title: The phylogeny and chemical diversity of quinone-tanned glues and varnishes.
abstract: 1. 3,4-Dihydroxyphenyl-L-alanine (DOPA)-containing proteins are widely distributed throughout the animal kingdom and appear to serve chiefly as waterproof adhesives and varnishes. 2. The unique chemical and physical stability of these adhesives and varnishes is imparted by quinone-tanning, an oxidative process that leads to the polymerization of DOPA-containing and other proteins. 3. Recent advances in the biochemistry of DOPA-containing proteins suggest that most consist of tandemly repeated sequence motifs. Each motif contains DOPA, a basic amino acid (usually lysine), and abundant glycine or proline. 4. The DOPA residues undergo catechol oxidase-catalyzed conversion to o-quinones at the onset of quinone-tanning. 5. The complexity of quinone chemistry is discussed with regard to quinone-tanning.
authors.affiliation: Marine Biology/Biochemistry Program, College of Marine Studies, University of Delaware, Lewes 19958.
authors.forename: J H
authors.initials: JH
authors.lastname: Waite
mesh_terms: D000269:Adhesives / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D016384:Consensus Sequence; D004295:Dihydroxyphenylalanine / Q000737:chemistry*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry*; D011809:Quinones / Q000737:chemistry*
chemical_list: D000269:Adhesives; D011506:Proteins; D011809:Quinones; D004295:Dihydroxyphenylalanine