Putrescine Oxidase, a Diamine Oxidase Requiring Flavin Adenine Dinucleotide
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چکیده
منابع مشابه
African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase.
Protein pB119L of African swine fever virus belongs to the Erv1p/Alrp family of sulfhydryl oxidases and has been described as a late nonstructural protein required for correct virus assembly. To further our knowledge of the function of protein pB119L during the virus life cycle, we have investigated whether this protein possesses sulfhydryl oxidase activity, using a purified recombinant protein...
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The reconstitution reaction of glucose oxidase from FAD and apoenzyme was studied : (1) Unimolecular reaction takes part in the reaction of glucose apooxidase with FAD as a rate limiting step. (2) At the very initial stage of the reaction, intensity of the fluorescence derived from FAD was observed to increase rapidly and to be quenched slowly after reaching the maximum state. (3) When glucose ...
متن کاملD-Amino Acid Oxidase III. STIJDIES OF FLAVIN ADENINE DINUCLEOTIDE BINDING*
A recently described spectrophotometric assay for Damino acid oxidase was used to study the inhibition of the enzyme by a series of adenine and flavin derivatives. AMP, ADP, and ADP-ribose inhibited the enzyme competitively with respect to FAD. No instantaneous inhibition was observed with flavin derivatives. These inhibition studies indicated that the adenosine moiety and the pyrophosphate gro...
متن کاملCharacterisation of the flavin adenine dinucleotide binding region of Myxococcus xanthus protoporphyrinogen oxidase
Protoporphyrinogen oxidase (PPOX), the penultimate enzyme in the haem biosynthetic pathway catalysers the six electron oxidation of protoporphyrinogen-IX to protoporphyrin-IX, in the presence of flavin adenine dinucleotide (FAD) and oxygen. In humans, partial defects in PPOX result in variegate porphyria. In this study, the FAD binding region in Myxococcus xanthus PPOX was analysed by engineeri...
متن کاملPhotoinactivation of porcine D-amino acid oxidase with flavin adenine dinucleotide.
FAD photosensitizes its own oxidation and that of D-amino acid oxidase. First order photoinactivation of the enzyme is paraIieIed by losses of cysteine, histidine, tyrosine, lysine, and, at saturating levels of FAD, tryptophan. Minimal photo-oxidation of methionine has also been found with illuminated enzyme samples. Native and partially photoinactivated enzyme have the same pH activity profile...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1965
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.29.1148