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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

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.

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

Keywords

  • 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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