Search Results - "JONGEJAN, J. A"

The enantiomeric ratio: origin, determination and prediction by Straathof, A.J.J., Jongejan, J.A.

“…The enantiomeric ratio E =(kcatR/KmR)/(kcatS/KmS) offers a concise representation of the enantioselective properties of an enzyme in reactions that involve…”
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Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states by Overbeeke, P. L. Antoine, Jongejan, J. A., Heijnen, J. J.

“…The enantioselectivity of lipase‐catalyzed kinetic resolutions has been measured at various temperatures in binary mixtures of solvents. Varying the solvent…”
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Competitive lipase-catalyzed ester hydrolysis and ammoniolysis in organic solvents; equilibrium model of a solid-liquid-vapor system by Litjens, M. J. J., Sha, M., Straathof, A. J. J., Jongejan, J. A., Heijnen, J. J.

“…Enzymatic ester hydrolysis and ammoniolysis were performed as competitive reactions in methyl isobutyl ketone without a separate aqueous phase. The reaction…”
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Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation by Jongejan, A., Jongejan, J. A., Hagen, W. R.

“…Oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone (PQQ) cofactor of quinoprotein alcohol dehydrogenases has been studied using…”
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On the relationship between affinity for molecular hydrogen and the physiological directionality of hydrogenases by van Haaster, D J, Hagedoorn, P-L, Jongejan, J A, Hagen, W R

“…The physiological significance of the generic reaction H(2)<-->2[H] is not always clear because hydrogenases may function in the breakdown of molecular…”
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Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation step in the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus by Wandel, U, Machado, S.Salgueiro, Jongejan, J.A, Duine, J.A

“…It is already known that kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) takes place when Acetobacter pasteurianus oxidizes the compound to…”
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Understanding the influence of temperature change and cosolvent addition on conversion rate of enzymatic suspension reactions based on regime analysis by Wolff, A., Zhu, L., Wong, Y. W., Straathof, A. J. J., Jongejan, J. A., Heijnen, J. J.

“…It is a commonly held belief that enzymatic conversions of substrate in aqueous suspensions can be speeded up by raising the temperature or adding organic…”
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Quinoproteins, Enzymes with Pyrrolo-Quinoline Quinone as Cofactor by Duine, J A, Jongejan, J A

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Hydrolytic activity in baker's yeast limits the yield of asymmetric 3-oxo ester reduction by Chin-Joe, Ifoeng, Nelisse, Pieter M., Straathof, Adrie J. J., Jongejan, Jaap A., Pronk, Jack T., Heijnen, Joseph J.

“…Microbial reductions of ketones hold great potential for the production of enantiopure alcohols, as long as highly selective redox enzymes are not interfered…”
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Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution by Vellieux, F.M., Huitema, F., Groendijk, H., Kalk, K.H., Jzn, J.F., Jongejan, J.A., Duine, J.A., Petratos, K., Drenth, J., Hol, W.G.

“…The three‐dimensional structure of quinoprotein methylamine dehydrogenase from Thiobacillus versutus has been determined at 2.25 A resolution by a combination…”
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Influence of lid conformation on lipase enantioselectivity by Overbeeke, P.L.A, Govardhan, C, Khalaf, N, Jongejan, J.A, Heijnen, J.J

“…The enantioselectivity of porcine pancreatic lipase (PPL) in the hydrolysis reaction of racemic glycidyl butyrate has been observed to increase substantially…”
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Simple dissolution-reaction model for enzymatic conversion of suspension of solid substrate by Wolff, A., Zhu, L., Kielland, V., Straathof, A. J. J., Jongejan, J. A., Heijnen, J. J.

“…Although reactions in substrate suspension are employed in industry for several bioconversion processes, there appears to be no quantitative model available in…”
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Bovine serum amine oxidase: a mammalian enzyme having covalently bound PQQ as prosthetic group by Lobenstein-Verbeek, C.L., Jongejan, J.A., Frank, J., Duine, J.A.

“…In addition to the metal ion, copper-containing amine oxidases possess an organic prosthetic group, the nature of which has long been controversial. We show…”
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Homology model of the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni by Jongejan, A, Jongejan, J A, Duine, J A

“…A molecular model of QH-ADH, the quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni, has been built by homology modelling. Sequence similarity…”
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Simple conformation space search protocols for the evaluation of enantioselectivity of lipases by Orrenius, C, van Heusden, C, van Ruiten, J, Overbeeke, P L, Kierkels, H, Duine, J A, Jongejan, J A

“…Two computational protocols have been evaluated regarding their ability to reproduce the enthalpic part of lipase enantioselectivity by forcefield potential…”
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Pyrroloquinoline quinone as cofactor in galactose oxidase (EC 1.1.3.9) by van der Meer, R A, Jongejan, J A, Duine, J A

“…Galactose oxidase from Dactylium dendroides was shown to contain one molecule of covalently bound pyrroloquinoline quinone (PQQ/enzyme molecule. From the…”
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Isolation, preparation, and assay of pyrroloquinoline quinone by van der Meer, R A, Groen, B W, van Kleef, M A, Frank, J, Jongejan, J A, Duine, J A

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Characterization of the enantioselective properties of the quinohemoprotein alcohol dehydrogenase of Acetobacter pasteurianus LMG 1635, 1: Different enantiomeric ratios of whole cells and purified enzyme in the kinetic resolution of racemic glycidol by Machado, S.S. (Delft Univ. of Technology (Netherlands)), Wandel, U, Jongejan, J.A, Straathof, A.J.J, Duine, J.A

“…Resting cells of Acetobacter pasteurianus, LMG 1635 (ATCC 12874) show appreciable enantioselectivity (E=16-18) in the oxidative kinetic resolution of racemic…”
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Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor by Huizinga, Eric G, Van Zanten, Ben A. M, Duine, Johannis A, Jongejan, Jaap A, Huitema, Fienke, Wilson, Keith S, Hol, Wim G. J

“…To identify the reactive part of the orthoquinone function of the tryptophan-derived cofactor found in methylamine dehydrogenase (MADH), we have determined the…”
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Electron transfer between a quinohemoprotein alcohol dehydrogenase and an electrode via a redox polymer network by Stigter, E.C.A., de Jong, G.A.H., Jongejan, J.A., Duine, J.A., van der Lugt, J.P., Somers, W.A.C.

“…A quinohemoprotein alcohol dehydrogenase (QH-EDH) from Comamonas testosteroni was immobilized on an electrode in a redox polymer network consisting of a…”
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