메뉴 건너뛰기




Volumn 52, Issue 4, 2005, Pages 765-780

Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades

Author keywords

Enzyme kinetics; Fractional modification; Multicyclic cascades; Steady state; Transient phase

Indexed keywords


EID: 31544432831     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2005_3388     Document Type: Article
Times cited : (7)

References (73)
  • 2
    • 0024597907 scopus 로고
    • Control analysis of time-dependent metabolic systems
    • Acerenza L, Sauro HM, Kacser H (1989) Control analysis of time-dependent metabolic systems. J Theor Biol 137: 423-444.
    • (1989) J Theor Biol , vol.137 , pp. 423-444
    • Acerenza, L.1    Sauro, H.M.2    Kacser, H.3
  • 3
    • 0034881019 scopus 로고    scopus 로고
    • Molecular mechanisms mediating mammalian mitogen-activated protein kinase (MAPK) kinase (MEK)-MAPK cell survival signals
    • Ballif BA, Blenis J (2001) Molecular mechanisms mediating mammalian mitogen-activated protein kinase (MAPK) kinase (MEK)-MAPK cell survival signals. Cell Growth Differ 12: 397-408.
    • (2001) Cell Growth Differ , vol.12 , pp. 397-408
    • Ballif, B.A.1    Blenis, J.2
  • 4
    • 4544300880 scopus 로고    scopus 로고
    • A walk-through of the yeast mating pheromone response pathway
    • Bardwell L (2004) A walk-through of the yeast mating pheromone response pathway. Peptides 25: 1465-1476.
    • (2004) Peptides , vol.25 , pp. 1465-1476
    • Bardwell, L.1
  • 5
    • 0037444809 scopus 로고    scopus 로고
    • Docking sites on mitogen-activated protein kinase (MAPK) kinases MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzyme activity
    • Bardwell AJ, Abdollahi M, Bardwell L (2003) Docking sites on mitogen-activated protein kinase (MAPK) kinases MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzyme activity. Biochem J 370: 1077-1085.
    • (2003) Biochem J , vol.370 , pp. 1077-1085
    • Bardwell, A.J.1    Abdollahi, M.2    Bardwell, L.3
  • 10
    • 0024578338 scopus 로고
    • Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector
    • Cárdenas ML, Cornish-Bowden A (1989) Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector. Biochem J 257: 339-345.
    • (1989) Biochem J , vol.257 , pp. 339-345
    • Cárdenas, M.L.1    Cornish-Bowden, A.2
  • 11
    • 0008195031 scopus 로고
    • Properties needed for the enzymes of an interconvertible cascade to generate a highly sensitive response
    • Cornish-Bowden A, Cárdenas ML, eds, Plenum Press, New York
    • Cárdenas ML, Cornish-Bowden A (1990) Properties needed for the enzymes of an interconvertible cascade to generate a highly sensitive response. In Control of Metabolic Processes. Cornish-Bowden A, Cárdenas ML, eds, pp 195-208. Plenum Press, New York.
    • (1990) Control of Metabolic Processes , pp. 195-208
    • Cárdenas, M.L.1    Cornish-Bowden, A.2
  • 12
    • 0030574081 scopus 로고    scopus 로고
    • The glucose-induced switch between glycogen phosphorylase and glycogen synthase in the liver: Outlines of a theoretical approach
    • Cárdenas ML, Goldbeter A (1996) The glucose-induced switch between glycogen phosphorylase and glycogen synthase in the liver: outlines of a theoretical approach J Theor Biol 182: 421-426.
    • (1996) J Theor Biol , vol.182 , pp. 421-426
    • Cárdenas, M.L.1    Goldbeter, A.2
  • 13
    • 0344832766 scopus 로고
    • Superiority of interconvertible enzyme cascades in metabolic regulation: Analysis of multicyclic systems
    • Chock PB, Stadtman ER (1977) Superiority of interconvertible enzyme cascades in metabolic regulation: analysis of multicyclic systems. Proc Natl Acad Sci USA 74: 2766-2770.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2766-2770
    • Chock, P.B.1    Stadtman, E.R.2
  • 14
    • 0018882509 scopus 로고
    • Covalently interconvertible enzyme cascade systems
    • Chock PB, Stadtman ER (1980) Covalently interconvertible enzyme cascade systems. Methods Enzymol 64: 297-325.
    • (1980) Methods Enzymol , vol.64 , pp. 297-325
    • Chock, P.B.1    Stadtman, E.R.2
  • 15
    • 0018823802 scopus 로고
    • Interconvertible enzyme cascades in cellular regulation
    • Chock PB, Rhee SG, Stadtman ER (1980) Interconvertible enzyme cascades in cellular regulation. Annu Rev Biochem 49: 813-843.
    • (1980) Annu Rev Biochem , vol.49 , pp. 813-843
    • Chock, P.B.1    Rhee, S.G.2    Stadtman, E.R.3
  • 16
    • 0038670562 scopus 로고
    • Metabolic control by cyclic cascades mechanism: A study of E. coli glutamine synthetase
    • Cornish-Bowden A, Cárdenas ML, eds, Plenum Press, New York
    • Chock PB, Rhee SG, Stadtman ER (1990) Metabolic control by cyclic cascades mechanism: a study of E. coli glutamine synthetase. In Control of Metabolic Processes. Cornish-Bowden A, Cárdenas ML, eds, pp 183-194. Plenum Press, New York.
    • (1990) Control of Metabolic Processes , pp. 183-194
    • Chock, P.B.1    Rhee, S.G.2    Stadtman, E.R.3
  • 18
    • 0026023024 scopus 로고
    • MetaModel: A program for modelling and control analysis of metabolic pathways on the IBM PC and compatibles
    • Cornish-Bowden A, Hofmeyr J-HS (1991) MetaModel: a program for modelling and control analysis of metabolic pathways on the IBM PC and compatibles. Comp Appl Biosci 7: 89-93
    • (1991) Comp Appl Biosci , vol.7 , pp. 89-93
    • Cornish-Bowden, A.1    Hofmeyr, J.-H.S.2
  • 19
    • 0036241648 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the Neurospora crassa glycogen synthase encoded by the gsn cDNA
    • De Paula R, Azzariti de Pinho C, Terenzi HF, Bertolini MC (2002) Molecular and biochemical characterization of the Neurospora crassa glycogen synthase encoded by the gsn cDNA. Mol Gent Genomics 267: 241-253.
    • (2002) Mol Gent Genomics , vol.267 , pp. 241-253
    • De Paula, R.1    Azzariti De Pinho, C.2    Terenzi, H.F.3    Bertolini, M.C.4
  • 21
    • 34250486951 scopus 로고
    • Classische Runge-Kutta Formeln vierter und niedrigerer Ordnung mit Schrittweitenkontrolle und ihre Anvendung auf Wärmeleitungs-probleme
    • Fehlberg E (1970) Classische Runge-Kutta Formeln vierter und niedrigerer Ordnung mit Schrittweitenkontrolle und ihre Anvendung auf Wärmeleitungs- probleme. Computing 6: 61-71.
    • (1970) Computing , vol.6 , pp. 61-71
    • Fehlberg, E.1
  • 22
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell JE Jr, Machleder EM (1998) The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280: 895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 24
    • 0019874460 scopus 로고
    • Transient phase kinetics of enzyme reactions
    • Gálvez J, Varón R (1981) Transient phase kinetics of enzyme reactions. J Theor Biol 89: 1-17.
    • (1981) J Theor Biol , vol.89 , pp. 1-17
    • Gálvez, J.1    Varón, R.2
  • 26
    • 0023223150 scopus 로고
    • Energy expenditure in the control of biochemical systems by covalent modification
    • Goldbeter A, Koshland DE Jr (1987) Energy expenditure in the control of biochemical systems by covalent modification. J Biol Chem 262: 4460-4471.
    • (1987) J Biol Chem , vol.262 , pp. 4460-4471
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 27
    • 31544434574 scopus 로고
    • Zero-order ultrasensitivity in interconvertible enzyme systems
    • Cornish-Bowden A, Cárdenas ML, eds, Plenum Press, New York
    • Goldbeter A, Koshland DE Jr (1990) Zero-order ultrasensitivity in interconvertible enzyme systems. In Control of Metabolic Processes. Cornish-Bowden A, Cárdenas ML, eds, pp 173-182. Plenum Press, New York.
    • (1990) Control of Metabolic Processes , pp. 173-182
    • Goldbeter, A.1    Koshland Jr., D.E.2
  • 28
    • 0032825010 scopus 로고    scopus 로고
    • Mathematical simulation and analysis of cellular metabolism and regulation
    • Goryanin I, Hodman TC, Selkov E (1999) Mathematical simulation and analysis of cellular metabolism and regulation. Bioinformatics 15: 449-758
    • (1999) Bioinformatics , vol.15 , pp. 449-758
    • Goryanin, I.1    Hodman, T.C.2    Selkov, E.3
  • 31
    • 0037082107 scopus 로고    scopus 로고
    • Mutations of muscle glycogen synthase that disable activation by glucose 6-phosphate
    • Hanashiro I, Roach PJ (2002) Mutations of muscle glycogen synthase that disable activation by glucose 6-phosphate. Arch Biochem Biophys 397: 286-292.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 286-292
    • Hanashiro, I.1    Roach, P.J.2
  • 33
    • 0002162833 scopus 로고
    • Theorems on linear systems
    • Hearon JZ (1963) Theorems on linear systems. Ann NY Acad Sci USA 108: 36-68.
    • (1963) Ann NY Acad Sci USA , vol.108 , pp. 36-68
    • Hearon, J.Z.1
  • 34
    • 0015989446 scopus 로고
    • Linear steady state treatment of enzymatic chains-general properties control and effector strength
    • Heinrich R, Rapoport TA (1974) Linear steady state treatment of enzymatic chains-general properties control and effector strength. Eur J Biochem 42: 89-95
    • (1974) Eur J Biochem , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 36
    • 0032530281 scopus 로고    scopus 로고
    • The regulation of Escherichia coli glutamine synthetase revisited: Role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state
    • Jiang P, Peliska JA, Ninfa AJ (1998) The regulation of Escherichia coli glutamine synthetase revisited: role of 2-ketoglutarate in the regulation of glutamine synthetase adenylylation state. Biochemistry 37: 12802-12810.
    • (1998) Biochemistry , vol.37 , pp. 12802-12810
    • Jiang, P.1    Peliska, J.A.2    Ninfa, A.J.3
  • 40
    • 0037237791 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor receptor-2 activity by caveolin-1 and plasma membrane cholesterol
    • Labrecque L, Royal I, Surprenant DS, Patterson C, Gingras D, Béliveau R (2003) Regulation of vascular endothelial growth factor receptor-2 activity by caveolin-1 and plasma membrane cholesterol. Mol Biol Cell 14: 334-347.
    • (2003) Mol Biol Cell , vol.14 , pp. 334-347
    • Labrecque, L.1    Royal, I.2    Surprenant, D.S.3    Patterson, C.4    Gingras, D.5    Béliveau, R.6
  • 41
    • 0030034961 scopus 로고    scopus 로고
    • Gain and kinetics of activation in the G-protein cascade of phototransduction
    • Lamb TD (1996) Gain and kinetics of activation in the G-protein cascade of phototransduction. Proc Natl Acad Sci USA 93: 566-570.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 566-570
    • Lamb, T.D.1
  • 42
    • 0030921160 scopus 로고    scopus 로고
    • Biochemistry by numbers: Simulation of biochemical pathways with Gepasi 3
    • Mendes P (1997) Biochemistry by numbers: simulation of biochemical pathways with Gepasi 3. Trends Biochem Sci 22: 361-363.
    • (1997) Trends Biochem Sci , vol.22 , pp. 361-363
    • Mendes, P.1
  • 43
    • 0038712811 scopus 로고    scopus 로고
    • Allosteric interactions and bifunctionality make the response of glutamine synthetase cascade system of Escherichia coli robust and ultrasensitive
    • Mutalik VK, Shah P, Venkatesh KV (2003) Allosteric interactions and bifunctionality make the response of glutamine synthetase cascade system of Escherichia coli robust and ultrasensitive. J Biol Chem 278: 26327-26332.
    • (2003) J Biol Chem , vol.278 , pp. 26327-26332
    • Mutalik, V.K.1    Shah, P.2    Venkatesh, K.V.3
  • 44
    • 0842281546 scopus 로고    scopus 로고
    • Robust global sensitivity in multiple enzyme cascade system explains how the downstream cascade structure may remain unaffected by cross-talk
    • Mutalik VK, Singh AP, Edwards JS, Venkatesh KV (2004) Robust global sensitivity in multiple enzyme cascade system explains how the downstream cascade structure may remain unaffected by cross-talk. FEBS Lett 558: 79-84.
    • (2004) FEBS Lett , vol.558 , pp. 79-84
    • Mutalik, V.K.1    Singh, A.P.2    Edwards, J.S.3    Venkatesh, K.V.4
  • 45
    • 0021266684 scopus 로고
    • Substrate cycles: Their role in improving sensitivity in metabolic control
    • Newsholme EA, Challiss RAJ, Crabtree B (1984) Substrate cycles: their role in improving sensitivity in metabolic control. Trends Biochem Sci 9: 277-280.
    • (1984) Trends Biochem Sci , vol.9 , pp. 277-280
    • Newsholme, E.A.1    Challiss, R.A.J.2    Crabtree, B.3
  • 49
    • 0034704085 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone and cyclic AMP activate p38 mitogen-activated protein kinase cascade
    • Pomerance M, Abduullah HB, Kamerji S, Corrèze C, Blondeau JP (2000) Thyroid-stimulating hormone and cyclic AMP activate p38 mitogen-activated protein kinase cascade. J Biol Chem 275: 40539-40546.
    • (2000) J Biol Chem , vol.275 , pp. 40539-40546
    • Pomerance, M.1    Abduullah, H.B.2    Kamerji, S.3    Corrèze, C.4    Blondeau, J.P.5
  • 50
    • 0141750574 scopus 로고    scopus 로고
    • 2+ oscillations on activation of glycogen phosphorylase
    • 2+ oscillations on activation of glycogen phosphorylase. Biophys Chem 106: 193-202.
    • (2003) Biophys Chem , vol.106 , pp. 193-202
    • Rozi, A.1    Jia, Y.2
  • 52
    • 0027178664 scopus 로고
    • SCAMP: A general-purpose simulator and metabolic control analysis program
    • Sauro HM (1993) SCAMP: a general-purpose simulator and metabolic control analysis program. Comp Appl Biosci 9: 441-450.
    • (1993) Comp Appl Biosci , vol.9 , pp. 441-450
    • Sauro, H.M.1
  • 53
    • 0002203999 scopus 로고    scopus 로고
    • JARNAC: A system for interactive metabolic analysis
    • Hofmeyr J-HS, Rohwer JM, Snoep JL, eds, Stellenbosch University Press, Stellenbosch
    • Sauro HM (2000) JARNAC: a system for interactive metabolic analysis. In Animating the Cellular Map. Hofmeyr J-HS, Rohwer JM, Snoep JL, eds, pp 221-228. Stellenbosch University Press, Stellenbosch.
    • (2000) Animating the Cellular Map , pp. 221-228
    • Sauro, H.M.1
  • 54
    • 0031878025 scopus 로고    scopus 로고
    • Control analysis of muscle glycogen metabolism
    • Schulz AR (1998) Control analysis of muscle glycogen metabolism. Arch Biochem Biophys 353: 172-180.
    • (1998) Arch Biochem Biophys , vol.353 , pp. 172-180
    • Schulz, A.R.1
  • 55
  • 57
    • 0025208219 scopus 로고
    • Discovery of glutamine synthetase cascade
    • Stadtman ER (1990) Discovery of glutamine synthetase cascade. Methods Enzymol 182: 793-809.
    • (1990) Methods Enzymol , vol.182 , pp. 793-809
    • Stadtman, E.R.1
  • 58
    • 0035976909 scopus 로고    scopus 로고
    • The story of glutamine synthetase regulation
    • Stadtman ER (2001) The story of glutamine synthetase regulation. J Biol Chem 276: 44357-44364.
    • (2001) J Biol Chem , vol.276 , pp. 44357-44364
    • Stadtman, E.R.1
  • 59
    • 0344832766 scopus 로고
    • Superiority of interconvertible enzyme cascades in metabolic regulation: Analysis of monocyclic systems
    • Stadtman ER, Chock PB (1977) Superiority of interconvertible enzyme cascades in metabolic regulation: analysis of monocyclic systems. Proc Nat Acad Sci USA 74: 2761-2765.
    • (1977) Proc Nat Acad Sci USA , vol.74 , pp. 2761-2765
    • Stadtman, E.R.1    Chock, P.B.2
  • 60
    • 31544441693 scopus 로고
    • Advantages of enzyme cascades in the regulation of key metabolic processes
    • Schmidtt FO, ed, M.I.T. Press, Cambridge
    • Stadtman ER, Chock PB (1979) Advantages of enzyme cascades in the regulation of key metabolic processes. In The Neurosciences Fourth Study Program. Schmidtt FO, ed, pp 801-817. M.I.T. Press, Cambridge.
    • (1979) The Neurosciences Fourth Study Program , pp. 801-817
    • Stadtman, E.R.1    Chock, P.B.2
  • 62
    • 0026527708 scopus 로고
    • Response coefficients of interconvertible enzyme cascades towards effectors that act on one or both modifier enzymes
    • Szedlacsek SE, Cárdenas ML, Cornish-Bowden A (1992) Response coefficients of interconvertible enzyme cascades towards effectors that act on one or both modifier enzymes. Eur J Biochem 204: 807-813.
    • (1992) Eur J Biochem , vol.204 , pp. 807-813
    • Szedlacsek, S.E.1    Cárdenas, M.L.2    Cornish-Bowden, A.3
  • 63
    • 0036111831 scopus 로고    scopus 로고
    • Attenuation of noise in ultrasensitive signaling cascades
    • Thattai M, van Oudenaarden A (2002) Attenuation of noise in ultrasensitive signaling cascades. Biophys J 82: 2943-2950.
    • (2002) Biophys J , vol.82 , pp. 2943-2950
    • Thattai, M.1    Van Oudenaarden, A.2
  • 64
    • 0030586273 scopus 로고    scopus 로고
    • Optimizing enzymatic cycling assays: Spectrophotometric determination of pyruvate and L-lactate
    • Valero E, García-Carmona F (1996) Optimizing enzymatic cycling assays: spectrophotometric determination of pyruvate and L-lactate. Anal Biochem 239: 47-52.
    • (1996) Anal Biochem , vol.239 , pp. 47-52
    • Valero, E.1    García-Carmona, F.2
  • 65
    • 0030740566 scopus 로고    scopus 로고
    • Mathematical model for the determination of enzyme activity based on enzymatic amplification by substrate cycling
    • Valero E, Varón R, García-Carmona F (1997) Mathematical model for the determination of enzyme activity based on enzymatic amplification by substrate cycling. Anal Chim Acta 346: 215-221.
    • (1997) Anal Chim Acta , vol.346 , pp. 215-221
    • Valero, E.1    Varón, R.2    García-Carmona, F.3
  • 66
    • 0034663477 scopus 로고    scopus 로고
    • Kinetics of a self-amplifying substrate cycle: ADP-ATP cycling assay
    • Valero E, Varón R, García-Carmona F (2000) Kinetics of a self-amplifying substrate cycle: ADP-ATP cycling assay. Biochem J 350: 237-243.
    • (2000) Biochem J , vol.350 , pp. 237-243
    • Valero, E.1    Varón, R.2    García-Carmona, F.3
  • 67
    • 0031602226 scopus 로고    scopus 로고
    • Cytokine and protease glycosylation as a regulatory mechanism in inflammation and autoimmunity
    • Van den Steen P, Rudd PM, Dwek RA, Van Damme J, Opdenakker G (1998) Cytokine and protease glycosylation as a regulatory mechanism in inflammation and autoimmunity. Avd Exp Med Biol 435: 133-143.
    • (1998) Avd Exp Med Biol , vol.435 , pp. 133-143
    • Van Den Steen, P.1    Rudd, P.M.2    Dwek, R.A.3    Van Damme, J.4    Opdenakker, G.5
  • 68
    • 0025369137 scopus 로고
    • Kinetics of the transient phase and steady-state of the monocyclic enzyme cascades
    • Varón R, Havsteen BH (1990) Kinetics of the transient phase and steady-state of the monocyclic enzyme cascades. J Theor Biol 14: 397-413.
    • (1990) J Theor Biol , vol.14 , pp. 397-413
    • Varón, R.1    Havsteen, B.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.