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

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

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

22 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 2mM 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.

Original language	English
Pages (from-to)	303-308
Number of pages	6
Journal	Comparative Biochemistry and Physiology - 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
Externally published	Yes

Keywords

Hemocyanin
Hemocyanin-derived phenoloxidase
Inhibition
Kinetics
Phenoloxidase

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10.1016/j.cbpb.2012.07.003

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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 Ki values were similar to those observed for hemocyanin-derived phenoloxidase from another chelicerate, Eurypelma californicum. In addition, substrate inhibition was observed at concentrations above 2mM 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.",

keywords = "Hemocyanin, Hemocyanin-derived phenoloxidase, Inhibition, Kinetics, Phenoloxidase",

author = "Jamie Wright and Clark, {William Mc Caskill} 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 - B Biochemistry and Molecular Biology",

issn = "1096-4959",

publisher = "Elsevier Inc.",

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}

Effects of known phenoloxidase inhibitors on hemocyanin-derived phenoloxidase from Limulus polyphemus. / Wright, Jamie; Clark, William Mc Caskill; Cain, Jennifer A. et al.
In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 163, No. 3-4, 11.2012, p. 303-308.

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

TY - JOUR

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

AU - Wright, Jamie

AU - Clark, William Mc Caskill

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 Ki values were similar to those observed for hemocyanin-derived phenoloxidase from another chelicerate, Eurypelma californicum. In addition, substrate inhibition was observed at concentrations above 2mM 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.

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 Ki values were similar to those observed for hemocyanin-derived phenoloxidase from another chelicerate, Eurypelma californicum. In addition, substrate inhibition was observed at concentrations above 2mM 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.

KW - Hemocyanin

KW - Hemocyanin-derived phenoloxidase

KW - Inhibition

KW - Kinetics

KW - Phenoloxidase

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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 - B Biochemistry and Molecular Biology

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

IS - 3-4

ER -

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

Abstract

Keywords

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