Escherichia coli kinetics

Akiyama, S. IC, and Hamme.s, G. G., 1980. Elementary. step.s in die reaction mechani.sm of die pyruvate dehydrogena.se mnltienzyme complex from Escherichia coli Kinetics of acetylation and deacetylation. Biochemistry 19 4208-4213. 

Shames, S.L. Wedler, RC. Homoserine kinase of Escherichia coli kinetic mechanism and inhibition by L-aspartate semialdehyde. Arch. Biochem. Biophys., 235, 359-370 (1984)... 

Ertl P, Unterladstaetter B, Bayer K, Mikkelsen SR (2000) Ferricyanide reduction by escherichia coli kinetics, mechanism, and application to the optimization of recombinant fermentations. Anal Chem 72(20) 4949-4956. doi 10.1021/ac000358d... 

Comparison of whole cell biocatalytic reaction kinetics for recombinant Escherichia coli with periplasmic-secreting or cytoplasmic-expressing organophosphorus hydrolase... 

D Ham, C. Romieu, A. Jaquinod, M. Gasparutto, D. Cadet, J. Excision of 5,6-dihydroxy-5,6-dihydrothymine, 5,6-dihydrothymine, and 5- hydroxycytosine from defined sequence oligonucleotides by Escherichia coli endonuclease III and Fpg proteins Kinetic and mechanistic aspects. Biochemistry 1999, 38, 3335-3344. 

Chang JS, Kuo TS (2000) Kinetics of bacterial decolorization of azo dye with Escherichia coli N03. Bioresour Technol 75 107-111... 

D. Visser, J. W. Schmid, K.Mauch, M. Reuss, and J. J. Heijnen, Optimal re design of primary metabolism in Escherichia coli using linlog kinetics. Metab. Eng. 6(4), 378 390 (2004). 

K. Balasingham, D. Warburton, P. Dunhill, M. D. Lilly, The Isolation and Kinetics of Penicillin Amidase from Escherichia coli , Biochem. Biophys. Acta 1972, 276, 250-256. 

Selected entries from Methods in Enzymology [vol, page(s)] Equilibrium isotope exchange study of kinetic mechanism, 249, 466 site-directed mutagenesis of Escherichia coli enzyme, 249, 93 positional isotope exchange studies, 249, 423 product inhibition studies of three substrates three products reactions, 249, 207-208. 

M. L. Sinnot and P. J. Smith, Affinity labelling with deaminatively generated carbonium ion. Kinetics and stoicheiometry of die alkylation of methionine-500 of die lacZ p-galactosidase of Escherichia coli by p-D-galactopyranosylmethyl-p-nitrophenyltriazene, Biochem. J., 175 (1978) 525—538. 

R.S. Cozzone, A.J. Gortay, J.G. Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues. Eur. J. Biochem., 237, 247-254 (1996)... 

Zhang, W.W. Jiang, W.H. Zhao, G.P. Yang, Y.L. Chiao, J.S. Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase from the rifamycin SV-producing Amycolatopsis mediterranei U32. Appl. Microbiol. Biotechnol., 54, 52-58 (2000)... 

Chauvin, R Brand, L. Roseman, S. Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy. J. Biol. Chem., 269, 20270-20274 (1994)... 

Recorbet, G., Picard, C., Normand, P. Simonet, P. (1993). Kinetics of the persistence of chromosomal DNA from genetically engineered Escherichia coli introduced to soil. Applied and Environmental Microbiology, 59, 4289-94. 

Other bacterial mutants, such as a mutant Escherichia coli enzyme tolerant to glyphosate, have been described (47). The E. coli mutant had a single amino acid change from the wild type, resulting in substitution of glycine 96 with alanine. An identical mutation was reported in glyphosate-tolerant Klebsiella pneumoniae (48). The nature of changes in the kinetic constants of the K pneumoniae enzyme is similar to that of the E. coli enzyme. 

Enantioselective enzymatic amide hydrolyses can also be applied for the preparation of optically active organosilicon compounds. The first example of this is the kinetic resolution of the racemic [l-(phenylacetamido)ethyl] silane rac-84 using immobilized penicillin G acylase (PGA E.C. 3.5.1.11) from Escherichia coli as the biocatalyst (Scheme 18)69. (R)-selective hydrolysis of rac-84 yielded the corresponding (l-aminoethyl)silane (R)-85 which was obtained on a preparative scale in 40% yield (relative to rac-84). The enantiomeric purity of the biotransformation product was 92% ee. This method has not yet been used for the synthesis of optically active silicon compounds with the silicon atom as the center of chirality. 

Campbell JM, Schulte-Frohlinde D, von Sonntag C (1974) Quantum yields in the UV photolysis of 5-bromo-uracil in the presence of hydrogen donors. Photochem Photobiol 20 465-467 Chapman JD (1984) The cellular basis of radiotherapeutic response. Radiat Phys Chem 24 283-291 Chatterjee M, Mah SC, Tullius TD, Townsend CA (1995) Role of the aryl iodide in the sequence-selective cleavage of DNA by calicheamicin. Importance of thermodynamic binding vs kinetic activation process. J Am Chem Soc 117 8074-8082 Chaudry MA, Weinfeld M (1995) The action of Escherichia coli endonuclease III on multiply damaged sites in DNA. J Mol Biol 249 914-922... 

Zuccotti S, Zanardi D, Rosano C et al (2001) Kinetic and crystallographic analyses support a sequential-ordered bi-bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase. J Mol Biol 313 831-843... 

Cole, P., and Crothers, D. (1972). Conformational changes of transfer ribonucleic acid. Relaxation kinetics of the early melting transition of methionine transfer ribonucleic acid (Escherichia coli). Biochemistry 11(23), 4368—4374. 

MT Record Jr, WS Reznikoff, ML Craig, KL McQuade, PJ Schlax. Escherichia coli RNA polymerase (Eo70), promoters, and the kinetics of the steps of transcription initiation. In FC Neidhardt, ed. Escherichia coli and Salmonella. Cellular and Molecular Biology. Washington, DC ASM Press, 1996, pp 792-821. 

The NADP-IDH from Escherichia coli has been thoroughly studied. It is a dimeric protein of two identical 40-kDa subunits. High-resolution X-ray crystal structures have been determined for the enzyme with and without substrate [16,17], and for the pseudo-Michaelis complex of the enzyme with isocitrate and NADP [18], Structures of sequential intermediates formed during the catalytic action of IDH are also available [19], Additionally, the kinetic and catalytic mechanisms have been determined in detail [20], Amino acid residues which are involved in interactions with substrate, coenzyme, metal ions, and catalysis have been identified [10,21],... 

AM Dean, DE Koshland Jr. The kinetic mechanism of Escherichia coli isocitrate dehydrogenase. Biochemistry 32 9302-9309, 1993. 

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