Proteus rettgeri has been found to contain two separable 1-amino acid oxidases. Both enzymes are particulate in nature, neither being ribosomal bound. One of these enzymes appears to have broad specificity, being active toward monoaminomonocarboxylic, imino, aromatic, sulfur-containing, and beta-hydroxyamino acids. The other enzyme has more limited specificity, catalyzing the oxidative deaminat...

NAD+-dependent phenylalanine dehydrogenases were purified 1,500- and 1,600-fold, and crystallized from Sporosarcina ureae SCRC-R04 and Bacillus sphaericus SCRC-R79a, respectively. The purified enzymes were homogeneous as judged by disc gel electrophoresis. The enzyme from S. ureae has a molecular weight of 305,000, while that of B. sphaericus has a molecular weight of 340,000. Each is probably ...

Escherichia coli RidA is a member of a structurally conserved, yet functionally highly diverse protein family involved in translation inhibition (human), Hsp90-like chaperone activity (fruit fly) and enamine/imine deamination (Salmonella enterica). Here, we show that E. coli RidA modified with HOCl acts as a highly effective chaperone. Although activation of RidA is reversed by treatment with D...

Abstract: Flavoprotein monoamine oxidase is located on the outer membrane of mitochondria. It catalyzes oxidative deamination of monoamine neurotransmitters such as serotonin, norepinephrine and dopamine and hence is a target enzyme for antidepressant drugs. MAO (mono amine oxidase) has two isoforms, namely MAO-A and MAO-B. MAO-A isoform has higher affinity for serotonin and norepinephrine, whi...

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...

This study reports the kinetics and mechanism of Fe(III)-catalyzed oxidative decarboxylation and deamination of a series of acyclic (α-aminoisobutyric acid, α-(methylamino)isobutyric acid, alanine, norvaline, and 2-aminobutyric acid) and cyclic (1-aminocyclopropane-1-carboxylic acid, 1-amino-1-cyclobutanecarboxylic acid, 1-aminocyclopentanecarboxylic acid, and 1-aminocyclohexanecarboxylicacid) ...

Suspensions of purified elementary bodies of vaccinia exhibit fluorescence in the presence of ultraviolet light. This fluorescent constituent can be separated by chromatographic methods provided the virus is first denatured by acid and heat. By means of the specific protein of d-amino acid oxidase it has been possible to identify the flavin constituent as flavin-adenine-dinucleotide and show th...

D-amino acid oxidase (DAAO) and catalase (CAT) have been genetically modified by fusing them to an elastin-like polypeptide (ELP). ELP-DAAO and ELP-CAT have been separately immobilized on multi-walled carbon nanotubes (MWNTs). It has been found that the secondary structures of the enzymes have been preserved. ELP-DAAO catalyzed the oxidative deamination of D-alanine, and H2O2 was evolved contin...

Deoxyinosine (dI) occurs in DNA either by oxidative deamination of a previously incorporated deoxyadenosine residue or by misincorporation of deoxyinosine triphosphate (dITP) from the nucleotide pool during replication. To exclude dITP from the pool, mammals possess specific hydrolysing enzymes, such as inosine triphosphatase (ITPA). Previous studies have shown that deficiency in ITPA results i...

Valine dehydrogenase was purified to homogeneity from the crude extracts of Streptomyces aureofaciens. The molecular weight of the native enzyme was 116,000 by equilibrium ultracentrifugation and 118,000 by size exclusion high-performance liquid chromatography. The enzyme was composed of four subunits with molecular weights of 29,000. The isoelectric point was 5.1. The enzyme required NAD+ as a...