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Volumn 34, Issue 1-2, 1998, Pages 3-17

Mechanism from isotope effects

Author keywords

Carbon 13; Carbon 14; Competitive method; Dehydrogenases; Deuterium; Isotope effects; Malic enzyme; Nitrogen 15; Noncompetitive method; Tritium

Indexed keywords

ALCOHOL DEHYDROGENASE; ENZYME; FORMATE DEHYDROGENASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; ISOTOPE; MALATE DEHYDROGENASE; MALATE DEHYDROGENASE (OXALOACETATE DECARBOXYLATING) (NAD+); MALATE DEHYDROGENASE-(OXALOACETATE-DECARBOXYLATING) (NAD+); PHOSPHOGLUCONATE DEHYDROGENASE;

EID: 0032247029     PISSN: 10256016     EISSN: None     Source Type: Journal    
DOI: 10.1080/10256019708036327     Document Type: Article
Times cited : (26)

References (19)
  • 2
    • 0012297369 scopus 로고
    • The magnitude of the primary kinetic isotope effect for the compounds of hydrogen and deuterium
    • F. H. Westheimer: The magnitude of the primary kinetic isotope effect for the compounds of hydrogen and deuterium. Chem. Rev. 61 (1961) 265-275.
    • (1961) Chem. Rev. , vol.61 , pp. 265-275
    • Westheimer, F.H.1
  • 3
    • 0019194597 scopus 로고
    • Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions
    • P. F. Cook, J. S. Blanchard and W. W. Cleland: Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry 19 (1980) 4853-4858.
    • (1980) Biochemistry , vol.19 , pp. 4853-4858
    • Cook, P.F.1    Blanchard, J.S.2    Cleland, W.W.3
  • 4
    • 0018815070 scopus 로고
    • Measurement of isotope effects by the equilibrium perturbation technique
    • W. W. Cleland: Measurement of isotope effects by the equilibrium perturbation technique. Methods Enzymol. 64 (1980) 104-125.
    • (1980) Methods Enzymol. , vol.64 , pp. 104-125
    • Cleland, W.W.1
  • 5
    • 33947478924 scopus 로고
    • Kinetic isotope effects in the acetolysis of deuterated cyclopentyl tosylates
    • A. Streitweiser Jr., R. H. Jagow, R. C. Fahey and S. Sukuku: Kinetic isotope effects in the acetolysis of deuterated cyclopentyl tosylates. J. Am. Chem. Soc. 80 (1958) 2326-2332.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 2326-2332
    • Streitweiser Jr., A.1    Jagow, R.H.2    Fahey, R.C.3    Sukuku, S.4
  • 6
    • 0011093098 scopus 로고
    • Methods for the determination of competitive and noncompetitive kinetic isotope effects
    • P. F. Cook (Ed.): CRC Press, Boca Raton
    • D. W. Parkins: Methods for the determination of competitive and noncompetitive kinetic isotope effects. P. F. Cook (Ed.): Enzyme Mechanism from Isotope Effects, CRC Press, Boca Raton 1991, pp. 269-290.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 269-290
    • Parkins, D.W.1
  • 7
    • 0042099212 scopus 로고
    • Heavy-atom isotope effects using the isotope ratio mass spectrometer
    • P. F. Cook (Ed.): CRC Press, Boca Raton
    • P. M. Weiss: Heavy-atom isotope effects using the isotope ratio mass spectrometer. P. F. Cook (Ed.): Enzyme Mechanism from Isotope Effects, CRC Press, Boca Raton 1991, pp. 291-311.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 291-311
    • Weiss, P.M.1
  • 8
    • 0043101146 scopus 로고
    • Use of the stable isotope, remote label technique to determine isotope effects for enzyme-catalyzed reactions
    • P. F. Cook (Ed.): CRC Press, Boca Raton
    • D. M. Kiick: Use of the stable isotope, remote label technique to determine isotope effects for enzyme-catalyzed reactions. P. F. Cook (Ed.): Enzyme Mechanism from Isotope Effects, CRC Press, Boca Raton 1991, pp. 313-329.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 313-329
    • Kiick, D.M.1
  • 9
    • 0016832598 scopus 로고
    • Steady state analysis of kinetic isotope effects in enzymic reactions
    • D. B. Northrop: Steady state analysis of kinetic isotope effects in enzymic reactions. Biochemistry 14, (1975) 2644-2651.
    • (1975) Biochemistry , vol.14 , pp. 2644-2651
    • Northrop, D.B.1
  • 10
    • 0019891912 scopus 로고
    • Mechanistic deductions from isotope effects in multireactant enzyme mechanisms
    • P. F. Cook and W. W. Cleland: Mechanistic deductions from isotope effects in multireactant enzyme mechanisms. Biochemistry 20 (1981a) 1790-1796.
    • (1981) Biochemistry , vol.20 , pp. 1790-1796
    • Cook, P.F.1    Cleland, W.W.2
  • 11
    • 0019472074 scopus 로고
    • PH Variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent kinetic mechanism of alcohol dehydrogenase
    • P. F. Cook and W. W. Cleland: pH Variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent kinetic mechanism of alcohol dehydrogenase. Biochemistry 20, (1981 b) 1805-1816.
    • (1981) Biochemistry , vol.20 , pp. 1805-1816
    • Cook, P.F.1    Cleland, W.W.2
  • 12
    • 0032497367 scopus 로고    scopus 로고
    • Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants
    • submitted
    • C.-C. Hwang, A. J. Berdis, M. A. McAllister, W. W. Cleland and P. F. Cook: Oxidative decarboxylation of 6-phosphogluconate by 6-phosphogluconate dehydrogenase proceeds by a stepwise mechanism with NADP and APADP as oxidants. Biochemistry (1998) submitted.
    • (1998) Biochemistry
    • Hwang, C.-C.1    Berdis, A.J.2    McAllister, M.A.3    Cleland, W.W.4    Cook, P.F.5
  • 13
    • 0001191624 scopus 로고
    • Multiple isotope effects in enzyme-catalyzed reactions
    • P. F. Cook (Ed.): CRC Press, Boca Raton
    • W. W. Cleland: Multiple isotope effects in enzyme-catalyzed reactions. P. F. Cook (Ed.): Enzyme Mechanism from Isotope Effects, CRC Press, Boca Raton 1991, pp. 248-265.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 248-265
    • Cleland, W.W.1
  • 14
    • 0021756501 scopus 로고
    • Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. formate dehydrogenase
    • J. D. Hermes, S. W. Morrical, M. H. O'Leary and W. W. Cleland: Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. formate dehydrogenase. Biochemistry 23 (1984) 5479-5488.
    • (1984) Biochemistry , vol.23 , pp. 5479-5488
    • Hermes, J.D.1    Morrical, S.W.2    O'Leary, M.H.3    Cleland, W.W.4
  • 15
    • 0020492976 scopus 로고
    • Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose 6-phosphate dehydrogenase
    • J. D. Hermes, C. A. Roeske, M. H. O'Leary and W. W. Cleland: Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose 6-phosphate dehydrogenase. Biochemistry 21 (1982) 5106-5114.
    • (1982) Biochemistry , vol.21 , pp. 5106-5114
    • Hermes, J.D.1    Roeske, C.A.2    O'Leary, M.H.3    Cleland, W.W.4
  • 16
    • 0028230767 scopus 로고
    • Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: A reinvestigation
    • W. E. Karsten and P. F. Cook: Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: A reinvestigation. Biochemistry 33 (1994) 2096-2103.
    • (1994) Biochemistry , vol.33 , pp. 2096-2103
    • Karsten, W.E.1    Cook, P.F.2
  • 17
    • 0025837657 scopus 로고
    • Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction
    • P. M. Weiss, S. R. Gavva, B. G. Harris, J. Urbauer, W. W. Cleland and P. F. Cook: Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry 30 (1991) 5755-5763.
    • (1991) Biochemistry , vol.30 , pp. 5755-5763
    • Weiss, P.M.1    Gavva, S.R.2    Harris, B.G.3    Urbauer, J.4    Cleland, W.W.5    Cook, P.F.6
  • 18
    • 0031053278 scopus 로고    scopus 로고
    • Determination of the chemical mechanism of malic enzyme by isotope effects
    • W. A. Edens, J. Urbauer and W. W. Cleland: Determination of the chemical mechanism of malic enzyme by isotope effects. Biochemistry 36 (1997) 1141-1147.
    • (1997) Biochemistry , vol.36 , pp. 1141-1147
    • Edens, W.A.1    Urbauer, J.2    Cleland, W.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.