Oxalate decarboxylase (OxDC), an enzyme of the bicupin superfamily, catalyzes the decomposition of oxalate into carbon dioxide and formate at an optimal pH of 4.3 in the presence of oxygen. However, about 0.2% of all reactions occur through an oxidase mechanism that consumes oxygen while producing two equivalents of carbon dioxide and one equivalent of hydrogen peroxide. The kinetics of oxidase...

Lysosomal enzyme release from PMN exposed to STZ was examined using PMN from normal and CGD donors. Normal PMN showed an increase of extracellular lysosomal enzyme activity and a marked reduction of totol (extra-plus intra-cellular) enzyme activity after phagocytosis. On the other hand, in PMN from CGD patients, such a reduction of total enzyme activity was not observed and much more enzyme tha...

Choline oxidase from Arthrobacter globiformis is a flavin-dependent enzyme that catalyzes the oxidation of choline to betaine aldehyde through two sequential hydride-transfer steps. The study of this enzyme is of importance to the understanding of glycine betaine biosynthesis found in pathogenic bacterial or economic relevant crop plants as a response to temperature and salt stress in adverse e...

BACKGROUND AND OBJECTIVES The attempts were made to describe the development of a whole cell immobilization of P. pastoris by entrapping the cells in polyacrylamide gel beads. The alcohol oxidase activity of the whole cell Pichia pastoris was evaluated in comparison with yeast biomass production. MATERIALS AND METHODS Methylotrophic yeast P. pastoris was obtained from Collection of Standard M...

Copper amine oxidases are important enzymes, which contribute to the regulation of mono- and polyamine levels. Each monomer contains one Cu(II) ion and 2,4,5-trihydroxyphenylalanine (TPQ) as cofactors. They catalyze the oxidative deamination of primary amines to aldehydes with a ping-pong mechanism consisting of a transamination. The mechanism is followed by the transfer of two electrons to mol...

Although no amine oxidase could be detected in crude extracts, the enzyme has been purified to apparent homogeneity from Hordeum vulgare seedlings using ammonium sulfate precipitation and chromatography on DEAE cellulose, Hydroxylapatite, and Sephadex G200 columns. Gel filtration experiments indicate a molecular weight of about 150,000. The pH optimum of the enzyme was found to be 7.5 in potass...

Lysyl oxidase purified from urea extracts of various connective tissues resolves into multiple catalytically functional species upon chromatography on DEAE-cellulose in 6 M urea. The four enzyme species of bovine aorta retain their original chromatographic behavior on DEAE with time of storage and after purification to homogeneity by gel exclusion chromatography. The peptide maps of each aortic...

In humans and rats, angiotensin I-converting enzyme activity is significantly determined by a gene polymorphism. Homozygous Brown Norway rats have higher plasma angiotensin I-converting enzyme activity and circulating angiotensin II (Ang II) levels than Lewis rats. Because Ang II induces NAD(P)H oxidase activation, we hypothesized here that Brown Norway rats have higher vascular NAD(P)H oxidase...

Aortic tissue from chicks raised 8 to 11 days on diets lacking copper contains diminished levels of the enzyme lysyl oxidase, a copper metalloenzyme. By incubating the deficient aortic tissue in fully oxygenated Waymouth growth medium (MB 751/2) supplemented with 3 to 5 pg/ml of CuSO4, it was possible to restore lysyl oxidase activity to the aorta. Enzyme activation required copper supplements ...

Xanthine oxidase is a highly versatile enzyme which is widely distributed among various species. Though the presence of the enzyme in serum is not yet established, high antibody titre of this enzyme has been reported. Xanthine oxidase is thought to be the principal source of free radical generation via degradation of nucleotides to the end product, uric acid. The aim of this study was to detect...