Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Jaap A. Jongejan"'
Publikováno v:
Recueil des Travaux Chimiques des Pays-Bas. 110:247-254
The enantioselective properties of a large number of enzymes are conveniently characterized by the enantiomeric ratio, E = (kcat/KM)s/(kcat/KM)R. Chen and coworkers [Chen et al., J. Am. Chem. Soc. 104, 7294-9 (1982)] have shown that the value of E ca
Publikováno v:
Recueil des Travaux Chimiques des Pays-Bas. 110:255-262
Three methods for the determination of the enantiomeric ratio, E, of enantioselective, Michaelis-Menten-type enzymes have been investigated with respect to accuracy, using the method of propagation of standard deviation. In addition, estimations of s
Publikováno v:
International Journal of Hydrogen Energy. 31:1432-1438
Molecular hydrogen is activated by two classes of enzymes, Fe-hydrogenases and NiFe-hydrogenases, which have similar sulfur-bridged dinuclear metal active sites with biologically unusual ligands CO and CN - . While detailed structural knowledge on th
Autor:
Chris Oostenbrink, Yu Zhou, Wilfred F. van Gunsteren, Aldo Jongejan, Simon W. de Leeuw, Wilfred R. Hagen, Jaap A. Jongejan
Publikováno v:
Zhou, Y, Oostenbrink, C, Jongejan, A, van Gunsteren, W F, Hagen, W F, de Leeuw, S W & Jongejan, J A 2006, ' Computational study of ground-state chiral induction in small peptides: comparison of the relative stability of selected amino acid dimers and oligomers in homochiral and heterochiral combinations ', Journal of Computational Chemistry, vol. 27, no. 7, pp. 857-867 . https://doi.org/10.1002/jcc.20378
Journal of Computational Chemistry, 27(7), 857-867. John Wiley and Sons Inc.
Journal of Computational Chemistry, 27(7), 857-867. John Wiley and Sons Inc.
The relative stabilities of homochiral and heterochiral forms of selected dipeptides, AA, AS, AC, AV, AF, AD, AK, tripeptides, AAA, AVA, and an acetylpentapeptide, AcGLSFA, have been calculated using thermodynamic integration protocols and the GROMOS
Autor:
Wilfred R. Hagen, Jaap A. Jongejan, Yu Zhou, Wilfred F. van Gunsteren, Simon W. de Leeuw, Chris Oostenbrink
Publikováno v:
Molecular Physics. 103:1961-1969
The relative stability of homochiral (D,D or L,L) and heterochiral (D,L or L,D) dipeptides may have been a decisive factor in the evolutionary propagation of a symmetry-breaking event leading to the present-day predominance of L-amino acids in natura
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647:297-302
Isotopic substitution provides an effective tool to probe the mechanism of enzyme-catalyzed reactions. To our knowledge, kinetic isotope effects on the enantioselectivity of enzymes have not been reported. We investigated the effect of deuterium subs
Publikováno v:
Enzyme and Microbial Technology. 31:656-664
The asymmetric reduction of ethyl 3-oxobutanoate to ethyl ( S )-3-hydroxybutanoate by baker’s yeast ( Saccharomyces cerevisiae ) immobilized in calcium alginate was studied. The reaction was carried out under aerobic conditions with glucose fed as
Autor:
Ifoeng Chin-Joe, Adrie J. J. Straathof, Andreas Liese, Joseph J. Heijnen, Jürgen Haberland, Jaap A. Jongejan
Publikováno v:
Enzyme and Microbial Technology. 31:665-672
The reduction of ethyl 3-oxobutanoate (EOB) to ethyl (S)-3-hydroxybutanoate ((S)-EHB) by cell suspensions of baker’s yeast (Saccharomyces cerevisiae) in a continuously operated reactor with cell retention has been investigated. The continuous reduc
Publikováno v:
Biocatalysis and Biotransformation. 20:337-345
Baker's-yeast-mediated asymmetric ethyl 3-oxobutanoate reduction using a fed-batch feeding strategy for both the 3-oxo ester and the electron donor, was explored as potential production system for enantiopure ethyl ( S )-3-hydroxybutanoate. The dual
Autor:
Jong Keun Kim, Bart Devreese, Ayse Hacisalihoglu, Isabel Vandenberghe, Johannis A. Duine, Katsuyuki Tanizawa, Toshihide Okajima, Osao Adachi, Shun'ichi Kuroda, Hidehiko Iwabuki, Jozef Van Beeumen, Jaap A. Jongejan
Publikováno v:
Journal of Biological Chemistry. 276:42923-42931
Pseudomonas putida contains an amine dehydrogenase that is called a quinohemoprotein as it contains a quinone and two hemes c as redox active groups. Amino acid sequence analysis of the smallest (8.5 kDa), quinone-cofactor-bearing subunit of this het