Evidence for pyrroloquinolinequinone as the carbonyl cofactor in lysyl oxidase by absorption and resonance Raman spectroscopy.
The present study investigated the possibility that pyrroloquinolinequinone (PQQ), an aromatic carbonyl recently indicated to be the carbonyl cofactor in bovine plasma amine oxidase, may also be present at the active site of lysyl oxidase. The absorption and resonance Raman spectra of the phenylhydrazones of bovine plasma amine oxidase, of peptides derived from the active site of bovine aorta lysyl oxidase, and of PQQ were very similar, indicating that the carbonyl cofactor of lysyl oxidase is PQQ or a compound which closely resembles PQQ.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000818:Animals; D001011:Aorta / Q000201:enzymology; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D009131:Muscle, Smooth, Vascular / Q000201:enzymology; D045542:PQQ Cofactor; D010659:Phenylhydrazines / Q000378:metabolism; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D011804:Quinolines / Q000378:metabolism*; D013053:Spectrophotometry / Q000379:methods; D013059:Spectrum Analysis, Raman / Q000379:methods
D010659:Phenylhydrazines; D011804:Quinolines; C030299:phenylhydrazine; D045542:PQQ Cofactor; D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase