Zobrazeno 1 - 10
of 13
pro vyhledávání: '"W J, Van Berkel"'
Publikováno v:
Biochemistry. Biokhimiia. 66(8)
Gram-positive bacteria of the genus Rhodococcus catabolize p-hydroxybenzoate (PHB) through the initial formation of 3,4-dihydroxybenzoate. High levels of p-hydroxybenzoate hydroxylase (PHBH) activity are induced in six different Rhodococcus species w
Publikováno v:
European journal of biochemistry. 267(23)
The ascomycetous yeast Candida parapsilosis CBS604 catabolizes 4-hydroxybenzoate through the initial formation of hydroquinone (1, 4-dihydroxybenzene). High levels of hydroquinone hydroxylase activity are induced when the yeast is grown on either 4-h
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 131
Publikováno v:
Journal of molecular biology. 292(1)
p-Hydroxybenzoate hydroxylase (PHBH) is the archetype of the family of NAD(P)H-dependent flavoprotein aromatic hydroxylases. These enzymes share a conserved FAD-binding domain but lack a recognizable fold for binding the pyridine nucleotide. We have
Publikováno v:
The Journal of biological chemistry. 274(37)
A novel nicotinoprotein, catalyzing the dichlorophenolindophenol-dependent oxidation of carveol to carvone, was purified to homogeneity from Rhodococcus erythropolis DCL14. The enzyme is specifically induced after growth on limonene and carveol. Dich
Autor:
V S, Bondar, M G, Boersma, E L, Golovlev, J, Vervoort, W J, Van Berkel, Z I, Finkelstein, I P, Solyanikova, L A, Golovleva, I M, Rietjens
Publikováno v:
Biodegradation. 9(6)
Of all NMR observable isotopes 19F is the one perhaps most convenient for studies on biodegradation of environmental pollutants. The reasons underlying this potential of 19F NMR are discussed and illustrated on the basis of a study on the biodegradat
Publikováno v:
Proteins. 27(4)
Vanillyl-alcohol oxidase catalyses the oxidation of several 4-hydroxybenzyl alcohols by using 8-alpha-(N3-histidyl)-FAD as a covalently bound prosthetic group. Crystals of vanillyl-alcohol oxidase from Penicillium simplicissimum have been grown by us
Publikováno v:
European journal of biochemistry. 237(3)
The side chain of Tyr222 in p-hydroxybenzoate hydroxylase interacts with the carboxy moiety of the substrate. Studies on the Tyr222--Phe mutant, [F222]p-hydroxybenzoate hydroxylase, have shown that disruption of this interaction hampers the hydroxyla
Publikováno v:
Journal of molecular biology. 230(4)
The structure of Pseudomonas fluorescens lipoamide dehydrogenase, a dimeric flavoenzyme with a molecular mass of 106,000 daltons, was solved by the molecular replacement method and refined to an R-factor of 19.4% at 2.8 A resolution. The root-mean-sq
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 21(2)
In vivo and in vitro biotransformation of secondary aromatic amines was investigated using 4-fluoro-N-methylaniline as the model compound. Attention was focused on the role of cytochromes P-450 and the flavin-containing monooxygenase in formation of