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

doi:10.1016/j.cbpb.2012.07.003

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

School of Biology

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	303-308
Number of pages	6
Journal	Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology
Volume	163
Issue number	3-4
DOIs	https://doi.org/10.1016/j.cbpb.2012.07.003
Publication status	Published - Nov 2012

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

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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10.1016/j.cbpb.2012.07.003

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@article{6165ed1cf1b447d687e43707663f413f,

title = "Effects of known phenoloxidase inhibitors on hemocyanin-derived phenoloxidase from Limulus polyphemus",

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.",

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",

author = "Jamie Wright and Clark, \{William McCaskill\} and Cain, \{Jennifer A.\} and Alan Patterson and Coates, \{Christopher J.\} and Jacqueline Nairn",

year = "2012",

month = nov,

doi = "10.1016/j.cbpb.2012.07.003",

language = "English",

volume = "163",

pages = "303--308",

journal = "Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology",

issn = "1096-4959",

publisher = "Elsevier Inc.",

number = "3-4",

}

TY - JOUR

T1 - Effects of known phenoloxidase inhibitors on hemocyanin-derived phenoloxidase from Limulus polyphemus

AU - Wright, Jamie

AU - Clark, William McCaskill

AU - Cain, Jennifer A.

AU - Patterson, Alan

AU - Coates, Christopher J.

AU - Nairn, Jacqueline

PY - 2012/11

Y1 - 2012/11

N2 - 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.

AB - 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.

KW - Hemocyanin

KW - Phenoloxidase

KW - Hemocyanin-derived phenoloxidase

KW - Kinetics

KW - Inhibition

KW - AGARICUS-BISPORUS TYROSINASE

KW - CATECHOLOXIDASE ACTIVITY

KW - TARANTULA HEMOCYANIN

KW - OXIDASE ACTIVATION

KW - CRYSTAL-STRUCTURE

KW - CANCER-MAGISTER

KW - HORSESHOE-CRAB

KW - PROPHENOLOXIDASE

KW - CONVERSION

KW - TROPOLONE

UR - https://www.scopus.com/pages/publications/84867903902

U2 - 10.1016/j.cbpb.2012.07.003

DO - 10.1016/j.cbpb.2012.07.003

M3 - Article

SN - 1096-4959

VL - 163

SP - 303

EP - 308

JO - Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology

IS - 3-4

ER -

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

Abstract

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Keywords

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