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The FASEB Journal, Vol 8, 513-521, Copyright © 1994 by The Federation of American Societies for Experimental Biology
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WS McIntire
Molecular Biology Division, Department of Veterans Affairs Medical Center, San Francisco, California 94121.
As used today, the word quinoprotein defines three distinct groups of enzymes. Before 1979, the structures of the essential, quinonoid oxidation-reduction cofactors were a mystery for all these enzymes. The first proteins proven to harbor this type prosthetic group are those with noncovalently bound pyrroloquinoline quinone (PQQ). PQQ-containing enzymes can be described as alcohol dehydrogenases, with the exception of a single protein, which is an amine dehydrogenase. More recently, it was discovered that copper-containing amine oxidases contain 6- hydroxydopa quinone, also known as topa quinone (TQ), whereas certain bacterial amine dehydrogenases require 2',4-bitryptophan-6,7-dione (tryptophan tryptophylquinone, TTQ) for activity. These latter two quinones are formed, by unknown processes, from a specific tyrosyl residue for the amine oxidases, and from two widely separate tryptophyl residues in the polypeptide of the amine dehydrogenases.
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