메뉴 건너뛰기




Volumn 267, Issue 12, 2000, Pages 3442-3452

Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo

Author keywords

6 phosphogluconate dehydrogenase; Corynebacterium glutamicum; Glucosde 6 phosphate dehydrogenase; Metabolite pools; OpcA protein

Indexed keywords

GLUCOSE 6 PHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHOGLUCONATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0033946341     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01354.x     Document Type: Article
Times cited : (127)

References (52)
  • 1
    • 0030609285 scopus 로고    scopus 로고
    • Response of the central metabolism of Corynebacterium glutamicum to different flux burdens
    • 1. Marx, A., Striegel, K., de Graaf, A.A., Sahm, H. & Eggeling, L. (1997) Response of the central metabolism of Corynebacterium glutamicum to different flux burdens. Biotechnol. Bioeng. 56, 168-180.
    • (1997) Biotechnol. Bioeng. , vol.56 , pp. 168-180
    • Marx, A.1    Striegel, K.2    De Graaf, A.A.3    Sahm, H.4    Eggeling, L.5
  • 2
    • 0032600814 scopus 로고    scopus 로고
    • Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase
    • 2. Marx, A., Eikmanns, B.J., Sahm, H., de Graaf, A.A. & Eggeling, L. (1999) Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase. Metabolic Eng. 1, 35-48.
    • (1999) Metabolic Eng. , vol.1 , pp. 35-48
    • Marx, A.1    Eikmanns, B.J.2    Sahm, H.3    De Graaf, A.A.4    Eggeling, L.5
  • 3
  • 4
    • 0028086742 scopus 로고
    • Carbon flux distributions at the glucose 6-phosphate branch point in Corynebacterium glutamicum during lysine overproduction
    • 4. Vallino, J. & Stephanopoulos, G. (1994) Carbon flux distributions at the glucose 6-phosphate branch point in Corynebacterium glutamicum during lysine overproduction. Biotechnol. Prog. 10, 327-334.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 327-334
    • Vallino, J.1    Stephanopoulos, G.2
  • 5
    • 0000620741 scopus 로고
    • Regulation of 6-phoxphogluconate dehydrogenase in Brevibacterium flavum
    • 5. Sugimoto, S. & Shiio, I. (1987) Regulation of 6-phoxphogluconate dehydrogenase in Brevibacterium flavum. Agric. Biol. Chem. 51, 1257-1263.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 1257-1263
    • Sugimoto, S.1    Shiio, I.2
  • 6
    • 0000620741 scopus 로고
    • Regulation of glucose-6-phosphate dehydrogenase in Brevibacterium flavum
    • 6. Sugimoto, S. & Shiio, I. (1987) Regulation of glucose-6-phosphate dehydrogenase in Brevibacterium flavum. Agric. Biol. Chem. 51, 101-108.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 101-108
    • Sugimoto, S.1    Shiio, I.2
  • 7
    • 0016415480 scopus 로고
    • 6-Phosphogluconate dehydrogenase from Streptococcus faecalis
    • 7. Bridges, R.B. & Wittenberger, C.L. (1975) 6-Phosphogluconate dehydrogenase from Streptococcus faecalis. Methods Enzymol 41, 232-237.
    • (1975) Methods Enzymol , vol.41 , pp. 232-237
    • Bridges, R.B.1    Wittenberger, C.L.2
  • 8
    • 0033107539 scopus 로고    scopus 로고
    • In vivo dynamics of the pentose phosphate pathway in Saccharomyces cerevisiae
    • 8. Vaseghi, S., Baumeister, A., Rizzi, M. & Reuss, M. (1999) In vivo dynamics of the pentose phosphate pathway in Saccharomyces cerevisiae. Metabolic Engineering 1, 128-140.
    • (1999) Metabolic Engineering , vol.1 , pp. 128-140
    • Vaseghi, S.1    Baumeister, A.2    Rizzi, M.3    Reuss, M.4
  • 9
    • 0001400983 scopus 로고    scopus 로고
    • The glycolytic flux in E. coli appears to be controlled by the demand for ATP
    • Larsson, C., Påhlman, I.-L. & Gustafsson, L. eds, Göteborg, Sweden
    • 9. Koebmann, B.J., Nilsson, D., Snoep, J.L., Westerhoff, H.V. & Jensen, P.R. (1998) The glycolytic flux in E. coli appears to be controlled by the demand for ATP. In Biothermokinetics in the Post Genomic Era (Larsson, C., Påhlman, I.-L. & Gustafsson, L. eds), pp. 205-210. Göteborg, Sweden.
    • (1998) Biothermokinetics in the Post Genomic Era , pp. 205-210
    • Koebmann, B.J.1    Nilsson, D.2    Snoep, J.L.3    Westerhoff, H.V.4    Jensen, P.R.5
  • 10
    • 0026715777 scopus 로고
    • A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH
    • 10. de Koning, W. & van Dam, K. (1992) A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH. Anal. Biochem. 204, 118-123.
    • (1992) Anal. Biochem. , vol.204 , pp. 118-123
    • De Koning, W.1    Van Dam, K.2
  • 11
    • 0033562562 scopus 로고    scopus 로고
    • Automated sampling device for monitoring of intracellular metabolite dynamics
    • 11. Schäfer, U., Boos, W., Takors, R. & Weuster Botz, D. (1999) Automated sampling device for monitoring of intracellular metabolite dynamics. Anal. Biochem. 270, 88-96.
    • (1999) Anal. Biochem. , vol.270 , pp. 88-96
    • Schäfer, U.1    Boos, W.2    Takors, R.3    Weuster Botz, D.4
  • 12
    • 0033526410 scopus 로고    scopus 로고
    • Determination of the phosphorylated sugars of the Embden-Meyerhoff-Parnas pathway in Lactococcus lactis using a fast sampling technique and solid phase extraction
    • 12. Jensen, N.B.S., Jokumsen, K.V. & Villadsen, J. (1999) Determination of the phosphorylated sugars of the Embden-Meyerhoff-Parnas Pathway in Lactococcus lactis using a fast sampling technique and solid phase extraction. Biotechnol. Bioeng. 63, 356-362.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 356-362
    • Jensen, N.B.S.1    Jokumsen, K.V.2    Villadsen, J.3
  • 13
    • 0343471961 scopus 로고    scopus 로고
    • In vivo analysis of metabolic dynamics in Saccharomyces cerevisiae: I. Experimental observations
    • 13. Theobald, U., Mailinger, W., Baltes, M., Rizzi, M. & Reuss, M. (1997) In vivo analysis of metabolic dynamics in Saccharomyces cerevisiae: I. Experimental observations. Biotechnol. Bioeng. 55, 305-316.
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 305-316
    • Theobald, U.1    Mailinger, W.2    Baltes, M.3    Rizzi, M.4    Reuss, M.5
  • 14
    • 0017823090 scopus 로고
    • +-dependent dehydrogenases by immobilized procion red HE-3B
    • +-dependent dehydrogenases by immobilized procion red HE-3B. Biochem. J. 173, 591-596.
    • (1978) Biochem. J. , vol.173 , pp. 591-596
    • Watson, D.H.1
  • 15
    • 45949113916 scopus 로고
    • Purification of 6-phosphogluconate dehydrogenase from Acer pseudoplatanus L. using immobilized Procion Red HE-3B
    • 15. Jessup, W. & Dean, P.D.G. (1981) Purification of 6-phosphogluconate dehydrogenase from Acer pseudoplatanus L. using immobilized Procion Red HE-3B. J. Chromatogr. 219, 419-426.
    • (1981) J. Chromatogr. , vol.219 , pp. 419-426
    • Jessup, W.1    Dean, P.D.G.2
  • 16
    • 0016138153 scopus 로고
    • 6-(6-aminohexyl)-adenosine 3′,5′-bisphosphate and their application as general ligands in biospecific affinity chromatography
    • 6-(6-aminohexyl)-adenosine 3′,5′-bisphosphate and their application as general ligands in biospecific affinity chromatography. Eur. J. Biochem. 47, 81-89.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 81-89
    • Brodelius, P.1
  • 17
    • 0014064044 scopus 로고
    • A protein sequencer
    • 17. Edman, P. & Begg, G. (1967) A protein sequencer. Eur. J. Biochem. 1, 80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 18
    • 0020198680 scopus 로고
    • Electrophoresis buffers for polyacrylamide gels at various pH
    • 18. McLellan, T. (1982) Electrophoresis buffers for polyacrylamide gels at various pH. Anal. Biochem. 126, 94-99.
    • (1982) Anal. Biochem. , vol.126 , pp. 94-99
    • McLellan, T.1
  • 19
    • 0029956595 scopus 로고    scopus 로고
    • Growth of Corynebacterium glutamicum in ammonium-and potassium-limited continuous cultures under high osmotic pressure
    • 19. Guillouet, S. & Engasser, J.M. (1996) Growth of Corynebacterium glutamicum in ammonium-and potassium-limited continuous cultures under high osmotic pressure. Appl. Microbiol. Biotechnol. 46, 291-296.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 291-296
    • Guillouet, S.1    Engasser, J.M.2
  • 20
    • 0014909964 scopus 로고
    • Glutamine (amide) 2-oxoglutarate amidotransferase oxidoreductase (NADP); an enzyme involved in the synthesis of glutamate by some bacteria
    • 20. Meers, J.L., Tempest, D.W. & Brown, C.M. (1970) Glutamine (amide) 2-oxoglutarate amidotransferase oxidoreductase (NADP); an enzyme involved in the synthesis of glutamate by some bacteria. J. Gen. Microbiol. 64, 187-194.
    • (1970) J. Gen. Microbiol. , vol.64 , pp. 187-194
    • Meers, J.L.1    Tempest, D.W.2    Brown, C.M.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 21. Bradford, M.M. (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
  • 23
    • 0018411269 scopus 로고
    • The protein concentration of crude cell and tissue extracts as estimated by the method of dye binding: Comparison with the Lowry method
    • 23. Chiappelli, F., Vasil, A. & Haggerty, D.F. (1979) The protein concentration of crude cell and tissue extracts as estimated by the method of dye binding: comparison with the Lowry method. Anal. Biochem. 94, 160-165.
    • (1979) Anal. Biochem. , vol.94 , pp. 160-165
    • Chiappelli, F.1    Vasil, A.2    Haggerty, D.F.3
  • 24
    • 0026497546 scopus 로고
    • Carrier mediated glutamate secretion by Corynebacterium glutamicum under biotin limitation
    • 24. Gutmann, M., Hoischen, C. & Krämer, R. (1992) Carrier mediated glutamate secretion by Corynebacterium glutamicum under biotin limitation. Biochim. Biophys. Acta 1112, 115-123.
    • (1992) Biochim. Biophys. Acta , vol.1112 , pp. 115-123
    • Gutmann, M.1    Hoischen, C.2    Krämer, R.3
  • 25
    • 0015888084 scopus 로고
    • An improved cycling assay for nicotinamide adenine dinucleotide
    • 25. Bernofsky, C. & Swan, M. (1973) An improved cycling assay for nicotinamide adenine dinucleotide. Anal. Biochem. 53, 452-458.
    • (1973) Anal. Biochem. , vol.53 , pp. 452-458
    • Bernofsky, C.1    Swan, M.2
  • 26
    • 0343267785 scopus 로고    scopus 로고
    • Rapid extraction of (di)nucleotides from bacterial cells and determination by ion pair reversed-phase HPLC
    • 26. Müller, R.H., Loffhagen, N. & Babel, W. (1996) Rapid extraction of (di)nucleotides from bacterial cells and determination by ion pair reversed-phase HPLC. J. Microbiol. Meth. 25, 29-35.
    • (1996) J. Microbiol. Meth. , vol.25 , pp. 29-35
    • Müller, R.H.1    Loffhagen, N.2    Babel, W.3
  • 27
    • 0003443846 scopus 로고
    • Chapter 2, Verlag Chemie GmbH, Weinheim, Germany
    • 27. Bergmeyer, H.U. (1984) Methods of Enzymatic Analysis, Chapter 2, pp. 141-198. Verlag Chemie GmbH, Weinheim, Germany.
    • (1984) Methods of Enzymatic Analysis , pp. 141-198
    • Bergmeyer, H.U.1
  • 30
    • 0001211645 scopus 로고
    • Studies on liver alcohol dehydrogenase II. The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide
    • 30. Theorell, H. & Chance, B. (1951) 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) Acta Chem. Scand. , vol.5 , pp. 1127-1144
    • Theorell, H.1    Chance, B.2
  • 31
    • 0016245484 scopus 로고
    • Inhibition of glucose-6-phosphate dehydrogenase by palmitoyl coenzyme A
    • 31. Kawaguchi, A. & Bloch, K. (1974) Inhibition of glucose-6-phosphate dehydrogenase by palmitoyl coenzyme A. J. Biol. Chem. 249, 5793-5800.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5793-5800
    • Kawaguchi, A.1    Bloch, K.2
  • 32
    • 0018296923 scopus 로고
    • Glucose-6-phosphate dehydrogenases
    • Meister, A., ed., John Wiley and Sons, New York
    • 32. Levy, H.R. (1979) Glucose-6-phosphate dehydrogenases. In Advances in Enzymology (Meister, A., ed.), Vol. 48. pp. 97-192. John Wiley and Sons, New York.
    • (1979) Advances in Enzymology , vol.48 , pp. 97-192
    • Levy, H.R.1
  • 33
    • 0023318540 scopus 로고
    • The biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase
    • 33. Rosemeyer (1987) The biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase. Cell Biochem. Function 5, 79-95.
    • (1987) Cell Biochem. Function , vol.5 , pp. 79-95
  • 35
    • 0002075578 scopus 로고    scopus 로고
    • Biosynthesis and building blocks
    • Lengeler, J.W., Drews, G. & Schlegel, H.G., eds, Thieme, Stuttgart & New York
    • 35. Fuchs, G. (1999) Biosynthesis and building blocks. In Biology of the Prokaryotes (Lengeler, J.W., Drews, G. & Schlegel, H.G., eds), pp. 110-162. Thieme, Stuttgart & New York.
    • (1999) Biology of the Prokaryotes , pp. 110-162
    • Fuchs, G.1
  • 36
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • 36. Cole, S.T. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1
  • 37
    • 0031778261 scopus 로고    scopus 로고
    • Multiple oligomeric forms of glucose-6-phosphate dehydrogenase in cyanobacteria and the role of opca in the assembly process
    • 37. Sundaram, S., Karakaya, H., Scanlan, D.J. & Mann, N.H. (1998) Multiple oligomeric forms of glucose-6-phosphate dehydrogenase in cyanobacteria and the role of opcA in the assembly process. Microbiology 144, 1549-1556.
    • (1998) Microbiology , vol.144 , pp. 1549-1556
    • Sundaram, S.1    Karakaya, H.2    Scanlan, D.J.3    Mann, N.H.4
  • 38
    • 0028787216 scopus 로고
    • Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strain ATCC 29133
    • 38. Summers, M.L., Wallis, J.G., Campbell, E.L. & Meeks, J.C. (1995) Genetic evidence of a major role for glucose-6-phosphate dehydrogenase in nitrogen fixation and dark growth of the cyanobacterium Nostoc sp. strain ATCC 29133. J. Bacteriol 177, 6184-6194.
    • (1995) J. Bacteriol , vol.177 , pp. 6184-6194
    • Summers, M.L.1    Wallis, J.G.2    Campbell, E.L.3    Meeks, J.C.4
  • 39
    • 0016475699 scopus 로고
    • Human erythrocyte glucose 6-phosphate dehydrogenase. Influence of coenzyme derivatives on thermostability and kinetic properties
    • 39. De Flora, A., Morelli, A., Giuliano, F., Benatti, U. & Radin, L. (1975) Human erythrocyte glucose 6-phosphate dehydrogenase. Influence of coenzyme derivatives on thermostability and kinetic properties. Ital. J. Biochem. 24, 147-161.
    • (1975) Ital. J. Biochem. , vol.24 , pp. 147-161
    • De Flora, A.1    Morelli, A.2    Giuliano, F.3    Benatti, U.4    Radin, L.5
  • 40
    • 0017176394 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Interaction of the enzyme with coenzymes and coenzyme analogs
    • 40. Grove, T.H., Ishaque, A. & Levy, H.R. (1976) Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Interaction of the enzyme with coenzymes and coenzyme analogs. Arch. Biochem. Biophys. 177, 307-316.
    • (1976) Arch. Biochem. Biophys. , vol.177 , pp. 307-316
    • Grove, T.H.1    Ishaque, A.2    Levy, H.R.3
  • 41
    • 0018788391 scopus 로고
    • Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from methanol utilizing yeast. Candida boidinii
    • 41. Kato, N., Sahm, H., Schütte, H. & Wagner, F. (1979) Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from methanol utilizing yeast. Candida boidinii. Biochimica Biophysica Acta 566, 1-11.
    • (1979) Biochimica Biophysica Acta , vol.566 , pp. 1-11
    • Kato, N.1    Sahm, H.2    Schütte, H.3    Wagner, F.4
  • 43
    • 8544236670 scopus 로고
    • 6-Phospho-D-gluconate dehydrogenase from Gluconobacter suboxydans
    • 43. Adachi, O. & Ameyama, M. (1982) 6-Phospho-D-gluconate dehydrogenase from Gluconobacter suboxydans. Methods Enzymol 89, 291-295.
    • (1982) Methods Enzymol , vol.89 , pp. 291-295
    • Adachi, O.1    Ameyama, M.2
  • 44
    • 0025608162 scopus 로고
    • Nuclear magnetic resonance studies of cellular metabolism
    • 44. Lundberg, P., Harmsen, E., Ho, C. & Vogel, H.J. (1990) Nuclear magnetic resonance studies of cellular metabolism. Anal. Biochem. 191, 193-222.
    • (1990) Anal. Biochem. , vol.191 , pp. 193-222
    • Lundberg, P.1    Harmsen, E.2    Ho, C.3    Vogel, H.J.4
  • 45
    • 0021796287 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance studies on intact erythrocytes. Determination of intracellular pH and time course changes in phosphorus metabolites
    • 45. Mitsumori, F. (1984) Phosphorus-31 nuclear magnetic resonance studies on intact erythrocytes. Determination of intracellular pH and time course changes in phosphorus metabolites. J. Biochem. 97, 1551-1560.
    • (1984) J. Biochem. , vol.97 , pp. 1551-1560
    • Mitsumori, F.1
  • 46
    • 0016418706 scopus 로고
    • 6-Phospho-D-gluconate dehydrogenase from sheep liver
    • 46. Silverberg, M. & Daliziel, K. (1975) 6-Phospho-D-gluconate dehydrogenase from sheep liver. Methods Enzymol. 41, 215-220.
    • (1975) Methods Enzymol. , vol.41 , pp. 215-220
    • Silverberg, M.1    Daliziel, K.2
  • 47
    • 0030908487 scopus 로고    scopus 로고
    • Evidence for channeling of intermediates in the oxidative pentose phosphate pathway by soybean and pea nodule extracts, yeast extracts, and purified yeast enzymes
    • 47. Debnam, P.M., Shearer, G., Blackwood, L. & Kohl, D.H. (1997) Evidence for channeling of intermediates in the oxidative pentose phosphate pathway by soybean and pea nodule extracts, yeast extracts, and purified yeast enzymes. Eur. J. Biochem. 246, 283-290.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 283-290
    • Debnam, P.M.1    Shearer, G.2    Blackwood, L.3    Kohl, D.H.4
  • 48
    • 0021741048 scopus 로고
    • The branch point effect. Ultrasensitivety and subsensitivity to metabolic control
    • 48. LaPorte, D.C., Walsh, K. & Koshland, D.E. (1984) The branch point effect. Ultrasensitivety and subsensitivity to metabolic control. J. Biol. Chem. 259, 14068-14075.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14068-14075
    • Laporte, D.C.1    Walsh, K.2    Koshland, D.E.3
  • 49
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme-catalysed reactions
    • 49. King, E.L. & Altmann, C. (1956) A schematic method of deriving the rate laws for enzyme-catalysed reactions. J. Phys. Chem. 60, 1375-1378.
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altmann, C.2
  • 50
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalysed reactions with two or more substrates or products. I. Nomenclature and rate-equations
    • 50. Cleland, W.W. (1963) The kinetics of enzyme-catalysed reactions with two or more substrates or products. I. Nomenclature and rate-equations. Biochim. Biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 51
    • 50549188738 scopus 로고
    • The kinetics of enzyme-catalysed reactions with two or more substrates or products. II. Inhibition: Nomenclature and theory
    • 51. Cleland, W.W. (1963) The kinetics of enzyme-catalysed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim. Biophys. Acta 67, 173-187.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 173-187
    • Cleland, W.W.1
  • 52
    • 50549155520 scopus 로고
    • The kinetics of enzyme-catalysed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection
    • 52. Cleland, W.W. (1963) The kinetics of enzyme-catalysed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochim. Biophys. Acta 67, 188-196.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.