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On the role of organized multienzyme systems in cellular metabolism: A general synthesis

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Welch, G.Rickey·1978·Progress in Biophysics and Molecular Biology

DOI 10.1016/0079-6107(78)90019-6

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Methods of Theoretical Physics
Morse, P. M., Feshbach, H., & Hill, E. L. (1954) · American Journal of Physics · doi:10.1119/1.1933765 · Cited by 13,197
On the nature of allosteric transitions: A plausible model
Monod, J., Wyman, J., & Changeux, J.-P. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 8,825
Sociobiology: The New Synthesis.
Lenski, G., & Wilson, E. O. (1976) · Social Forces · doi:10.2307/2576242 · Cited by 6,271
Evolutionary Rate at the Molecular Level
KIMURA, M. (1968) · Nature · doi:10.1038/217624a0 · Cited by 3,737
Adaptation and Natural Selection: A Critique of Some Current Evolutionary Thought
Williams, G. C. (2008) · Project Muse (Johns Hopkins University) · doi:10.1515/9781400820108 · Cited by 2,762
Kinetics and Mechanism
Moore, J. W., Pearson, R. G., & Frost, A. A. (1961) · Andalas University Repository (Andalas University) · Cited by 2,342
Non-Darwinian Evolution: Most evolutionary change in proteins may be due to neutral mutations and genetic drift.
King, J. L., & Jukes, T. H. (1969) · Science · doi:10.1126/science.164.3881.788 · Cited by 1,768
Nonequilibrium Thermodynamics in Biophysics
Katchalsky, A., & Curran, P. F. (1965) · Harvard University Press eBooks · doi:10.4159/harvard.9780674494121 · Cited by 1,724
Structural chemistry and molecular biology
Rich, A., Davidson, N., & Pauling, L. C. (1968) · Medical Entomology and Zoology · Cited by 1,702
Evolution. The Modern Synthesis.
Huxley, J. S. (1942) · DigitalGeorgetown (Georgetown University Library) · Cited by 1,421

Show all 277 references

Research works printed but not linked: 66

Allen, 1976, 73, 665
Arroyo-Begovich, 1969, 64, 1072
Atkinson, 1970, Vol. 1, 461
Ayala, 1974, Amer. Scient., 62, 692
Berlyn, 1969, J. Bacteriol., 99, 231, 10.1128/jb.99.1.222-230.1969 · DOI
Bernhardt, 1972, 69, 1868
Berquist, 1974, 71, 4352
Boiteux, 1975, 72, 3829
Brown, 1972, 69, 1467
Brown, 1976, 73, 143
Changeux, 1967, 57, 335
Damjanovich, 1971, Vol. 6, 133
Deneubourg, 1976, Insectes Sociaux
Dixon, 1966, Vol. 2, 147
Doy, 1968, Rev. pure appl. Chem., 18, 41
Eigen, 1963, Adv. Enzymol., 25, 1
1976, 35, 2079
Florkin, 1974, Vol. 29A, 1
Fröhlich, 1975, 72, 4211
Gaertner, 1971, 30, 1131
Gaertner, 1970, Methods Enzymol., 17, 386
Ghosh, 1974, Sub-Cell. Biochem., 3, 311
Gibson, 1968, Bacteriol. Rev., 32, 465, 10.1128/br.32.4_pt_2.465-492.1968 · doi:10.1128/br.32.4_pt_2.465-492.1968
Giles, 1967, 58, 1930
Giles, 1967, 58, 1453
Goethe, 1970, Oeuvres d'Histoire Naturelle, Jacob
Goldbeter, 1973, 70, 3255
Green, 1957, Harvey Lectures, 52, 177
Green, 1973, 70, 904
Huxley, 1869, Eiseley, 335
Katchalski, 1971, Adv. Enzymol., 34, 445
Kemeny, 1974, 71, 2655
Kent, 1975, 72, 1712
Kirschner, 1972, Vol. 29, 71
Kozak, 1975, 72, 683
Laidler, 1951, Archs. Biochem., 30, 226
Likhtenshtein, 1966, Biofisika, 11, 24
Lotka, 1922, 8, 147
Lotka, 1945, Hum. Biol., 17, 167
Low, 1975, 72, 3305
L'vov, 1974, Biofizika, 19, 576
Lynen, 1972, Vol. 29, 177
Mosbach, 1976, FEBS Lett. (Suppl.), 62, E80
Odum, 1955, Am. Scient., 43, 331
Ortoleva, 1975, Vol. 29, 49
Paley, 1822, Natural Theology, 184
Prigogine, 1975, Vol. 29, 1
Rashevsky, 1973, Vol. 3, 177
Reed, 1970, Vol. 1, 213
Somogyi, 1971, Acta biochim. biophys. Acad. Sci., Hung., 6, 289
Somogyi, 1974, Acta biochim. biophys. Acad. Sci., Hung., 9, 175
Somogyi, 1974, Acta biochim. biophys. Acad. Sci., Hung., 9, 185
Somogyi, 1971, Acta biochim. biophys. Acad. Sci., Hung., 6, 353
Somogyi, 1973, Acta biochim. biophys. Acad. Sci., Hung., 8, 153
Srere, 1973, 70, 2534
Stoops, 1975, 72, 1940
Tata, 1971, Sub-Cell Biochem., 1, 83
Telford, 1975, 72, 3054
Tewari, 1973, Sub-Cell. Biochem., 2, 287
Vallee, 1968, 59, 498
Vegotsky, 1958, Enzymologia, 19, 143
Wakil, 1966, 55, 880
Wald, 1963, Vol. 3, 12
Webb, 1963, Vol. 1
Welch, 1975, 72, 4218
Wyman, 1975, 72, 3983

Micellar enzymology
MARTINEK, K., LEVASHOV, A. V., KLYACHKO, N., KHMELNITSKI, Y. L., & BEREZIN, I. V. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09512.x · Cited by 504
Adenylate Kinase and AMP Signaling Networks: Metabolic Monitoring, Signal Communication and Body Energy Sensing
Dzeja, P., & Terzic, A. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10041729 · Cited by 475
“In this way, adenylate kinase through negative and positive feedback loops governs adenine nucleotide and glycolytic oscillations providing a dynamic component for facilitated intracellular energetic signal communication [5,29,117,119].”
Background
Enzyme clustering accelerates processing of intermediates through metabolic channeling
Castellana, M., Wilson, M. Z., Xu, Y., Joshi, P., Cristea, I. M., Rabinowitz, J. D., Gitai, Z., & Wingreen, N. S. (2014) · Nature Biotechnology · doi:10.1038/nbt.3018 · Cited by 445
“(4) This implies a maximal local enzyme density nmax that cannot be exceeded27, which we modeled by the constraint”
Channeling of Substrates and Intermediates in Enzyme-Catalyzed Reactions
Huang, X., Holden, H. M., & Raushel, F. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.149 · Cited by 377
On the functional proton current pathway of electron transport phosphorylation
Kell, D. B. (1979) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(79)90018-1 · Cited by 339
The metabolon
Srere, P. A. (1985) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(85)90266-x · Cited by 301
Micellar enzymology: its relation to membranology
Martínek, K., Klyachko, N. L., Kabanov, A. V., Khmelnitsky, Y. L., & Levashov, A. V. (1989) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(89)90024-2 · Cited by 282
1 Transient-State Kinetic Analysis of Enzyme Reaction Pathways
(1992) · The Enzymes · doi:10.1016/s1874-6047(08)60019-0 · Cited by 273
Metabolite Transfer via Enzyme-Enzyme Complexes
Srivastava, D. K., & Bernhard, S. A. (1986) · Science · doi:10.1126/science.3775377 · Cited by 269
Physiological significance of metabolic channelling
Ovádi, J. (1991) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(05)80500-4 · Cited by 268
Mitochondrial and cellular mechanisms for managing lipid excess
Aon, M. A., Bhatt, N., & Cortassa, S. C. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00282 · Cited by 253
“In these biomolecular assemblies, sequential catalytic reactions proceed via transfer of the intermediates between individual component enzymes, precluding their diffusion into the bulk aqueous medium, thus “metabolically channeled” (Welch, 1977; Sumegi et al., 1991).”
Background
Metabolic compartmentation and substrate channelling in muscle cells: Role of coupled creatine kinases inin vivo regulation of cellular respiration ? a synthesis
Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y., & Kuznetsov, A. V. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01267954 · Cited by 256
Rapid Diffusion of Green Fluorescent Protein in the Mitochondrial Matrix
Partikian, A., Ölveczky, B. P., Swaminathan, R., Li, Y., & Verkman, A. S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.821 · Cited by 228
“Although extensive evidence for enzyme clustering in the mitochondrial matrix has been reported (Welch, 1977; Von Hippel and Berg, 1989; Srere and Ovadi, 1990; Robinson and Srere, 1995), which is consistent with metabolite channeling, there has been no direct measurement of solute diffusion in the matrix.”
Background
Membrane-bound ATP fuels the Na/K pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes.
Mercer, R. W., & Dunham, P. B. (1981) · The Journal of General Physiology · doi:10.1085/jgp.78.5.547 · Cited by 208
Macromolecular Compartmentation and Channeling
Ovádi, J., & Sreret, P. A. (1999) · International review of cytology · doi:10.1016/s0074-7696(08)60529-x · Cited by 205
Interactions Between Soluble Enzymes and Subcellular Structur
Masters, C. J., & Wilson, J. E. (1981) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238109108700 · Cited by 182
Spatially Organized Enzymes Drive Cofactor-Coupled Cascade Reactions
Ngo, T. A., Nakata, E., Saimura, M., & Morii, T. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10198 · Cited by 179
The role of protein fluctuations in enzyme action: A review
Welch, G. R., Somogyi, B., & Damjanovich, S. (1982) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(83)90015-9 · Cited by 179
Self-citation
Cryptobiosis 300 Years on from van Leuwenhoek: What Have We Learned about Tardigrades?
Wright, J. C. (2001) · Zoologischer Anzeiger · doi:10.1078/0044-5231-00068 · Cited by 167
Control of cellular respiration in vivo by mitochondrial outer membrane and by Creatine Kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interactions
Saks, V. A., Kuznetsov, A. V., Khuchua, Z. A., Vasilyeva, E. V., BELIKOVA, J., Kesvatera, T., & Tiivel, T. (1995) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(08)80056-9 · Cited by 164
Tryptophan Synthase: Structure, Function, and Subunit Interaction
Miles, E. W. (1979) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122945.ch4 · Cited by 162
Enzyme–Enzyme Interactions and the Regulation of Metabolic Reaction Pathways
Srivastava, D. K., & Bernhard, S. A. (1986) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152828-7.50003-2 · Cited by 161
Separation of metabolic supply and demand: aerobic glycolysis as a normal physiological response to fluctuating energetic demands in the membrane
Epstein, T., Xu, L., Gillies, R. J., & Gatenby, R. A. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-7 · Cited by 160
“Prior studies have similarly localized glycolytic metabolism adjacent to the membrane in muscle cells [32] and erythrocytes [33] and it has been suggested that this co-localization of the glycolytic enzymes expedites the production of ATP by metabolic channeling [34,35].”
Photosynthetic cytochromes of oxygenic organisms
Bendall, D. S. (1982) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(82)90008-8 · Cited by 143
Further characterization of the Krebs tricarboxylic acid cycle metabolon.
Robinson, J. B. D., Inman, L. R., Sümegi, B., & Srere, P. A. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75707-x · Cited by 142
New Perspectives on Aflatoxin Biosynthesis
Bennett, J. W., & Christensen, S. B. (1983) · Advances in applied microbiology · doi:10.1016/s0065-2164(08)70354-x · Cited by 138
Rates of membrane-associated reactions: reduction of dimensionality revisited.
McCloskey, M. A., & Poo, M. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.102.1.88 · Cited by 134
“"Channeling" of common intermediates through anabolic or catabolic pathways is often considered a function of multienzyme assemblies, be they on the membrane or elsewhere (Welch, 1977; Freedman, 1981).”
Background
The Molecular Nature of the F-actin Binding Activity of Aldolase Revealed with Site-directed Mutants
Wang, J., Morris, A. J., Tolan, D. R., & Pagliaro, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6861 · Cited by 126
Interaction between Citrate Synthase and Malate Dehydrogenase
Morgunov, I. G., & Srere, P. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29540 · Cited by 121
Adrenal Mitochondria and Steroidogenesis: From Individual Proteins to Functional Protein Assemblies
Midzak, A., & Papadopoulos, V. (2016) · Frontiers in Endocrinology · doi:10.3389/fendo.2016.00106 · Cited by 114
“Proc Natl Acad Sci U S A (2010) 107(26):11775–80.”
Background
Metabolic Dormancy in Aquatic Invertebrates
Hand, S. C. (1991) · Advances in comparative and environmental physiology · doi:10.1007/978-3-642-75900-0_1 · Cited by 107
Metabolic compartmentation and substrate channelling in muscle cells
Saks, V. A., Khuchua, Z. A., Vasilyeva, E. V., Belikova, O. Y., & Kuznetsov, A. V. (1994) · Springer eBooks · doi:10.1007/978-1-4615-2612-4_12 · Cited by 107
Organization of citric acid cycle enzymes into a multienzyme cluster
Barnes, S. J., & Weitzman, P. D. J. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80621-4 · Cited by 100
Preferential support of Ca 2+ uptake in smooth muscle plasma membrane vesicles by an endogenous glycolytic cascade
Paul, R. J., Hardin, C. D., Raeymaekers, L., Wuytack, F., & Casteels, R. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.11.2528493 · Cited by 99
“Alternately, this relatively high glycolytic flux may reflect an organization of the enzymes that allows this cascade to function in a concerted fashion at concentrations of glycolytic intermediates lower than would be expected for soluble enzymes (12).”
Background
Metabolic channelling and control of the flux
Kholodenko, B. Ν., & Westerhoff, H. V. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81660-r · Cited by 98
Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)
Dick, L. R., Moomaw, C. R., Demartino, G., & Slaughter, C. A. (1991) · Biochemistry · doi:10.1021/bi00224a022 · Cited by 98
Metabolic Compartmentation – A System Level Property of Muscle Cells
Saks, V. A., Béraud, N., & Wallimann, T. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9050751 · Cited by 94
“Thus, the possibility that physical barriers resulting from a dense cytoskeletal or mitochondrial network or from macromolecular crowding [1-27] were not taken into account at all.”
BackgroundInfluential
Crystal structure of human mitochondrial trifunctional protein, a fatty acid β-oxidation metabolon
Xia, C., Fu, Z., Battaile, K. P., & Kim, J. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816317116 · Cited by 91
“The concept of a metabolon was first proposed by Welch (16) over 40 y ago and heavily promoted by Srere (17).”
Background
Why are enzymes so big?
Srere, P. A. (1984) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(84)90221-4 · Cited by 89
The dynamic basis of energy transduction in enzymes
Somogyi, B., Welch, G. R., & Damjanovich, S. (1984) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(84)90001-6 · Cited by 87
Self-citation
Unique catalytic properties of enzyme clusters
Gaertner, F. H. (1978) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(78)94045-8 · Cited by 83
The structure of the mitochondrial inner membrane-matrix compartment
Srere, P. A. (1982) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(82)90119-0 · Cited by 84
In Vivo Detection of Brain Krebs Cycle Intermediate by Hyperpolarized Magnetic Resonance
Mishkovsky, M., Comment, A., & Rolf Gruetter, A. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.136 · Cited by 86
Compartmentation of carbohydrate metabolism in vascular smooth muscle
Lynch, R. M., & Paul, R. J. (1987) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1987.252.3.c328 · Cited by 78
[6] Fundamental mechanisms of substrate channeling
Anderson, K. S. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)08008-8 · Cited by 76
The Cytomatrix as a Cooperative System of Macromolecular and Water Networks
Shepherd, V. A. (2006) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)75006-2 · Cited by 74
Channelling can decrease pool size
Mendes, P., Kell, D. B., & Westerhoff, H. V. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16632.x · Cited by 72
Catalysis by enzymes entrapped into hydrated surfactant aggregates having lamellar or cylindrical (hexagonal) or ball‐shaped (cubic) structure in organic solvents
Klyachko, N. L., Levashov, A. V., Pshezhetsky, A. V., Bogdanova, N. G., Berezin, I. V., & Martínek, K. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb10135.x · Cited by 69
Why and when channelling can decrease pool size at constant net flux in a simple dynamic channel
Mendes, P. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(95)00152-2 · Cited by 64
Coordinate interplay between (Na+ + K+)-ATPase and creatine phosphokinase optimizes (Na+/K+)-antiport across the membrane of vesicles formed from the plasma membrane of cardiac muscle cell
Grosse, R., Spitzer, E., Kupriyanov, V. V., Saks, V. A., & REPKE, K. R. H. (1980) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(80)90397-1 · Cited by 64
Supramolecular organization of tricarboxylic acid cycle enzymes
Lyubarev, A. E., & Kurganov, B. I. (1989) · Biosystems · doi:10.1016/0303-2647(89)90038-5 · Cited by 62
Metabolic Consequences of Enzyme Interactions
Ovádi, J., & Srere, P. A. (1996) · Cell Biochemistry and Function · doi:10.1002/cbf.699 · Cited by 62
Metabolic Compartmentation
Spivey, H. O., & Merz, J. M. (1989) · BioEssays · doi:10.1002/bies.950100409 · Cited by 59
Metabolic Compartmentation in Living Cells: Structural Association of Aldolase
Wang, J., Tolan, D. R., & Pagliaro, L. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3811 · Cited by 58
Kinetic and physico-chemical analysis of enzyme complexes and their possible role in the control of metabolism
Keleti, T., Ovádi, J., & Batke, J. (1989) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(89)90016-3 · Cited by 57
Enzyme Organization and the Direction of Metabolic Flow: Physicochemical Considerations
Westerhoff, H. V., & WELCH, G. R. (1992) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152833-1.50026-5 · Cited by 56
Self-citation
Preparation and Characterization of a Bifunctional Aldolase/Kinase Enzyme: A More Efficient Biocatalyst for CC Bond Formation
Iturrate, L., Sánchez‐Moreno, I., Oroz‐Guinea, I., Pérez‐Gil, J., & García‐Junceda, E. (2010) · Chemistry - A European Journal · doi:10.1002/chem.200903096 · Cited by 53
The fractal architecture of cytoplasmic organization: Scaling, kinetics and emergence in metabolic networks
Aon, M. A., O'Rourke, B. P., & Cortassa, S. C. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009867.54552.09 · Cited by 54
“Intimate association of enzymes and ultrastructure as well as their dynamics have been considered of utmost importance in metabolic regulation [4, 38, 40, 55–65].”
Background
Structural and functional properties of a multi‐enzyme complex from spinach chloroplasts
Gontero, B., Mulliert, G., Rault, M., Giudici‐Orticoni, M., & Ricard, J. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18339.x · Cited by 52
Transient-time analysis of substrate-channelling in interacting enzyme systems
Ovádi, J., Tompa, P., Vértessy, B. G., Orosz, F., Keleti, T., & Welch, G. R. (1989) · Biochemical Journal · doi:10.1042/bj2570187 · Cited by 51
Self-citation
The mechanism of self‐assembly of the multi‐enzyme complex tryptophan synthase from Escherichia coli.
Lane, A. N., Paul, C. H., & Kirschner, K. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01797.x · Cited by 51
Protein-protein interactions
Williamson, M. P., & Sutcliffe, M. J. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380875 · Cited by 50
From protoplasmic theory to cellular systems biology: a 150-year reflection
Welch, G. R., & Clegg, J. S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00016.2010 · Cited by 51
Self-citation
On the “cytosociology” of enzyme action in vivo: A novel thermodynamic correlate of biological evolution
Welch, G. R., & Keleti, T. (1981) · Journal of Theoretical Biology · doi:10.1016/0022-5193(81)90336-2 · Cited by 50
Self-citation
Control of Metabolism by Dynamic Macromolecular Interactions
Keleti, T., & Ovádi, J. (1988) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152829-4.50003-3 · Cited by 48
The evolution of enzyme kinetic power
Keleti, T., & Welch, G. R. (1984) · Biochemical Journal · doi:10.1042/bj2230299 · Cited by 47
Self-citation
Fibronectin: chains of domains with diversified functions
VARTIO, T., & Vaheri, A. I. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90031-2 · Cited by 47
Substrate channelling in an engineered bifunctional aldolase/kinase enzyme confers catalytic advantage for C–C bond formation
Iturrate, L., Sánchez‐Moreno, I., Doyagüez, E. G., & García‐Junceda, E. (2009) · Chemical Communications · doi:10.1039/b822345a · Cited by 46
Group translocation as a mechanism for sucrose transfer into vacuoles from sugarcane cells
Thom, M., & Maretzki, A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.14.4697 · Cited by 46
Philosophical Basis and Some Historical Aspects of Systems Biology: From Hegel to Noble - Applications for Bioenergetic Research
Saks, V. A., Monge, C., & Guzun, R. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10031161 · Cited by 48
“Metabolite channeling directly transfers the intermediate from one enzyme to an adjacent enzyme without the need of free aqueous-phase diffusion [40,41,7,42-46].”
Background
Some structural and regulatory aspects of citrate synthase
Beeckmans, S. (1984) · International Journal of Biochemistry · doi:10.1016/0020-711x(84)90131-9 · Cited by 45
The indirect binding of triose-phosphate isomerase to myofibrils to form a glycolytic enzyme mini-complex
Stephan, P., Clarke, F. M., & Morton, D. (1986) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(86)90198-6 · Cited by 44
Diffusion theory, the cell and the synapse
Wheatley, D. N. (1998) · Biosystems · doi:10.1016/s0303-2647(97)00073-7 · Cited by 44
Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase).
Srivenugopal, K. S., & Adiga, P. R. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68795-8 · Cited by 43
Dynamic spatial distribution of proteins in the cell
Kaprelyants, A. S. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90024-2 · Cited by 43
Stoichiometry and composition of an aminoacyl-tRNA synthetase complex from rat liver.
Johnson, D. L., & Yang, D. C. H. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4059 · Cited by 43
A simple approach to detect active‐site‐directed enzyme‐enzyme interactions
Vértessy, B. G., & Ovádi, J. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11176.x · Cited by 41
Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase
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“One common mechanism for coordinating sequential enzymatic reactions is the formation of a multienzyme complex (34).”
Background

Authors: Welch, G. R.
Affiliations: The University of Texas Health Science Center at Houston (US)
Corresponding author: Welch, G.Rickey
Venue: Progress in Biophysics and Molecular Biology
Publisher: Elsevier BV
Published: 1978
Volume: 32
Issue: 2
Pages: 103-191
ISSN: 0079-6107 (ISSN-L)
DOI: 10.1016/0079-6107(78)90019-6
OpenAlex: W2133890603
Cited by: 260
References: 277
Citations by year: 2025: 2 · 2024: 2 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 1 · 2017: 12 · 2016: 4 · 2015: 2 · 2014: 3 · 2012: 3
FWCI: 4.72
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 15716 d)
Locations: Progress in Biophysics and Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: multienzyme systems, enzyme organization, cellular metabolism, enzyme kinetics, metabolic networks
MeSH terms: Catalysis, Cells, Diffusion, Escherichia coli, Euglena gracilis, Biological Evolution, Fatty Acids, Kinetics, Mathematics, Mitochondria, Models, Biological, Multienzyme Complexes, Neurospora crassa, Prephenate Dehydratase, Protein Conformation, Pyruvate Dehydrogenase Complex, Saccharomyces cerevisiae, Tetrahydrofolates, Tryptophan Synthase, Fatty Acid Synthases

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On the role of organized multienzyme systems in cellular metabolism: A general synthesis

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