Studies on sulfhydryl groups of Aspergillus niger amine oxidase.

Amino acid analysis of the amine oxidase of Aspergillus niger (monoamine:O2 oxidoreductase (deaminating), EC 1.4.3.4) showed a composition similar to that of bovine plasma enzyme. One molecule of enzyme contained 25 Cys residues. It was shown that 9 to 11 residues of Cys were titrated to be SH groups. The amine oxidase reaction was markedly inhibited by metal ions (Cu2+, Hg2+, Ag+). The enzyme was inactivated with SH reagents (phenyl mercuric acetate, Cl-HgBzO-) and the extent of this inactivation was dependent on the time of incubation with SH reagents. Also, the Cl-HgBzO- -inactivated enzyme was reactivated with cysteine and this reactivation was biphasic with the time of incubation. The Cl-HgBzO--inactivated amine oxidase was compared with the native enzyme in their reactivity with phenylhydrazine and their spectral properties. The results showed that the Cl-HgBzO--inactivated enzyme had lower reactivity with phenylhydrazine than the native enzyme and had higher absorbance values than the native enzyme around 400 nm wavelengths.