53, 467-505, 2002.
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 467-505
    • Gao, J.1    Truhlar, D.G.2
  • 102
    • 0034679001 scopus 로고    scopus 로고
    • Computational studies of the mechanism for proton and hydride transfer in liver alcohol dehydrogenase
    • Agarwal, P. K., Webb, S. P., and Hammes-Schiffer, S., Computational studies of the mechanism for proton and hydride transfer in liver alcohol dehydrogenase, J. Am. Chem. Soc., 122, 4803-4812, 2000.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4803-4812
    • Agarwal, P.K.1    Webb, S.P.2    Hammes-Schiffer, S.3
  • 103
    • 0030887896 scopus 로고    scopus 로고
    • Simulation of the enzyme reaction mechanism of malate dehydrogenase
    • Cunningham, M. A., Ho, L. L., Nguyen, D. T., Gillilan, R. E., and Bash, P. A., Simulation of the enzyme reaction mechanism of malate dehydrogenase, Biochemistry, 36, 4800-4816, 1997.
    • (1997) Biochemistry , vol.36 , pp. 4800-4816
    • Cunningham, M.A.1    Ho, L.L.2    Nguyen, D.T.3    Gillilan, R.E.4    Bash, P.A.5
  • 104
    • 0020346954 scopus 로고
    • Solvent isotope effects on enzyme systems
    • Schowen, K. B. and Schowen, R. L., Solvent isotope effects on enzyme systems, Methods Enzymol., 87, 551-606, 1982.
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 107
    • 0019323518 scopus 로고
    • Transition-state structure in the yeast alcohol dehydrogenase reaction: The magnitude of solvent and alpha-secondary hydrogen isotope effects
    • Welsh, K. M., Creighton, D. J., and Klinman, J. P., Transition-state structure in the yeast alcohol dehydrogenase reaction: the magnitude of solvent and alpha-secondary hydrogen isotope effects, Biochemistry, 19, 2005-2016, 1980.
    • (1980) Biochemistry , vol.19 , pp. 2005-2016
    • Welsh, K.M.1    Creighton, D.J.2    Klinman, J.P.3
  • 108
    • 0033863236 scopus 로고    scopus 로고
    • Effects of high pressure on solvent isotope effects of yeast alcohol dehydrogenase
    • Northrop, D. B. and Cho, Y. K., Effects of high pressure on solvent isotope effects of yeast alcohol dehydrogenase, Biophys. J., 79, 1621-1628, 2000.
    • (2000) Biophys. J. , vol.79 , pp. 1621-1628
    • Northrop, D.B.1    Cho, Y.K.2
  • 109
    • 0020726823 scopus 로고
    • Solvent isotope effects on the reaction catalyzed by alcohol dehydrogenase from equine liver
    • Taylor, K. B., Solvent isotope effects on the reaction catalyzed by alcohol dehydrogenase from equine liver, Biochemistry, 22, 1040-1045, 1983.
    • (1983) Biochemistry , vol.22 , pp. 1040-1045
    • Taylor, K.B.1
  • 110
    • 0011132767 scopus 로고
    • Solvent deuterium isotope effect on the liver alcohol dehydrogenase reaction
    • Schmidt, J., Chen, J., DeTraglia, M., Minkel, D., and McFarland, J. T., Solvent deuterium isotope effect on the liver alcohol dehydrogenase reaction, J. Am. Chem. Soc., 101, 3634-3640, 1979.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3634-3640
    • Schmidt, J.1    Chen, J.2    DeTraglia, M.3    Minkel, D.4    McFarland, J.T.5
  • 111
    • 33847085649 scopus 로고
    • Structures and isotopic fractionation factors of complexes
    • Kreevoy, M. M. and Liang, T. M., Structures and isotopic fractionation factors of complexes, J. Am. Chem. Soc., 102, 3315-3322, 1980.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 3315-3322
    • Kreevoy, M.M.1    Liang, T.M.2
  • 112
    • 0031127432 scopus 로고    scopus 로고
    • Understanding enzymic catalysis:The importance of short, strong hydrogen bonds
    • Gerlt, J. A., Kreevoy, M. M., Cleland, W., and Frey, P. A., Understanding enzymic catalysis:the importance of short, strong hydrogen bonds, Chem. Biol., 4, 259-267, 1997.
    • (1997) Chem. Biol. , vol.4 , pp. 259-267
    • Gerlt, J.A.1    Kreevoy, M.M.2    Cleland, W.3    Frey, P.A.4
  • 113
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • Cleland, W. W., Frey, P. A., and Gerlt, J. A., The low barrier hydrogen bond in enzymatic catalysis, J. Biol. Chem., 273, 25529-25532, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25529-25532
    • Cleland, W.W.1    Frey, P.A.2    Gerlt, J.A.3
  • 114
    • 0023043191 scopus 로고
    • Energetics of proline racemase: Double fractionation experiment, a test for concertedness and for transition-state dominance
    • Belasco, J. G., Albery, W. J., and Knowles, J. R., Energetics of proline racemase: double fractionation experiment, a test for concertedness and for transition-state dominance, Biochemistry, 25, 2552-2558, 1986.
    • (1986) Biochemistry , vol.25 , pp. 2552-2558
    • Belasco, J.G.1    Albery, W.J.2    Knowles, J.R.3
  • 115
    • 0346963173 scopus 로고    scopus 로고
    • 2, consistent with a hydride transfer mechanism
    • 2, consistent with a hydride transfer mechanism, Biochemistry, 42, 13833-13838, 2003.
    • (2003) Biochemistry , vol.42 , pp. 13833-13838
    • Sobrado, P.1    Fitzpatrick, P.F.2
  • 116
    • 0026755601 scopus 로고
    • A vibrational analysis of the catalytically important C4-H bonds of NADH bound to lactate or malate dehydrogenase-ground state effects
    • Deng, H., Zheng, J., Sloan, D., Burgner, J., and Callender, R., A vibrational analysis of the catalytically important C4-H bonds of NADH bound to lactate or malate dehydrogenase-ground state effects, Biochemistry, 31, 5085-5092, 1992.
    • (1992) Biochemistry , vol.31 , pp. 5085-5092
    • Deng, H.1    Zheng, J.2    Sloan, D.3    Burgner, J.4    Callender, R.5
  • 117
    • 0023896340 scopus 로고
    • Molecular properties of p-(dimethylamino)benzaldehyde bound to liver alcohol dehydrogenase: A Raman spectroscopic study
    • Callender, R., Chen, D., Lugtenburg, J., Martin, C., Rhee, K. W., Sloan, D., Vandersteen, R., and Yue, K. T., Molecular properties of p-(dimethylamino)benzaldehyde bound to liver alcohol dehydrogenase: a Raman spectroscopic study, Biochemistry, 27, 3672-3681, 1988.
    • (1988) Biochemistry , vol.27 , pp. 3672-3681
    • Callender, R.1    Chen, D.2    Lugtenburg, J.3    Martin, C.4    Rhee, K.W.5    Sloan, D.6    Vandersteen, R.7    Yue, K.T.8
  • 118
    • 0032491153 scopus 로고    scopus 로고
    • A Raman spectroscopic characterization of bonding in the complex of horse liver alcohol dehydrogenase with NADH and N-cyclohexylformamide
    • Deng, H., Schindler, J. F., Berst, K. B., Plapp, B. V., and Callender, R., A Raman spectroscopic characterization of bonding in the complex of horse liver alcohol dehydrogenase with NADH and N-cyclohexylformamide, Biochemistry, 37, 14267-14278, 1998.
    • (1998) Biochemistry , vol.37 , pp. 14267-14278
    • Deng, H.1    Schindler, J.F.2    Berst, K.B.3    Plapp, B.V.4    Callender, R.5
  • 119
    • 0027434094 scopus 로고
    • Alternative pathways and reactions of benzyl alcohol and benzaldehyde with horse liver alcohol dehydrogenase
    • Shearer, G. L., Kim, K., Lee, K. M., Wang, C. K., and Plapp, B. V., Alternative pathways and reactions of benzyl alcohol and benzaldehyde with horse liver alcohol dehydrogenase, Biochemistry, 32, 11186-11194, 1993.
    • (1993) Biochemistry , vol.32 , pp. 11186-11194
    • Shearer, G.L.1    Kim, K.2    Lee, K.M.3    Wang, C.K.4    Plapp, B.V.5
  • 120
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W., Statistical analysis of enzyme kinetic data, Methods Enzymol., 63, 103-138, 1979.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 121
    • 85056399586 scopus 로고
    • Substrate Binding and Catalysis by Alcohol Dehydrogenases
    • The University of Iowa
    • Kim, K., Substrate Binding and Catalysis by Alcohol Dehydrogenases, Ph.D. Thesis, The University of Iowa, 1994.
    • (1994) Ph.D. Thesis
    • Kim, K.1
  • 122
    • 0017785093 scopus 로고
    • Evidence for site equivalence in the reaction mechanism of horse liver alcohol dehydrogenase with aromatic substrates at alkaline pH
    • Weidig, C. F., Halvorson, H. R., and Shore, J. D., Evidence for site equivalence in the reaction mechanism of horse liver alcohol dehydrogenase with aromatic substrates at alkaline pH, Biochemistry, 16, 2916-2922, 1977.
    • (1977) Biochemistry , vol.16 , pp. 2916-2922
    • Weidig, C.F.1    Halvorson, H.R.2    Shore, J.D.3
  • 123
    • 0018803823 scopus 로고
    • On site-site interactions in the liver alcohol dehydrogenase catalytic mechanism
    • Dunn, M. F., Bernhard, S. A., Anderson, D., Copeland, A., Morris, R. G., and Roque, J. P., On site-site interactions in the liver alcohol dehydrogenase catalytic mechanism, Biochemistry, 18, 2346-2354, 1979.
    • (1979) Biochemistry , vol.18 , pp. 2346-2354
    • Dunn, M.F.1    Bernhard, S.A.2    Anderson, D.3    Copeland, A.4    Morris, R.G.5    Roque, J.P.6
  • 124
    • 0014939331 scopus 로고
    • Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sites
    • Plapp, B. V., Enhancement of the activity of horse liver alcohol dehydrogenase by modification of amino groups at the active sites, J. Biol. Chem., 245, 1727-1735, 1970.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1727-1735
    • Plapp, B.V.1
  • 125
    • 0017821854 scopus 로고
    • Effect of pH on the process of ternary-complex inter-conversion in the liver alcohol dehydrogenase reaction
    • Kvassman, J. and Pettersson, G., Effect of pH on the process of ternary-complex inter-conversion in the liver alcohol dehydrogenase reaction, Eur. J. Biochem., 87, 417-427, 1978.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 417-427
    • Kvassman, J.1    Pettersson, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.