European journal of biochemistry, 225(3), 959-965 (1994-11-01)
Interactions of two distinct quinoprotein amine oxidases from Aspergillus niger, AO-I and AO-II, with active-site covalent modifiers have been investigated. Both enzymes are inhibited similarly by phenylhydrazine or p-nitrophenylhydrazine, forming an orange Schiff base with a carbonyl group of topaquinone
Pig kidney diamine oxidase was purified to homogeneity. The reaction product of the cofactor with p-nitrophenylhydrazine (pNPH) was liberated with pronase treatment and purified. 1H NMR, uv/vis, and electrospray tandem mass spectroscopy revealed it to be a dipeptide with the
Analytical and mechanistic aspects of the electrochemical oxidation of keto steroids derivatized with phenylhydrazine, (4-nitrophenyl)hydrazine, and (2,4-dinitrophenyl)hydrazine.
Biochimica et biophysica acta, 1647(1-2), 272-277 (2003-04-11)
Quinohemoprotein amine dehydrogenase (QH-AmDH) catalyzes the oxidative deamination of aliphatic and aromatic amines. The enzyme from Pseudomonas putida has an alpha beta gamma heterotrimeric structure with two heme c groups in the largest alpha subunit, and a novel quinone cofactor
Biochemistry and molecular biology international, 36(6), 1207-1216 (1995-08-01)
Structural properties of dimeric (2 x 75 kDa) copper-containing amine oxidase (EC 1.4.3.6) from Aspergillus niger were studied. The enzyme treated with SDS was dissociated into subunits which showed different mobility on polyacrylamide gel without SDS. The separated subunits had
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