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An aldehyde oxidase exhibiting high activity on glyoxal was purified to an electrophoretically homogenous state from Pseudomonas sp. AIU 362, which was isolated from a soil sample using a methoxyethanol medium. The enzyme oxidized not only glyoxal but also short-chain aliphatic aldehydes and aromatic aldehydes. Thus, this enzyme was classified into the(More)
An oxidase catalyzing the conversion of glycolaldehyde to glyoxal was purified to the homogeneous state from Paenibacillus sp. AIU 311, and its properties were revealed. This enzyme was specific to glycolaldehyde and glyceraldehyde, and the reaction rates to other alcohols and aldehydes were less than 6% of that of glycolaldehyde. The Km values for(More)
An L-amino acid oxidase was found from a newly isolated strain, Pseudomonas sp. AIU 813. This enzyme was remarkably induced by incubation with L-lysine as a nitrogen source, and efficiently purified using an affinity chromatography with L-lysine as ligand. The enzyme oxidized L-lysine, L-ornithine and L-arginine, but not other L-amino acids and d-amino(More)
A simple enzymatic method for production of a wide variety of D-amino acids was developed by kinetic resolution of DL-amino acids using L-amino acid oxidase (L-AAO) with broad substrate specificity from Rhodococcus sp. AIU Z-35-1. The optimum pH of the L-AAO reaction was classified into three groups depending on the L-amino acids as substrate, and their(More)
We have cloned a gene encoding an aldehyde oxidase (ALOD) oxidized glyoxal but not glyoxylic acid from Pseudomonas sp. AIU 362. The ALOD gene contained an open reading frame consisting of 888 nucleotides corresponding to 295 amino acid residues. The deduced amino acid sequence exhibited a high similarity to those of 3-hydroxyisobutyrate dehydrogenases(More)
An oxidase catalyzing conversion of N(alpha)-benzyloxycarbonyl-L-lysine (N(alpha)-Z-L-lysine) to N(alpha)-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde (N(alpha)-Z-L-AASA) was purified from Rhodococcus sp. AIU Z-35-1, and its properties were revealed. This enzyme catalyzed an oxidative deamination of the epsilon-amino group of N(alpha)-acyl-L-lysine(More)
An L-specific amino acid oxidase (L-AAO) suitable for assay of N-acyl-L-amino acid amidohydrolase (L-aminoacylase) activity was purified from Rhodococcus sp. AIU LAB-3. The enzyme exhibited broad substrate specificity and catalyzed an oxidative deamination of the a-amino group of L-amino acids. The optimal enzyme activities for L-amino acids tested were(More)
The factors for selective production of N(alpha)-benzyloxycarbonyl-L-aminoadipate-delta-semialdehyde (N(alpha)-Z-L-AASA) and N(alpha)-benzyloxycarbonyl-L-aminoadipic acid (N(alpha)-Z-L-AAA) from N(alpha)-benzyloxycarbonyl-L-lysine (N(alpha)-Z-L-lysine) by Rhodococcus sp. AIU Z-35-1 were analyzed. The cultivation time was important for selective production(More)
We have cloned a gene encoding an alcohol oxidase (AOD) specific to aldehyde alcohols from Paenibacillus sp. AIU 311. The AOD gene contains an open reading frame consisting of 618 nucleotides corresponding to 205 amino acid residues. The deduced amino acid sequence exhibits a high similarity to that of manganese superoxide dismutases (SODs). We expressed(More)
Cholesterol oxidase (CHO) with high stability in detergents was found from an isolated strain, Y-134, belonging to the gamma-subclass of Proteobacteria. CHO production reached its maximum by incubation at 30 degrees C for 12 d. It was purified from cell-free extract prepared by mixing the cells with 0.4% Triton X-100. The absorption spectrum of the purified(More)