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Results: 1-18 |
Results: 18
Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties
Authors: Oubrie, A Huizinga, EG Rozeboom, HJ Kalk, KH de Jong, GAH Duine, JA Dijkstra, BW
Citation: A. Oubrie et al., Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties, ACT CRYST D, 57, 2001, pp. 1732-1734
Ca2+ stabilizes the semiquinone radical of pyrroloquinoline quinone
Authors: Sato, A Takagi, K Kano, K Kato, N Duine, JA Ikeda, T
Citation: A. Sato et al., Ca2+ stabilizes the semiquinone radical of pyrroloquinoline quinone, BIOCHEM J, 357, 2001, pp. 893-898
Constitutive and inducible hydroxylase activities involved in the degradation of naphthalene by Cunninghamella elegans
Authors: Faber, BW Schonewille, ABJA van Gorcom, RFM Duine, JA
Citation: Bw. Faber et al., Constitutive and inducible hydroxylase activities involved in the degradation of naphthalene by Cunninghamella elegans, APPL MICR B, 55(4), 2001, pp. 486-491
Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation stepin the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus
Authors: Wandel, U Machado, SS Jongejan, JA Duine, JA
Citation: U. Wandel et al., Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation stepin the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus, ENZYME MICR, 28(2-3), 2001, pp. 233-239
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond
Authors: Vandenberghe, I Kim, JK Devreese, B Hacisalihoglu, A Iwabuki, H Okajima, T Kuroda, S Adachi, O Jongejan, JA Duine, JA Tanizawa, K Van Beeumen, J
Citation: I. Vandenberghe et al., The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond, J BIOL CHEM, 276(46), 2001, pp. 42923-42931
The first step in polyethylene glycol degradation by sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide
Authors: Sugimoto, M Tanabe, M Hataya, M Enokibara, S Duine, JA Kawai, F
Citation: M. Sugimoto et al., The first step in polyethylene glycol degradation by sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide, J BACT, 183(22), 2001, pp. 6694-6698
Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger
Authors: Faber, BW van Gorcom, RFM Duine, JA
Citation: Bw. Faber et al., Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger, ARCH BIOCH, 394(2), 2001, pp. 245-254
Enantioselective oxidation of amphetamine by copper-containing quinoprotein amine oxidases from Escherichia coli and Klebsiella oxytoca
Authors: Hacisalihoglu, A Jongejan, A Jongejan, JA Duine, JA
Citation: A. Hacisalihoglu et al., Enantioselective oxidation of amphetamine by copper-containing quinoprotein amine oxidases from Escherichia coli and Klebsiella oxytoca, J MOL CAT B, 11(2-3), 2000, pp. 81-88
Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols andaldehydes
Authors: Schenkels, P Duine, JA
Citation: P. Schenkels et Ja. Duine, Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols andaldehydes, MICROBIO-UK, 146, 2000, pp. 775-785
Ca2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH(2), in the oxidation of beta-D-glucose by soluble, quinoprotein glucose dehydrogenase
Authors: Dewanti, AR Duine, JA
Citation: Ar. Dewanti et Ja. Duine, Ca2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH(2), in the oxidation of beta-D-glucose by soluble, quinoprotein glucose dehydrogenase, BIOCHEM, 39(31), 2000, pp. 9384-9392
The PQQ story
Authors: Duine, JA
Citation: Ja. Duine, The PQQ story, J BIOSCI BI, 88(3), 1999, pp. 231-236
Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols
Authors: Machado, SS Jongejan, A Geerlof, A Jongejan, JA Duine, JA
Citation: Ss. Machado et al., Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols, BIOCATAL B, 17(3), 1999, pp. 179-207
The temperature dependence of enzymatic kinetic resolutions reveals the relative contribution of enthalpy and entropy to enzymatic enantioselectivity
Authors: Overbeeke, PLA Ottosson, J Hult, K Jongejan, JA Duine, JA
Citation: Pla. Overbeeke et al., The temperature dependence of enzymatic kinetic resolutions reveals the relative contribution of enthalpy and entropy to enzymatic enantioselectivity, BIOCATAL B, 17(1), 1999, pp. 61-79
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
Authors: Machado, SS Wandel, U Jongejan, JA Straathof, AJJ Duine, JA
Citation: Ss. Machado et al., 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, BIOS BIOT B, 63(1), 1999, pp. 10-20
Structure and mechanism of soluble quinoprotein glucose dehydrogenase
Authors: Oubrie, A Rozeboom, HJ Kalk, KH Olsthoorn, AJJ Duine, JA Dijkstra, BW
Citation: A. Oubrie et al., Structure and mechanism of soluble quinoprotein glucose dehydrogenase, EMBO J, 18(19), 1999, pp. 5187-5194
The 1.7 angstrom crystal structure of the Apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novelinternal conserved sequence repeat (vol 289, pg 319, 1999)
Authors: Oubrie, A Rozeboom, HJ Kalk, KH Duine, JA Dijkstra, BW
Citation: A. Oubrie et al., The 1.7 angstrom crystal structure of the Apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novelinternal conserved sequence repeat (vol 289, pg 319, 1999), J MOL BIOL, 292(1), 1999, pp. 191-191
The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novelinternal conserved sequence repeat
Authors: Oubrie, A Rozeboom, HJ Kalk, KH Duine, JA Dijkstra, BW
Citation: A. Oubrie et al., The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novelinternal conserved sequence repeat, J MOL BIOL, 289(2), 1999, pp. 319-333
Simple conformation space search protocols for the evaluation of enantioselectivity of lipases
Authors: Orrenius, C van Heusden, C van Ruiten, J Overbeeke, PLA Kierkels, H Duine, JA Jongejan, JA
Citation: C. Orrenius et al., Simple conformation space search protocols for the evaluation of enantioselectivity of lipases, PROTEIN ENG, 11(12), 1998, pp. 1147-1153
Risultati: 1-18 |