Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. Is a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also catalyzes nitric oxide (NO) production; under anaerobic conditions, reduces nitrite to NO with NADH or aldehyde as electron donor, but under aerobic conditions, NADH is the preferred substrate. These reactions may be catalyzed by several isozymes. May play a role in adipogenesis.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION;TISSUE SPECIFICITY;BLOCKAGE OF N-TERMINUS;HOMODIMER;VARIANTS 119-ALA-ARG-120; THR-649; LEU-1276 AND ARG-1315
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE;CATALYTIC ACTIVITY;ENZYME REGULATION;KINETIC PARAMETERS
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN SUPEROXIDE PRODUCTION;TISSUE SPECIFICITY;SUBCELLULAR LOCATION;HOMODIMER;COFACTOR
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN NITRIC OXIDE PRODUCTION;BIOPHYSICOCHEMICAL PROPERTIES;ENZYME REGULATION