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Quinoproteins

W S McIntire1

  • 1Molecular Biology Division, Department of Veterans Affairs Medical Center, San Francisco, California 94121.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|May 1, 1994
PubMed
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Quinoproteins, enzymes utilizing quinone cofactors, were poorly understood before 1979. This study details three enzyme groups: PQQ-containing alcohol dehydrogenases, copper-containing amine oxidases with topa quinone (TQ), and bacterial amine dehydrogenases using tryptophan tryptophylquinone (TTQ).

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein Science

Background:

  • The term "quinoprotein" encompasses three enzyme classes, historically lacking defined cofactor structures before 1979.
  • Quinonoid oxidation-reduction cofactors are essential for these enzymes' function.
  • Early research identified pyrroloquinoline quinone (PQQ) as a prosthetic group in certain enzymes.

Purpose of the Study:

  • To elucidate the diverse structures and origins of quinone cofactors in different quinoprotein classes.
  • To detail the specific quinone molecules involved in various enzymatic activities.
  • To highlight recent discoveries regarding cofactor biosynthesis in amine oxidases and dehydrogenases.

Main Methods:

  • Literature review and analysis of established biochemical and structural studies on quinoproteins.

Related Experiment Videos

  • Identification and classification of enzymes based on their quinone cofactor type (PQQ, TQ, TTQ).
  • Comparative analysis of cofactor biosynthesis pathways across different enzyme families.

    • Main Results:

    • Three distinct quinoprotein groups were identified: PQQ-containing enzymes (primarily alcohol dehydrogenases), copper-containing amine oxidases utilizing topa quinone (TQ), and bacterial amine dehydrogenases requiring tryptophan tryptophylquinone (TTQ).
    • PQQ was the first identified quinone cofactor.
    • TQ is derived from a tyrosyl residue in amine oxidases, while TTQ originates from two tryptophyl residues in bacterial amine dehydrogenases.

    Conclusions:

    • Quinoproteins represent a diverse group of enzymes with distinct quinone cofactors crucial for their catalytic activity.
    • The biosynthesis of TQ and TTQ involves post-translational modification of specific amino acid residues.
    • Further research is needed to fully understand the unknown processes involved in TQ and TTQ formation.