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Effects of known phenoloxidase inhibitors on hemocyanin-derived phenoloxidase from Limulus polyphemus

Research output: Contribution to journalArticle

Author(s)

Jamie Wright, William McCaskill Clark, Jennifer A. Cain, Alan Patterson, Christopher J. Coates, Jacqueline Nairn

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Abstract

Inhibitors of phenoloxidase are used routinely to characterise the structural and functional properties of phenoloxidases. Hemocyanin-derived phenoloxidase activity is also sensitive to standard phenoloxidase inhibitors. In this study, we characterise the effects of a number of phenoloxidase inhibitors on hemocyanin-derived phenoloxidase activity from the chelicerate, Limulus polyphemus. Both inhibition type and K-i values were similar to those observed for hemocyanin-derived phenoloxidase from another chelicerate, Eurypelma californicum. In addition, substrate inhibition was observed at concentrations above 2 mM dopamine. The conformation in which two of the inhibitors, namely tropolone and kojic acid, would bind near the Cu(II) centre of hemocyanin is proposed. (c) 2012 Elsevier Inc. All rights reserved.

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Details

Original languageEnglish
Pages (from-to)303-308
Number of pages6
JournalComparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology
Volume163
Issue number3-4
DOIs
Publication statusPublished - Nov 2012

    Research areas

  • Hemocyanin, Phenoloxidase, Hemocyanin-derived phenoloxidase, Kinetics, Inhibition, AGARICUS-BISPORUS TYROSINASE, CATECHOLOXIDASE ACTIVITY, TARANTULA HEMOCYANIN, OXIDASE ACTIVATION, CRYSTAL-STRUCTURE, CANCER-MAGISTER, HORSESHOE-CRAB, PROPHENOLOXIDASE, CONVERSION, TROPOLONE

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