메뉴 건너뛰기




Volumn 34, Issue 1, 2010, Pages 11-18

Enzyme catalyzed reactions: From experiment to computational mechanism reconstruction

Author keywords

Biochemical pathways; Chemical information; Enzyme kinetics assays; Law of mass action; Time series analysis

Indexed keywords

BEST FIT; BIOCHEMICAL PATHWAY; CHEMICAL INFORMATION; CHEMICAL INTERACTIONS; CHEMICAL SPECIES; ENZYME CATALYZED REACTION; ENZYME CONCENTRATIONS; EXPERIMENTAL DATA; EXPERIMENTAL DESIGN; EXPERIMENTAL PROTOCOLS; FUNCTION OF TIME; HARTLEY; IN-SILICO; INPUT DATAS; KINETIC RATE PARAMETERS; LAW OF MASS ACTION; MICHAELIS-MENTEN; NETWORK RECONSTRUCTION; NUMBER OF DATUM; PRODUCT CONCENTRATION; QUALITATIVE PROPERTIES; REACTION MECHANISM; RECONSTRUCTION PROCESS; TIME COURSE;

EID: 75449116704     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2009.10.007     Document Type: Article
Times cited : (7)

References (22)
  • 1
    • 0000122278 scopus 로고
    • Statistical construction of chemical reaction mechanisms from measured time-series
    • Arkin A., and Ross J. Statistical construction of chemical reaction mechanisms from measured time-series. J. Phys. Chem. 99 (1995) 970-979
    • (1995) J. Phys. Chem. , vol.99 , pp. 970-979
    • Arkin, A.1    Ross, J.2
  • 2
    • 0020740241 scopus 로고
    • Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM-a flexible, portable system
    • Barshop B.A., Wrenn R.F., and Frieden C. Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM-a flexible, portable system. Anal. Biochem. 130 (1983) 134-145
    • (1983) Anal. Biochem. , vol.130 , pp. 134-145
    • Barshop, B.A.1    Wrenn, R.F.2    Frieden, C.3
  • 3
    • 0014056388 scopus 로고
    • Alpha-Chymotrypsin: enzyme concentration and kinetics
    • Bender M.L., Kezdy F.J., and Wedler F.C. Alpha-Chymotrypsin: enzyme concentration and kinetics. J. Chem. Educ. 44 (1967) 84-88
    • (1967) J. Chem. Educ. , vol.44 , pp. 84-88
    • Bender, M.L.1    Kezdy, F.J.2    Wedler, F.C.3
  • 4
    • 0022347426 scopus 로고
    • Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by β-lactamase I from Bacillus cereus
    • Bicknell R., and Waley S.G. Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by β-lactamase I from Bacillus cereus. Biochem. J. 231 (1985) 83-88
    • (1985) Biochem. J. , vol.231 , pp. 83-88
    • Bicknell, R.1    Waley, S.G.2
  • 7
    • 33746660306 scopus 로고    scopus 로고
    • Extracting biochemical reaction kinetics from time series data
    • Crampin E.J., McSharry P.E., and Schnell S. Extracting biochemical reaction kinetics from time series data. Lect. Notes Artif. Intell. 3214 (2004) 329-336
    • (2004) Lect. Notes Artif. Intell. , vol.3214 , pp. 329-336
    • Crampin, E.J.1    McSharry, P.E.2    Schnell, S.3
  • 8
    • 0018480388 scopus 로고
    • Consistent estimation of system order
    • Fine T.L., and Hwang W.G. Consistent estimation of system order. IEEE Trans. Auto. Control 24 (1979) 387-402
    • (1979) IEEE Trans. Auto. Control , vol.24 , pp. 387-402
    • Fine, T.L.1    Hwang, W.G.2
  • 10
    • 0015218707 scopus 로고
    • Acylation of α-and δ-Chymotrypsins by p-nitrophenyl acetate enzyme-substrate complex formation and pH dependence
    • Hardman M.J., Valenzuela P., and Bender M.L. Acylation of α-and δ-Chymotrypsins by p-nitrophenyl acetate enzyme-substrate complex formation and pH dependence. J. Biol. Chem. 246 (1971) 5907-5913
    • (1971) J. Biol. Chem. , vol.246 , pp. 5907-5913
    • Hardman, M.J.1    Valenzuela, P.2    Bender, M.L.3
  • 11
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase
    • Kuzmič P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237 (1996) 260-273
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmič, P.1
  • 12
    • 21144455036 scopus 로고    scopus 로고
    • Assessing protease activity pattern by means of multiple substrate ESI-MS assays
    • Liesener A., and Karst U. Assessing protease activity pattern by means of multiple substrate ESI-MS assays. Analyst 130 (2005) 850-854
    • (2005) Analyst , vol.130 , pp. 850-854
    • Liesener, A.1    Karst, U.2
  • 13
    • 0032406131 scopus 로고    scopus 로고
    • Non-linear optimization of biochemical pathways: applications to metabolic engineering and parameter estimation
    • Mendes P., and Kell D.B. Non-linear optimization of biochemical pathways: applications to metabolic engineering and parameter estimation. Bioinformatics. 14 (1998) 869-883
    • (1998) Bioinformatics. , vol.14 , pp. 869-883
    • Mendes, P.1    Kell, D.B.2
  • 15
    • 0842310465 scopus 로고    scopus 로고
    • Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay
    • Pi N., and Leary J.A. Determination of enzyme/substrate specificity constants using a multiple substrate ESI-MS assay. J. Am. Soc. Mass Spectrom. 15 (2004) 233-243
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 233-243
    • Pi, N.1    Leary, J.A.2
  • 18
    • 33947732288 scopus 로고    scopus 로고
    • Reconstructing biochemical pathways from time course data
    • Srividhya J., Crampin E.J., McSharry P.E., and Schnell S. Reconstructing biochemical pathways from time course data. Proteomics 7 (2007) 828-838
    • (2007) Proteomics , vol.7 , pp. 828-838
    • Srividhya, J.1    Crampin, E.J.2    McSharry, P.E.3    Schnell, S.4
  • 20
    • 33750016109 scopus 로고    scopus 로고
    • Inferring gene regulatory networks from multiple microarray datasets
    • Wang Y., Joshi T., Zhang X.-S., Xu D., and Chen L. Inferring gene regulatory networks from multiple microarray datasets. Bioinformatics 22 (2006) 2413-2420
    • (2006) Bioinformatics , vol.22 , pp. 2413-2420
    • Wang, Y.1    Joshi, T.2    Zhang, X.-S.3    Xu, D.4    Chen, L.5
  • 21
    • 0037197936 scopus 로고    scopus 로고
    • Reverse engineering gene networks using singular value decomposition and robust regression
    • Yeung M.K.S., Tegnér J., and Collins J.J. Reverse engineering gene networks using singular value decomposition and robust regression. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 6163-6168
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6163-6168
    • Yeung, M.K.S.1    Tegnér, J.2    Collins, J.J.3
  • 22
    • 0024498315 scopus 로고
    • Analysis of progress curves by simulations generated by numerical integration
    • Zimmerle C.T., and Frieden C. Analysis of progress curves by simulations generated by numerical integration. Biochem. J. 258 (1989) 381-387
    • (1989) Biochem. J. , vol.258 , pp. 381-387
    • Zimmerle, C.T.1    Frieden, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.