Status of the cofactor identity in copper oxidative enzymes.
Much conflicting data have appeared in the literature regarding the nature of the active site structures responsible for catalysis in three classes of copper enzymes: the copper amine oxidases, dopamine beta-monooxygenase and galactose oxidase. Although pyrroloquinoline quinone has been proposed to be the active site cofactor in each instance, new findings indicate this is not the case. Instead, recently available data indicate a spectrum of strategies for substrate activation, which range from direct metal catalysis (dopamine beta-monooxygenase) to the involvement of protein-derived radicals (galactose oxidase) and protein-derived quinones (copper amine oxidases).
Klinman
J P
JP
Department of Chemistry, University of California, Berkeley 94720.
Dooley
D M
DM
Duine
J A
JA
Knowles
P F
PF
Mondovi
B
B
Villafranca
J J
JJ
D006631:Amine Oxidase (Copper-Containing); D001665:Binding Sites; D003067:Coenzymes / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000378:metabolism; D004299:Dopamine beta-Hydroxylase / Q000378:metabolism*; D005692:Galactose Oxidase / Q000378:metabolism*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D045542:PQQ Cofactor; D015363:Quinolones / Q000378:metabolism
D003067:Coenzymes; D015363:Quinolones; D004295:Dihydroxyphenylalanine; C067626:6-hydroxydopa quinone; D045542:PQQ Cofactor; D003300:Copper; D005692:Galactose Oxidase; D004299:Dopamine beta-Hydroxylase; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors