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Comp Biochem Physiol B Biochem Mol Biol. 2012 Sep;163(1):1-25. doi: 10.1016/j.cbpb.2012.05.005. Epub 2012 May 9.

Structure, biosynthesis and possible function of tunichromes and related compounds.

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  • 1Department of Biology, University of Massachusetts Boston, Boston, MA 02125, USA. manickam.sugumaran@umb.edu

Abstract

Several species of ascidians (phylum Chordata, subphylum Urochordata) contain a group of oligopeptides called "tunichromes" in their blood cells. These peptides have been implicated in (a) metal chelation and accumulation/sequestration of vanadium or iron; (b) crosslinking of structural fibers in tunic formation, (c) wound healing and (d) defense reactions. However, their biosynthesis, metabolism, and biological function remain largely un-elucidated due to their extreme instability and high reactivity. Tunichromes and related compounds uniquely possess dehydrodopamine moieties, all originating from post-translational modification of peptidyl tyrosine. It is conceivable that the presence of such novel post-translationally modified groups provide attributes that are crucial for their biological roles. Therefore, we examined the chemistry and reactivity of tunichromes in light of the available knowledge of the biochemistry of simple monomeric dehydro-N-acyldopamine units. Based on the reactivity of such simple compounds, the potential biological activities of tunichromes are predicted. Their possible biosynthetic route from peptidyl tyrosine is critically evaluated to provide a better basis for unraveling their biological functions. Prevalence of dehydro-N-acyldopamine units in different tunichromes, some marine antibiotic compounds, insect cuticular sclerotizing precursors and some bioadhesive marine proteins may aid in the de novo design of unique biomaterials with potential antibiotic/adhesive properties.

Published by Elsevier Inc.

PMID:
22580032
[PubMed - indexed for MEDLINE]
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