Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Lamoraal A.Æ. Sluyterman"'
Publikováno v:
Journal of Molecular Structure: THEOCHEM, 364(1), 33-43. Elsevier
Semiempirical (AM1 and PM3) calculations on active site models have been performed to study the mechanism of horse liver alcohol dehydrogenase (HLADH). The active site model used in the calculations consists of a Zn(II) ion coordinated by derivatives
Publikováno v:
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1295(2), 125-138. Elsevier
Poly(ethylene glycol)-bound nicotinamide adenine dinucleotide (PEG-NAD+) has been successfully employed in the continuous production of L-amino acids from the corresponding alpha-keto acids by stereospecific reductive amination. Like many other dehyd
Publikováno v:
Journal of Molecular Structure: THEOCHEM, 304, 53-59. Elsevier
The NAD+/NADH coenzyme is involved in many enzyme-catalysed oxidation-reduction reactions. In order to obtain better insight in the catalytic mechanism of NAD+/NADH dependent dehydrogenases, conformational studies of 1,3-substituted pyridines and ben
Publikováno v:
Annals of the New York Academy of Sciences, 613, 494-500. Wiley-Blackwell
So far, the interactions of nicotinamide adenine dinucleotide (NAD+) derivatives with dehydrogenases are not very well understood. This hampers the introduction of NAD+ analogues with improved characteristics concerning industrial application. We hav
Publikováno v:
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1039(2), 227-233. Elsevier
In the present study we show that the enzymatic activity of the coenzyme nicotinamide adenine dinucleotide (NAD + ) and its analogues (C(O)NH 2 replaced by C(S)NH 2 , C(O)CH 3 , C(O)H and CN) with horse liver alcohol dehydrogenase (LADH) (alcohol:NAD
Autor:
Lamoraal A.Æ. Sluyterman, C. Kooistra
Publikováno v:
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 997(1-2), 115-120. Elsevier
Guanidinated mercuri-papain (Gu-papain) was reacted with N -ethylbenziosoxazolium tetrafluoroborate at pH 4.2, 0°C, to yield highly reactive N -ethylsalicylamide esters. On varying the amount of reagent applied 2.5–10 car☐yl groups were modified
Autor:
Peter M. T. de Kok, HM Henk Buck, Nicoline A. Beijer, Emmo M. Meijer, Lamoraal A.Æ. Sluyterman
Publikováno v:
European Journal of Biochemistry, 175(3), 581-585. Wiley-Blackwell
The geometry of seven NAD+ analogues bound to horse liver alcohol dehydrogenase (LADH) modified only in their nicotinamide group, have been studied using AMBER molecular mechanics energy-minimization procedures. Starting geometries were taken from X-