Kinetic characterization of tyramine oxidase of Arthrobacter species.
Amine oxidases (EC 1.4.3) represent a rather nebulous group of proteins with relative narrow substrate and inhibitor specificities. Several different enzymes fall into these amine oxidase classes and the classification of some of them still remains ambiguous. Kinetic and physico-chemical properties of tyramine oxidase of Arthrobacter sp. were investigated to decide if this enzyme belongs to the flavin containing tyramine oxidase class (EC 1.4.3.9) or if it is more related to another amine oxidase class. On the basis of its spectral characteristics, molecular weight and inhibition profile, the enzyme was identified as a semicarbazide sensitive copper-containing amine oxidase.
Facultés Notre-Dame de la Paix, Namur, Belgium.
J
J
Wouters
P
P
Perpète
P
P
Hayen
N
N
Anceau
F
F
Durant
D001173:Arthrobacter / Q000201:enzymology*; D003300:Copper / Q000032:analysis; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D008995:Monoamine Oxidase; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012642:Selegiline / Q000494:pharmacology; D012663:Semicarbazides / Q000494:pharmacology; D013816:Thermodynamics
D012663:Semicarbazides; D012642:Selegiline; C010059:carbamylhydrazine; D003300:Copper; D004492:Edetic Acid; D008995:Monoamine Oxidase; D000587:Oxidoreductases Acting on CH-NH Group Donors