Evidence is presented for the existence in bacterium N.C.I.B. 8250 of two inducible NAD(+)-linked benzaldehyde dehydrogenases. They may be distinguished in crude extracts by their different thermal stabilities at high pH values, benzaldehyde dehydrogenase I being much more heat-stable than benzaldehyde dehydrogenase II. Only benzaldehyde dehydrogenase I is activated by K(+) and certain other un...

A quick, reliable, purification procedure was developed for purifying both benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from a single batch of Acinetobacter calcoaceticus N.C.I.B. 8250. The procedure involved disruption of the bacteria in the French pressure cell and preparation of a high-speed supernatant, followed by chromatography on DEAE-Sephacel, affinity chromatography o...

Two aldehyde dehydrogenases involved in the degradation of toluene and xylenes, namely, benzaldehyde dehydrogenase and 2-hydroxymuconic semialdehyde dehydrogenase, are encoded by the xylC and xylG genes, respectively, on TOL plasmid pWW0 of Pseudomonas putida. The nucleotide sequence of xylC was determined in this study. A protein exhibiting benzaldehyde dehydrogenase activity had been purified...

since measurements of O2 uptake with intact bacteriaor extracts indicated approximately the same ratio of activities. Further, bacteria growing on D(-)-mandelate did not accumulate benzaldehyde, which shows that D(-)-mandelate dehydrogenase, rather than benzaldehyde dehydrogenase I (Cook et al., 1975), was now rate-limiting. D(-)-Mandelate dehydrogenase resembles L(+)-mandelate dehydrogenase in...

The pathway of mandelate metabolism in Pseudomonas aeruginosa is composed of the following steps: l(+)-mandelate --> benzoylformate --> benzaldehyde --> benzoate. These three steps are unique to mandelate oxidation; the benzoate formed is further metabolized via the beta-ketoadipate pathway. The first enzyme, l(+)-mandelate dehydrogenase, is induced by its substrate. The second and third enzyme...

Rhodotorula graminis utilized DL-mandelate, L(+)-mandelate, and D(-)-mandelate as sole sources of carbon and energy. Growth on these aromatic substrates resulted in the induction of an NAD-dependent D(-)-mandelate dehydrogenase and a dye-linked L(+)-mandelate dehydrogenase, each catalyzing the stereospecific conversion of its respective enantiomer of mandelate to benzoylformate. Benzoylformate ...

Sequential cycloisomerizations of diynyl o-benzaldehyde substrates to access novel polycyclic cyclopropanes are reported. The reaction sequence involves initial Cu(I)-mediated cycloisomerization/nucleophilic addition to an isochromene followed by diastereoselective Pt(II)-catalyzed enyne cycloisomerization.

The mol-ecule of the title compound, [Sb(C(6)H(5))(3)(C(7)H(6)NO(2))(2)], is located on a twofold axis defined by the metal center and two C atoms of a coordinated phenyl group. The Sb center has a slightly distorted trigonal-bipyramidal geometry, with the axial positions occupied by the O atoms of symmetry-related 2-hydroxy-benzaldehyde oximate ligands. An intra-molecular O-H⋯N inter-action is...

The conversion of benzaldehyde to optically active L-phenylacetyl carbinol by yeast fermentation is a key step in the manufacture of L-ephedrine. ’ Typical fermentation raw materials are molasses, which provides a source of hexoses for glycolysis, and benzaldehyde. L-phenylacetyl carbinol formation is catalyzed by the pyruvate decarboxylase complex.’ In the carboligase reaction, pyruvate is dec...

Benzyl Alcohol Dehydrogenase (BADH) is an important enzyme for hydrocarbon degradation, which can oxidize benzyl alcohols to aldehydes, while being capable of catalyzing a reversible reaction by reducing benzaldehyde. BADH is a member of medium chain alcohol dehydrogenases, in which zinc and NAD are essential for enzyme activity. This paper describes the expression, purification, and characteri...