Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 313

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Cellular concentrations of enzymes and their substrates

Albe, Kathy R., Butler, Margaret H., Wright, Barbara E.·1990·Journal of Theoretical Biology

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/s0022-5193(05)80266-8

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 239

  1. Beeckmans, 1981, Demonstration of physical interactions between consecutive enzymes of the citric acid cycle and of the aspartate-malate shuttle: a study involving fumarase, malate dehydrogenase, citrate synthase and aspartate aminotransferase, Eur. J. Biochem., 117, 527, 10.1111/j.1432-1033.1981.tb06369.x · DOI
  2. Block, 1971, The nucleotide and acyl group content of native rabbit muscle glyceraldegyde-3-phosphate dehydrogenase, J. biol. Chem., 246, 780, 10.1016/S0021-9258(18)62478-0 · DOI
  3. Brammer, 1972, Distribution of α-amylase-resistant regions in the glycogen molecule, Carbohydrate Res., 24, 343, 10.1016/S0008-6215(00)85068-5 · DOI
  4. Chock, 1989, A reexamination of the kinetic evidence in support of the direct transfer mechanism in the glycolytic pathway, J. Cell Biol., 107, 836a
  5. Clarke, 1975, On the association of glycolytic enzymes with structural proteins of skeletal muscle, Biochem. biophys. Acta, 381, 37, 10.1016/0304-4165(75)90187-7 · DOI
  6. Clarke, 1976, Aldolase binding to actin-containing filaments: formation of paracrystals, Biochem. J., 159, 797, 10.1042/bj1590797 · doi:10.1042/bj1590797
  7. Fahien, 1983, Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase, Arch. biochem. Biophys., 220, 386, 10.1016/0003-9861(83)90428-9 · DOI
  8. Halper, 1977, Interaction between citrate synthase and mitochondrial malate dehydrogenase in the presence of polyethyleneglycol, Arch. biochem. Biophys., 184, 529, 10.1016/0003-9861(77)90462-3 · doi:10.1016/0003-9861(77)90462-3
  9. Heinrich, 1977, Metabolic regulation and mathematical models, Prog. biophys. molec. Biol., 32, 1, 10.1016/0079-6107(78)90017-2 · DOI · Paper page
  10. Hintz, 1984, Heterogeneity in regard to enzymes and metabolites within individual muscle fibers, Am. J. Physiol., 246, C288, 10.1152/ajpcell.1984.246.3.C288 · DOI
  11. Kelleher, 1978, A kinetic analysis of glucokinase and glucose-6-phosphate phosphatase in Dictyostelium, Molec. Cell. Biochem., 19, 67, 10.1007/BF00232596 · doi:10.1007/bf00232596
  12. Kelly, 1979, Glycogen phosphorylase from Dictyostelium: a kinetic analysis by computer simulation, Biosystems, 11, 55, 10.1016/0303-2647(79)90020-0 · doi:10.1016/0303-2647(79)90020-0
  13. Koch-Schmidt, 1977, Eur. J. Biochem., 81, 71, 10.1111/j.1432-1033.1977.tb11928.x · doi:10.1111/j.1432-1033.1977.tb11928.x
  14. Kohn, 1977, Distribution of adenine nucleotides in the perfused rat heart, Am J. Physiol., 232, R158
  15. Leu, 1970, Metabolic compartmentation at the molecular level: the function of a multienzyme aggregate in the pyrimidine pathway of yeast, Biochim. biophys. Acta, 220, 365, 10.1016/0005-2744(70)90268-8 · DOI
  16. London, 1966, A theoretical study of hepatic glycogen metabolism, J. biol. Chem., 241, 3008, 10.1016/S0021-9258(18)96490-2 · DOI
  17. McMinn, 1976, On the control of enzyme pathways, J. theor. Biol., 56, 57, 10.1016/S0022-5193(76)80045-8 · doi:10.1016/s0022-5193(76)80045-8
  18. Ottaway, 1977, The role of compartmentation in the control of glycolysis, Curr. Top. cell. Regul., 12, 107, 10.1016/B978-0-12-152812-6.50010-X · DOI
  19. Propaczy, 1983, Association between the α-ketoglutarate dehydrogenase complex and succinate thiokinase, Biochim. biophys. Acta, 749, 172, 10.1016/0167-4838(83)90249-2 · DOI
  20. Robinson, 1985, Organization of Krebs' tricarboxylic acid cycle enzymes in mitochondria, J. biol. Chem., 260, 10800, 10.1016/S0021-9258(19)85153-0 · DOI
  21. Seraydarian, 1962, The amount and compartmentalization of adenosine diphosphate in muscle, Biochem. biophys. Acta, 65, 443, 10.1016/0006-3002(62)90447-X · DOI
  22. Sols, 1970, Concentration of metabolites and binding sites. Implication in metabolic regulation, Curr. Top. cell. Regul., 2, 227, 10.1016/B978-0-12-152802-7.50013-X · DOI
  23. Srere, 1967, Enzyme concentrations in tissues, Science, 158, 936, 10.1126/science.158.3803.936 · DOI · Paper page
  24. Srivastava, 1986, Enzyme-enzyme interactions and the regulation of metabolic reaction pathways, Curr. Top. cell. Regul., 28, 1, 10.1016/B978-0-12-152828-7.50003-2 · DOI · Paper page
  25. Srivastava, 1986, Metabolite transfer via enzyme-enzyme complexes, Science, 234, 1081, 10.1126/science.3775377 · DOI · Paper page
  26. Sumegi, 1985, Interaction between citrate synthase and thiolase, J. biol. Chem., 260, 188, 10.1016/S0021-9258(18)89713-7 · doi:10.1016/s0021-9258(18)89713-7
  27. Sumegi, 1980, Interaction between the pyruvate dehydrogenase complex and citrate synthase, Biochim. biophys. Acta, 616, 158, 10.1016/0005-2744(80)90134-5 · doi:10.1016/0005-2744(80)90134-5
  28. Walsh, 1978, Kinetics of net RNA degradation during development in Dictyostelium discoideum, J. gen. Microbiol., 108, 57, 10.1099/00221287-108-1-57 · DOI
  29. Wistow, 1987, The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses, Nature, Lond., 326, 622, 10.1038/326622a0 · DOI
  30. Wright, 1986, Measuring metabolic control with kinetic models, Trends Biochem. Sci., 11, 164, 10.1016/0968-0004(86)90133-7 · doi:10.1016/0968-0004(86)90133-7
  31. Wright, 1981, Kinetic models of metabolism in intact cells, tissues, and organisms, Curr. Top. cell. Regul., 19, 103, 10.1016/B978-0-12-152819-5.50021-X · DOI
  32. Fox, 1976, Biosynthesis of bacterial glycogen. Purification and properties of Escherichia coli B ADP-glucose: 1,4-α-D-glucan 4-α-glucosyl transferase, Biochemistry, 15, 849, 10.1021/bi00649a019 · DOI
  33. Huang, 1974, Yeast glycogen synthetase in the glucose-6-phosphate dependent form. I. Purification and properties, J. biol. Chem., 249, 3851, 10.1016/S0021-9258(19)42552-0 · doi:10.1016/s0021-9258(19)42552-0
  34. Lin, 1973, Homogenous glycogen synthetase b from rat liver, J. biol. Chem., 248, 7007, 10.1016/S0021-9258(19)43352-8 · DOI
  35. Brown, 1971, Molecular characteristics of the totally dependent and independent forms of glycogen synthetase of rabbit skeletal muscle. I. Preparation and characteristics of the totally glucose 6-phosphate dependent form, Biochim. biophys. Acta, 242, 69, 10.1016/0005-2744(71)90088-X · DOI
  36. Hawker, 1974, Interaction of spinach leaf adenosine diphosphate glucose α-1,4-glucan α-4-glucosyl transferase and α-1,4-glucan, α-1,4-glucan-6-glycosyl transferase in synthesis of branched α-glucan, Arch. biochem. Biophys., 160, 530, 10.1016/0003-9861(74)90430-5 · DOI · Paper page
  37. Fosset, 1972, Glycogen phosphorylases a and b from yeast, Meth. Enzymol., 28, 960, 10.1016/0076-6879(72)28139-3 · doi:10.1016/0076-6879(72)28139-3
  38. Thomas, 1976, Glycogen phosphorylase in Dictyostelium discoideum. I. Purification and properties of the enzyme, J. biol. Chem., 251, 1253, 10.1016/S0021-9258(17)33733-X · doi:10.1016/s0021-9258(17)33733-x
  39. Sevilla, 1969, The purification and properties of rat muscle glycogen phosphorylase, Biochemistry, 8, 2161, 10.1021/bi00833a057 · doi:10.1021/bi00833a057
  40. Preiss, 1980, Characterization of the spinach leaf phosphorylases, Plant Physiol., 66, 864, 10.1104/pp.66.5.864 · DOI
  41. Ozaki, 1972, ADP-glucose pyrophosphorylase from Escherichia coli, Meth. Enzymol., 28, 539, 10.1016/0076-6879(72)28077-6 · doi:10.1016/0076-6879(72)28077-6
  42. Gustafson, 1973, Analysis of uridine diphosphate-glucose pyrophosphorylase synthesis during differentiation in Dictyostelium discoideum, J. biol. Chem., 248, 5188, 10.1016/S0021-9258(19)43688-0 · doi:10.1016/s0021-9258(19)43688-0
  43. Villar-Palasi, 1963, UDPG pyrophosphorylase from muscle, Meth. Enzymol., 6, 355, 10.1016/0076-6879(63)06186-3 · doi:10.1016/0076-6879(63)06186-3
  44. Tsuba, 1969, Purification and specific kinetic properties of erythrocyte uridine diphosphate pyrophosphorylase, J. biol. Chem., 244, 1008, 10.1016/S0021-9258(18)91886-7 · DOI
  45. Ribereau-Gayon, 1971, ADP-glucose pyrophosphorylase from spinach leaf, Meth. Enzymol., 23, 618, 10.1016/S0076-6879(71)23135-9 · DOI
  46. Maitra, 1975, Glucokinase from yeast, Meth. Enzymol., 42, 25, 10.1016/0076-6879(75)42087-0 · doi:10.1016/0076-6879(75)42087-0
  47. Baumann, 1969, Glucokinase of Dictyostelium discoideum, Biochemistry, 8, 5011, 10.1021/bi00840a050 · doi:10.1021/bi00840a050
  48. Grossman, 1974, The preparation and characterization of pure rat liver glucokinase, J. biol. Chem., 249, 3055, 10.1016/S0021-9258(19)42636-7 · DOI
  49. Lazarus, 1966, Yeast hexokinase. I. Preparation of the pure enzyme, Biochemistry, 5, 4003, 10.1021/bi00876a035 · doi:10.1021/bi00876a035
  50. Easterby, 1982, Hexokinase Type II from rat skeletal muscle, Meth. Enzymol., 90, 11, 10.1016/S0076-6879(82)90098-2 · doi:10.1016/s0076-6879(82)90098-2
  51. Joshi, 1964, Phosphoglucomutase I. Purification and properties of phosphoglucomutase from Escherichia coli, J. biol. Chem., 239, 2741, 10.1016/S0021-9258(18)93809-3 · DOI
  52. Joshi, 1982, Phosphoglucomutase from yeast, Meth. Enzymol., 89, 599, 10.1016/S0076-6879(82)89103-9 · doi:10.1016/s0076-6879(82)89103-9
  53. Cleland, 1968, Activities of glycolytic enzymes during the early stages of differentiation in the cellular slime mold Dictyostelium discoideum, Biochim. biophys. Acta, 156, 44, 10.1016/0304-4165(68)90102-5 · doi:10.1016/0304-4165(68)90102-5
  54. Scopes, 1982, Purification of all glycolytic enzymes from one muscle extract, Meth. Enzymol., 90, 479, 10.1016/S0076-6879(82)90175-6 · doi:10.1016/s0076-6879(82)90175-6
  55. Ray, 1978, The binding of lithium and of anionic metabolites to phosphoglucomutase, Biochim. biophys. Acta, 522, 434, 10.1016/0005-2744(78)90076-1 · DOI
  56. Nakgawa, 1965, Isolation of crystalline phosphoglucose isomerase from brewer's yeast, J. biol. Chem., 240, 1877, 10.1016/S0021-9258(18)97398-9 · doi:10.1016/s0021-9258(18)97398-9
  57. Thomas, 1981, Partial purification and characterization of glucose-6-phosphate isomerase from Dictyostelium discoideum, J. gen. Microbiol., 124, 403
  58. Phillips, 1976, Isolation of rabbit muscle glucose phosphate isomerase by a single-step substrate elution, Biochim. biophys. Acta, 429, 624, 10.1016/0005-2744(76)90311-9 · doi:10.1016/0005-2744(76)90311-9
  59. Tilley, 1974, A point mutation increasing the stability of human phosphoglucose isomerase, J. biol. Chem., 249, 4571, 10.1016/S0021-9258(19)42456-3 · doi:10.1016/s0021-9258(19)42456-3
  60. Kotlarz, 1982, Phosphofructokinases from Escherichia coli, Meth. Enzymol., 90, 60, 10.1016/S0076-6879(82)90107-0 · DOI
  61. Hofmann, 1982, Phosphofructokinase from yeast, Meth. Enzymol., 90, 49, 10.1016/S0076-6879(82)90106-9 · DOI
  62. Baumann, 1968, The phosphofructokinase of Dictyostelium discoideum, Biochemistry, 7, 3653, 10.1021/bi00850a044 · doi:10.1021/bi00850a044
  63. Wenzel, 1972, Purification of human erythrocyte phosphofructokinase, FEBS Lett., 19, 281, 10.1016/0014-5793(72)80060-7 · doi:10.1016/0014-5793(72)80060-7
  64. Rutter, 1966, Fructose diphosphate aldolase, Meth. Enzymol., 9, 479, 10.1016/0076-6879(66)09099-2 · DOI
  65. Gracy, 1970, Structural relationships in aldolases purified from rat liver and muscle and Novikoff hepatoma, Arch. biochem. Biophys., 136, 480, 10.1016/0003-9861(70)90219-5 · doi:10.1016/0003-9861(70)90219-5
  66. Penhoet, 1975, Detection and isolation of mammalian fructosediphosphate aldolases, Meth. Enzymol., 42, 240, 10.1016/0076-6879(75)42121-8 · DOI
  67. Yeltman, 1982, Fructose-bisphosphate aldolase from human erythroytes, Meth. Enzymol., 90, 251, 10.1016/S0076-6879(82)90134-3 · doi:10.1016/s0076-6879(82)90134-3
  68. Horecker, 1975, Fructose bisphosphate aldolase from spinach, Meth. Enzymol., 42, 234, 10.1016/0076-6879(75)42120-6 · doi:10.1016/0076-6879(75)42120-6
  69. Krietsch, 1975, Triosephosphate isomerase from yeast, Meth. Enzymol., 41, 434, 10.1016/S0076-6879(75)41094-1 · doi:10.1016/s0076-6879(75)41094-1
  70. Esnouf, 1982, Triosephosphate isomerase from chicken and rabbit muscle, Meth. Enzymol., 89, 579, 10.1016/S0076-6879(82)89100-3 · doi:10.1016/s0076-6879(82)89100-3
  71. Gracy, 1975, Triose phosphate isomerase from human erythrocytes, Meth. Enzymol., 41, 442, 10.1016/S0076-6879(75)41096-5 · doi:10.1016/s0076-6879(75)41096-5
  72. D'Alessio, 1971, Glycerladehyde phosphate dehydrogenase, phosphoglycerate kinase, and phosphoglyceromutase of Escherichia coli, J. biol. Chem., 242, 4319, 10.1016/S0021-9258(18)62087-3 · doi:10.1016/s0021-9258(18)62087-3
  73. Byers, 1982, Glyceraldehyde-3-phosphate dehydrogenase from yeast, Meth. Enzymol., 89, 326, 10.1016/S0076-6879(82)89059-9 · DOI
  74. Speranza, 1982, Glyceraldehyde-3-phosphate dehydrogenase (glycolytic form) from spinach leaves, Meth. Enzymol., 89, 316, 10.1016/S0076-6879(82)89057-5 · doi:10.1016/s0076-6879(82)89057-5
  75. D'Alessio, 1975, Phosphoglycerate kinase and phosphoglycerate mutase from Escherichia coli, Meth. Enzymol., 42, 139, 10.1016/0076-6879(75)42107-3 · doi:10.1016/0076-6879(75)42107-3
  76. Kulbe, 1982, 3-phosphoglycerate kinase from bovine liver and yeast, Meth. Enzymol., 90, 115, 10.1016/S0076-6879(82)90116-1 · doi:10.1016/s0076-6879(82)90116-1
  77. Kuntz, 1982, Phosphoglycerate kinase from animal tissues, Meth. Enzymol., 90, 103, 10.1016/S0076-6879(82)90114-8 · doi:10.1016/s0076-6879(82)90114-8
  78. Scopes, 1975, 3-phosphoglycerate kinase of skeletal muscle, Meth. Enzymol., 42, 127, 10.1016/0076-6879(75)42105-X · doi:10.1016/0076-6879(75)42105-x
  79. Kuntz, 1982, Phosphoglycerate kinase from spinach, blue-green algae, and yeast, Meth. Enzymol., 90, 110, 10.1016/S0076-6879(82)90115-X · doi:10.1016/s0076-6879(82)90115-x
  80. Grisolia, 1975, Phosphoglycerate mutase from yeast, chicken breast muscle, and kidney (2, 3-PGA-dependent), Meth. Enzymol., 42, 435, 10.1016/0076-6879(75)42149-8 · DOI
  81. Spring, 1975, Enolase from Escherichia coli, Meth. Enzymol., 42, 323, 10.1016/0076-6879(75)42135-8 · doi:10.1016/0076-6879(75)42135-8
  82. Westhead, 1966, Enolase from yeast and rabbit muscle, Meth. Enzymol., 9, 670, 10.1016/0076-6879(66)09136-5 · doi:10.1016/0076-6879(66)09136-5
  83. Rider, 1974, Enolase isoenzymes in rat tissue. Electrophoretic, chromatographic, immunological and kinetic properties, Biochem. biophys. Acta, 365, 285
  84. Malcovati, 1982, AMP- and Fructose 1,6-bisphosphate- activated pyruvate kinases from Escherichia coli, Meth. Enzymol., 90, 170, 10.1016/S0076-6879(82)90123-9 · doi:10.1016/s0076-6879(82)90123-9
  85. Aust, 1975, Pyruvate kinase from yeast (Saccharomyces cerevisiae), Meth. Enzymol., 42, 176, 10.1016/0076-6879(75)42112-7 · doi:10.1016/0076-6879(75)42112-7
  86. Imamura, 1982, Pyruvate kinase isoenzymes from rat, Meth. Enzymol., 90, 150, 10.1016/S0076-6879(82)90121-5 · DOI
  87. Kahn, 1982, Pyruvate kinases from human erythrocytes and liver, Meth. Enzymol., 90, 131, 10.1016/S0076-6879(82)90119-7 · doi:10.1016/s0076-6879(82)90119-7
  88. Kaczorowski, 1978, Purification and properties of D-lactate dehydrogenase from Escherichia coli ML 308-225, Meth. Enzymol., 53, 519, 10.1016/S0076-6879(78)53054-1 · doi:10.1016/s0076-6879(78)53054-1
  89. Pontremoli, 1975, Fructose 1,6-diphosphatase and sedoheptulose-1,7-diphosphate from Candida utilis, Meth. Enzymol., 42, 347, 10.1016/0076-6879(75)42139-5 · doi:10.1016/0076-6879(75)42139-5
  90. Baumann, 1969, The fructose-1,6-diphosphatase of Dictyostelium discoideum, Biochemistry, 8, 1655, 10.1021/bi00832a047 · doi:10.1021/bi00832a047
  91. Marcus, 1982, Fructose-1,6-bisphosphatase from rat liver, Meth. Enzymol., 90, 352, 10.1016/S0076-6879(82)90155-0 · DOI
  92. MacGregor, 1982, Fructose-1,6-bisphosphatase from chicken and rabbit muscle, Meth. Enzymol., 90, 340, 10.1016/S0076-6879(82)90152-5 · doi:10.1016/s0076-6879(82)90152-5
  93. Kelly, 1982, Fructose-bisphosphatase from spinach leaf chloroplast and cytoplasm, Meth. Enzymol., 90, 371, 10.1016/S0076-6879(82)90158-6 · doi:10.1016/s0076-6879(82)90158-6
  94. Kuby, 1966, Glucose 6-phosphate dehydrogenase (brewer's yeast), Meth. Enzymol., 9, 116, 10.1016/0076-6879(66)09029-3 · doi:10.1016/0076-6879(66)09029-3
  95. Thomas, 1979, Pentose phosphate metabolism during differentiation in Dictyostelium discoideum, J. gen. Microbiol., 113, 357, 10.1099/00221287-113-2-357 · DOI
  96. Matsuda, 1967, Glucose-6-phosphate dehydrogenase from rat liver. I. Crystallization and properties, J. Biochem., 61, 535, 10.1093/oxfordjournals.jbchem.a128583 · doi:10.1093/oxfordjournals.jbchem.a128583
  97. Holten, 1972, Relationships among the multiple molecular forms of rat liver glucose-6-phosphate dehydrogenase, Biochim. biophys. Acta, 268, 4, 10.1016/0005-2744(72)90190-8 · doi:10.1016/0005-2744(72)90190-8
  98. Cohen, 1975, Glucose-6-phosphate dehydrogenase from human erythrocytes, Meth. Enzymol., 41, 208, 10.1016/S0076-6879(75)41049-7 · doi:10.1016/s0076-6879(75)41049-7
  99. Veronese, 1976, Isolation and properties of 6-phosphogluconate dehydrogenase from Escherichia coli. Some comparisons with the thermophilic enzyme from Bacillus stearothermophilus, Biochemistry, 15, 4026, 10.1021/bi00663a017 · doi:10.1021/bi00663a017
  100. Rippa, 1975, 6-phosphogluconate from Canadida utilis, Meth. Enzymol., 41, 237, 10.1016/S0076-6879(75)41054-0 · doi:10.1016/s0076-6879(75)41054-0
  101. Pearse, 1975, 6-phosphogluconate dehydrogenase from human erythrocytes, Meth. Enzymol., 41, 220, 10.1016/S0076-6879(75)41051-5 · doi:10.1016/s0076-6879(75)41051-5
  102. Domagk, 1975, Ribose-5-phosphate isomerase from Candida utilis, Meth. Enzymol., 41, 427, 10.1016/S0076-6879(75)41092-8 · doi:10.1016/s0076-6879(75)41092-8
  103. Rutner, 1970, Spinach 5-phosphoribose isomerase. Purification and properties of the enzyme, Biochemistry, 9, 178, 10.1021/bi00803a023 · doi:10.1021/bi00803a023
  104. Williamson, 1966, Ribulose 5-phosphate 3-epimerase, Meth. Enzymol., 9, 605, 10.1016/0076-6879(66)09122-5 · doi:10.1016/0076-6879(66)09122-5
  105. Tabachnick, 1958, The oxidative pentose phosphate cycle. III. Interconversion of ribose 5-phosphate, ribulose 5-phosphate and xylulose 5-phosphate, Arch. biochem. Biophys., 74, 315, 10.1016/0003-9861(58)90003-1 · doi:10.1016/0003-9861(58)90003-1
  106. Wood, 1981, The preparation of transketolase free from D-ribulose-5-phosphate 3-epimerase, Biochim. biophys. Acta, 659, 233, 10.1016/0005-2744(81)90049-8 · doi:10.1016/0005-2744(81)90049-8
  107. Kochetov, 1982, Transketolase from yeast, rat liver, and pig liver, Meth. Enzymol., 90, 209, 10.1016/S0076-6879(82)90128-8 · doi:10.1016/s0076-6879(82)90128-8
  108. Schellenberg, 1982, Transketolase from human red blood cells, Meth. Enzymol., 90, 223, 10.1016/S0076-6879(82)90129-X · DOI
  109. Tsolas, 1975, Transaldolase, Meth. Enzymol., 42, 290, 10.1016/0076-6879(75)42130-9 · doi:10.1016/0076-6879(75)42130-9
  110. Siegel, 1975, Ribulose-diphosphate carboxylase from spinach leaves, Meth. Enzymol., 42, 234
  111. McCurry, 1982, Ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach, tomato, or tobacco leaves, Meth. Enzymol., 90, 515, 10.1016/S0076-6879(82)90178-1 · doi:10.1016/s0076-6879(82)90178-1
  112. Saito, 1967, Galactose 1-phosphate uridyltransferase of Escherichia coli, J. biol. Chem., 242, 2362, 10.1016/S0021-9258(18)95970-3 · doi:10.1016/s0021-9258(18)95970-3
  113. Fukasawa, 1982, Uridine diphosphate glucose-4-epimerase and uridyltransferase from Saccharomyces cerevisiae, Meth. Enzymol., 89, 584, 10.1016/S0076-6879(82)89101-5 · doi:10.1016/s0076-6879(82)89101-5
  114. Wilson, 1982, Galactokinase from Saccharomyces cerevisiae, Meth. Enzymol., 90, 30, 10.1016/S0076-6879(82)90102-1 · doi:10.1016/s0076-6879(82)90102-1
  115. Blume, 1971, Publication and properties of galactokinase from human red blood cells, J. biol. Chem., 246, 6507, 10.1016/S0021-9258(19)34143-2 · doi:10.1016/s0021-9258(19)34143-2
  116. Segal, 1970, L-alanine aminotransferase (rat liver), Meth. Enzymol., 17A, 153, 10.1016/0076-6879(71)17171-6 · DOI
  117. Porter, 1981, Purification and basic properties of the aspartate aminotransferases from a variety of sources, Comp. biochem. Physiol., 69B, 737
  118. Huynh, 1980, Glutamic oxaloacetic transaminase isoenzymes from rat liver. Purification and physiochemical characterization, J. Biochem., 88, 231
  119. Coranner, 1970, Tyrosine aminotransferase (rat liver), Meth. Enzymol., 17A, 633
  120. Veronese, 1975, Glutamate dehydrogenase from Escherichia coli: induction, purification and properties, Biochim. biophys. Acta, 377, 217, 10.1016/0005-2744(75)90304-6 · DOI
  121. Doherty, 1970, Glutamate dehydrogenase (yeast), Meth. Enzymol., 17A, 850, 10.1016/0076-6879(71)17294-1 · DOI
  122. Shapiro, 1970, Glutamine synthetase (Escherichia coli), Meth. Enzymol., 17A, 910, 10.1016/0076-6879(71)17305-3 · DOI · Paper page
  123. Meister, 1985, Glutamine synthetase from mammalian tissues, Meth. Enzymol., 113, 185, 10.1016/S0076-6879(85)13030-2 · DOI
  124. Rowe, 1985, Glutamine synthetase from muscle, Meth. Enzymol., 113, 199, 10.1016/S0076-6879(85)13031-4 · DOI
  125. Schimke, 1970, Arginase (rat liver), Meth. Enzymol., 17A, 313, 10.1016/0076-6879(71)17203-5 · doi:10.1016/0076-6879(71)17203-5
  126. Fonda, 1983, L-glutamate decarboxylase from bacteria, Meth. Enzymol., 113, 11, 10.1016/S0076-6879(85)13005-3 · DOI
  127. Robinson, 1971, D-Serine-dehydrase (Escherichia coli), Meth. Enzymol., 17B, 356, 10.1016/0076-6879(71)17062-0 · doi:10.1016/0076-6879(71)17062-0
  128. Simon, 1971, L-serine dehydrase from rat liver. Purification and some properties, Biochim. biophys. Acta, 321, 361, 10.1016/0005-2744(73)90091-0 · DOI
  129. Williams, 1971, Glutathione reductase, Meth. Enzymol., 17B, 503, 10.1016/0076-6879(71)17089-9 · doi:10.1016/0076-6879(71)17089-9
  130. Colman, 1971, Glutathione reductase (yeast), Meth. Enzymol., 17B, 500, 10.1016/0076-6879(71)17088-7 · DOI
  131. Carlberg, 1985, Glutathione reductase, Meth. Enzymol., 113, 484, 10.1016/S0076-6879(85)13062-4 · DOI · Paper page
  132. Staal, 1969, Purification and properties of glutathione reductase of human erythrocytes, Biochim. biophys. Acta, 350, 39, 10.1016/0005-2744(69)90280-0 · DOI · Paper page
  133. Morris, 1983, Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli, Meth. Enzymol., 94, 125, 10.1016/S0076-6879(83)94020-X · doi:10.1016/s0076-6879(83)94020-x
  134. Tyagi, 1983, Ornithine decarboxylase (Saccharomyces cerevisiae), Meth. Enzymol., 94, 135, 10.1016/S0076-6879(83)94021-1 · doi:10.1016/s0076-6879(83)94021-1
  135. Hayashi, 1983, Ornithine decarboxylase (rat liver), Meth. Enzymol., 94, 154, 10.1016/S0076-6879(83)94024-7 · doi:10.1016/s0076-6879(83)94024-7
  136. Boeker, 1971, Arginine decarboxylase (Escherichia coli), Meth. Enzymol., 17B, 657, 10.1016/0076-6879(71)17114-5 · doi:10.1016/0076-6879(71)17114-5
  137. White, 1971, Diaminopimelate decarboxylase (Escherichia coli), Meth. Enzymol., 17B, 140, 10.1016/0076-6879(71)17031-0 · doi:10.1016/0076-6879(71)17031-0
  138. Tamir, 1971, Dihdrodipicolinic acid reductase (Escherichia coli), Meth. Enzymol., 17B, 134, 10.1016/0076-6879(71)17030-9 · doi:10.1016/0076-6879(71)17030-9
  139. Shepherdson, 1962, Aspartate transcarbamoyl from Escherichia coli, Meth. Enzymol., 5, 925, 10.1016/S0076-6879(62)05337-9 · doi:10.1016/s0076-6879(62)05337-9
  140. Anderson, 1970, Carbamoyl phosphate synthetase (Escherichia coli), Meth. Enzymol., 17A, 235, 10.1016/0076-6879(71)17187-X · DOI
  141. Guthohrlein, 1968, Structure and function of carbamoylphosphate synthetase. I. Transitions between two catalytically inactive forms and the active form, Eur. J. Biochem., 7, 119, 10.1111/j.1432-1033.1968.tb19582.x · DOI
  142. Tokushigi, 1985, Aspartate ammonialyase, Meth. Enzymol., 113, 618, 10.1016/S0076-6879(85)13083-1 · doi:10.1016/s0076-6879(85)13083-1
  143. Boeker, 1983, Lysine decarboxylase (Escherichia coli), Meth. Enzymol., 94, 180, 10.1016/S0076-6879(83)94030-2 · doi:10.1016/s0076-6879(83)94030-2
  144. Pizer, 1971, 3-phosphoglycerate dehydrogenase (Escherichia coli), Meth. Enzymol., 17B, 325, 10.1016/0076-6879(71)17056-5 · doi:10.1016/0076-6879(71)17056-5
  145. Thorner, 1975, Glycerol kinase, Meth. Enzymol., 42, 148, 10.1016/0076-6879(75)42109-7 · doi:10.1016/0076-6879(75)42109-7
  146. Albe, 1989, Purification and kinetic characterization of uridine phosphorylase from Dictyostelium discoideum, Exp. Mycol., 13, 13, 10.1016/0147-5975(89)90003-0 · doi:10.1016/0147-5975(89)90003-0
  147. Kraut, 1971, Cytoplasmic uridine phosphorylase of rat liver: characterization and kinetics, J. biol. Chem., 246, 2021, 10.1016/S0021-9258(19)77183-X · doi:10.1016/s0021-9258(19)77183-x
  148. Smith, 1971, Escherichia coli phosphoenolpyruvate carboxylase: physical and chemical properties, J. biol. Chem., 246, 4234, 10.1016/S0021-9258(18)62076-9 · DOI
  149. Miziorko, 1974, Spinach leaf phosphoenolpyruvate carboxylase: purification, properties, and kinetic studies, Arch. biochem. Biophys., 163, 378, 10.1016/0003-9861(74)90489-5 · doi:10.1016/0003-9861(74)90489-5
  150. Young, 1969, Pyruvate carboxylase from Saccharomyces cerevisiae, Meth. Enzymol., 13, 250, 10.1016/0076-6879(69)13044-X · doi:10.1016/0076-6879(69)13044-x
  151. McClure, 1971, Rat liver pyruvate carboxylase. I. Preparation, properties, and cation specificity, J. biol. Chem., 246, 3569, 10.1016/S0021-9258(18)62167-2 · DOI
  152. Visser, 1982, Pyruvate dehydrogenase from Escherichia coli, Meth. Enzymol., 89, 391, 10.1016/S0076-6879(82)89069-1 · doi:10.1016/s0076-6879(82)89069-1
  153. Kresze, 1981, Pyruvate dehydrogenase complex from baker's yeast. 1. Purification and some kinetic and regulatory properties, Eur. J. Biochem., 119, 573, 10.1111/j.1432-1033.1981.tb05646.x · DOI
  154. Butler, 1985, The pyruvate dehydrogenase complex in Dictyostelium discoideum, Curr. Top. cell. Regul., 26, 337, 10.1016/B978-0-12-152826-3.50032-2 · doi:10.1016/b978-0-12-152826-3.50032-2
  155. Faloona, 1969, Escherichia coli citrate synthase. Purification and the effect of potassium on some properties, Biochemistry, 8, 4497, 10.1021/bi00839a041 · DOI
  156. Parvin, 1969, Citrate synthase from yeast, Meth. Enzymol., 13, 16, 10.1016/0076-6879(69)13007-4 · doi:10.1016/0076-6879(69)13007-4
  157. Porter, 1977, Partial purification of citrate synthase from Dictyostelium discoideum, Arch. biochem. Biophys., 181, 155, 10.1016/0003-9861(77)90493-3 · doi:10.1016/0003-9861(77)90493-3
  158. Moriyama, 1971, Purification of rat heart and rat liver citrate synthases: physical, kinetic, and immunological studies, J. biol. Chem., 246, 3217, 10.1016/S0021-9258(18)62217-3 · DOI
  159. Srere, 1969, Citrate synthase, Meth. Enzymol., 13, 3, 10.1016/0076-6879(69)13005-0 · DOI · Paper page
  160. Hy, 1976, NADP+-specific isocitrate dehydrogenase of Escherichia coli. III. Two-step purification employing affinity chromatography, Biochim. biophys. Acta, 445, 280, 10.1016/0005-2744(76)90082-6 · doi:10.1016/0005-2744(76)90082-6
  161. Kornberg, 1955, Isocitrate dehydrogenase of yeast (DPN), Meth. Enzymol., 1, 707, 10.1016/0076-6879(55)01123-3 · doi:10.1016/0076-6879(55)01123-3
  162. Emyanitoff, 1982, Purification and characterization of NAD-dependent isocitrate dehydrogenase from Dictyostelium discoideum, Exp. Mycology, 6, 274, 10.1016/0147-5975(82)90120-7 · doi:10.1016/0147-5975(82)90120-7
  163. Cleland, 1969, Isocitrate dehydrogenase (TPN-specific) from pig heart, Meth. Enzymol., 13, 30, 10.1016/0076-6879(69)13011-6 · DOI
  164. Gibson, 1967, Succinyl coenzyme A synthetase from Escherichia coli. I. Purification and properties, J. biol. Chem., 242, 2474, 10.1016/S0021-9258(18)95986-7 · doi:10.1016/s0021-9258(18)95986-7
  165. Cha, 1969, Succinate thiokinase from pig heart, Meth. Enzymol., 13, 62, 10.1016/0076-6879(69)13017-7 · DOI
  166. Reed, 1969, α-ketoglutarate dehydrogenase complex from Escherichia coli, Meth. Enzymol., 13, 55, 10.1016/0076-6879(69)13016-5 · DOI · Paper page
  167. Heckert, 1989, Purification and characterization of α-ketoglutarate dehydrogenase complex from Dictyostelium discoideum, J. gen. Microbiol., 135, 155
  168. Kaufman, 1955, α-ketoglutarate dehydrogenase system and phosphorylating enzyme from heart muscle, Meth. Enzymol., 1, 714, 10.1016/0076-6879(55)01125-7 · DOI
  169. Veeger, 1969, Succinate dehydrogenase, Meth. Enzymol., 13, 81, 10.1016/0076-6879(69)13020-7 · DOI
  170. Murphy, 1969, Malate dehydrogenase from Escherichia coli, Meth. Enzymol., 13, 145, 10.1016/0076-6879(69)13029-3 · doi:10.1016/0076-6879(69)13029-3
  171. Emyanitoff, 1982, Kinetic characterization of mitochondrial malate dehydrogenase from Dictyostelium discoideum, J. gen. Microbiol., 128, 1767
  172. Wada, 1975, Crystallization and properties of rat liver malate dehydrogenase (decarboxylating) (NADP+), Biocheim. biophys. Acta, 410, 237
  173. Yamagushi, 1973, Studies on regulatory functions of malic enzyme. II. Purification and molecular properties of nicotinamide adenine dinucleotide-linked malic enzyme from Escherichia coli, J. Biochem., 73, 169
  174. Kelleher, 1979, Amino acid catabolism and malic enzyme in differentiating Dictyostelium discoideum, J. Bact., 138, 467, 10.1128/JB.138.2.467-474.1979 · DOI
  175. Li, 1975, Nicotinamide adenine dinucleotide phosphate—malic enzyme of rat liver, J. biol. Chem., 250, 141, 10.1016/S0021-9258(19)41992-3 · doi:10.1016/s0021-9258(19)41992-3
  176. Sweierczynski, 1980, Purification and some properties of extramitochondrial malic enzyme from rat skeletal muscle, Biochim. biophys. Acta, 616, 10, 10.1016/0005-2744(80)90258-2 · doi:10.1016/0005-2744(80)90258-2
  177. Smith, 1971, Molecular characteristics of the totally dependent and independent forms of glycogen synthase of rabbit skeletal muscle. II. Some chemical characteristics of the enzyme protein and of its change on interconversion, Biochim. biophys. Acta, 242, 81, 10.1016/0005-2744(71)90089-1 · DOI
  178. Barnard, 1975, Hexokinases from yeast, Meth. Enzymol., 42, 6, 10.1016/0076-6879(75)42085-7 · doi:10.1016/0076-6879(75)42085-7
  179. Chou, 1972, Purification and properties of rat brain hexokinase, Arch. biochem. Biophys., 151, 48, 10.1016/0003-9861(72)90471-7 · doi:10.1016/0003-9861(72)90471-7
  180. Daugherty, 1975, Purification and properties of phosphoglucomutase from Fleischmann's yeast, Eur. J. Biochem., 57, 115, 10.1111/j.1432-1033.1975.tb02282.x · DOI
  181. Gracy, 1975, Phosphoglucose isomerase of human erythrocytes and cardiac tissue, Meth. Enzymol., 41, 392, 10.1016/S0076-6879(75)41086-2 · doi:10.1016/s0076-6879(75)41086-2
  182. Leonard, 1972, The self-association of rabbit-muscle phosphofructokinase, Eur. J. Biochem., 26, 442, 10.1111/j.1432-1033.1972.tb01785.x · DOI
  183. Wenzel, 1972, Evidence for different oligomeric forms of human erythrocyte phosphofructokinase, FEBS Lett, 19, 285, 10.1016/0014-5793(72)80061-9 · doi:10.1016/0014-5793(72)80061-9
  184. Harris, 1969, The molecular characteristics of yeast aldolase, Biochemistry, 8, 2442, 10.1021/bi00834a029 · DOI
  185. Kawahara, 1966, The number of polypeptide chains in rabbit muscle aldolase, Biochemistry, 5, 1578, 10.1021/bi00869a018 · doi:10.1021/bi00869a018
  186. Scheek, 1982, Glyceraldehyde-3 phosphate dehydrogenase from rabbit muscle, Meth. Enzymol., 89, 305, 10.1016/S0076-6879(82)89055-1 · doi:10.1016/s0076-6879(82)89055-1
  187. Mann, 1970, Molecular weight and subunit structure of yeast enolase, Biochemistry, 9, 4002, 10.1021/bi00822a020 · DOI
  188. Shimizu, 1983, Characterization of αα, ββ, δδ, and αδ human enolase isoenzymes and preparation of hybrid enolases (αδ, βδ, and αβ) from homodimeric forms, Biochim. biophys. Acta, 748, 278, 10.1016/0167-4838(83)90305-9 · doi:10.1016/0167-4838(83)90305-9
  189. Steinmetz, 1966, Metabolic control and structure of glycolytic enzymes. III. Dissociation and subunit structure of rabbit muscle pyruvate kinase, Biochemistry, 5, 1399, 10.1021/bi00868a038 · doi:10.1021/bi00868a038
  190. Andrews, 1965, The gel-filtration behavior of proteins related to their molecular weights over a wide range, Biochem. J., 96, 595, 10.1042/bj0960595 · DOI · Paper page
  191. Domagk, 1975, Glucose 6-phosphate dehydrogenases from Candida utilis, Meth. Enzymol., 41, 205, 10.1016/S0076-6879(75)41048-5 · doi:10.1016/s0076-6879(75)41048-5
  192. Domagk, 1973, Purification and properties of ribosephosphate isomerase from Candida utilis, Eur. J. Biochem., 38, 259, 10.1111/j.1432-1033.1973.tb03057.x · DOI
  193. Yagi, 1985, Glutamate-aspartate aminotransferase from microorganisms, Meth. Enzymol., 113, 83, 10.1016/S0076-6879(85)13020-X · DOI
  194. Doonan, 1981, Interspecies comparisons of aspartate aminotransferases based on amino acid compositions, Comp. biochem. Physiol., 69B, 747
  195. Yagi, 1982, Aspartate: 2-oxoglutarate aminotransferase from baker's yeast, J. Biochem., 92, 35, 10.1093/oxfordjournals.jbchem.a133929 · doi:10.1093/oxfordjournals.jbchem.a133929
  196. Auricchio, 1970, Studies on the structure of tyrosine aminotransferase, Biochim. biophys. Acta, 221, 307, 10.1016/0005-2795(70)90271-0 · doi:10.1016/0005-2795(70)90271-0
  197. Hemmings, 1977, The regulation of glutamate metabolism in Candida utilis: evidence for two interconvertible forms of NAD-dependent glutamate dehydrogenase, Eur. J. Biochem., 80, 143, 10.1111/j.1432-1033.1977.tb11866.x · doi:10.1111/j.1432-1033.1977.tb11866.x
  198. Hirsch-Kolb, 1968, Molecular characteristics of rat liver arginase, J. biol. Chem., 243, 6123, 10.1016/S0021-9258(18)94469-8 · doi:10.1016/s0021-9258(18)94469-8
  199. Cohlberg, 1972, Structure and arrangement of the regulatory subunits in aspartate transcarbamylase, Biochemistry, 11, 3396, 10.1021/bi00768a013 · doi:10.1021/bi00768a013
  200. Trotta, 1978, Glutamine-dependent carbamoyl-phosphate synthetase (Escherichia coli): preparation of subunits, Meth. Enzymol., 51, 21, 10.1016/S0076-6879(78)51005-7 · doi:10.1016/s0076-6879(78)51005-7

200 of 239 shown

Cited by

See all 313

Metadata

Authors
Albe, K. R., Butler, M. H., & Wright, B. E.
Venue
Journal of Theoretical Biology
Publisher
Elsevier BV
Published
1990-03
Volume
143
Issue
2
Pages
163-195
ISSN
0022-5193 (ISSN-L)
OpenAlex
W2036099201
Cited by
313
References
2
FWCI
2.43
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Cellular concentrations of enzymes and their substrates. https://app.cochat.ai/papers/10.1016/s0022-5193(05)80266-8
The paper
Albe, K. R., Butler, M. H., & Wright, B. E. (1990). Cellular concentrations of enzymes and their substrates. Journal of Theoretical Biology. https://doi.org/10.1016/s0022-5193(05)80266-8

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.