Evaluation of possible active site residues in GSTZ 1-1

M. Coggan; D. Liu; G. Chelvanayagam; W. B. Anderson; M. W. Anders; P. G. Board

Evaluation of possible active site residues in GSTZ 1-1

M. Coggan, D. Liu, G. Chelvanayagam, W. B. Anderson, M. W. Anders, P. G. Board^*

^*Corresponding author for this work

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

2 Citations (Scopus)

Abstract

Zeta class of glutathione transferases are responsible for several novel glutathione-dependent reactions including the isomerization of maleylacetoacetate to fumarylacetoacetate and the biotransformation of α halo acids such as dichloroacetic acid (DCA). N-terminal domain Tyr, Ser, Arg and Cys residues have been implicated in catalysis in other GST classes. A model structure for the N-terminal domain implicates Ser 14 as a significant active site residue and its mutation to Ala inactivates GSTZ1-1 with DCA and chlorofluroacetate. In contrast the mutations Tyr9Phe and Cys16Ala give rise to increased activity with DCA.

Original language	English
Pages (from-to)	185-187
Number of pages	3
Journal	Chemico-Biological Interactions
Volume	133
Issue number	1-3
Publication status	Published - 28 Feb 2001

Cite this

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title = "Evaluation of possible active site residues in GSTZ 1-1",

abstract = "Zeta class of glutathione transferases are responsible for several novel glutathione-dependent reactions including the isomerization of maleylacetoacetate to fumarylacetoacetate and the biotransformation of α halo acids such as dichloroacetic acid (DCA). N-terminal domain Tyr, Ser, Arg and Cys residues have been implicated in catalysis in other GST classes. A model structure for the N-terminal domain implicates Ser 14 as a significant active site residue and its mutation to Ala inactivates GSTZ1-1 with DCA and chlorofluroacetate. In contrast the mutations Tyr9Phe and Cys16Ala give rise to increased activity with DCA.",

keywords = "Dichloroacetic acid, Glutathione transferase zeta, Mutagenesis",

author = "M. Coggan and D. Liu and G. Chelvanayagam and Anderson, {W. B.} and Anders, {M. W.} and Board, {P. G.}",

year = "2001",

month = feb,

day = "28",

language = "English",

volume = "133",

pages = "185--187",

journal = "Chemico-Biological Interactions",

issn = "0009-2797",

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T1 - Evaluation of possible active site residues in GSTZ 1-1

AU - Coggan, M.

AU - Liu, D.

AU - Chelvanayagam, G.

AU - Anderson, W. B.

AU - Anders, M. W.

AU - Board, P. G.

PY - 2001/2/28

Y1 - 2001/2/28

N2 - Zeta class of glutathione transferases are responsible for several novel glutathione-dependent reactions including the isomerization of maleylacetoacetate to fumarylacetoacetate and the biotransformation of α halo acids such as dichloroacetic acid (DCA). N-terminal domain Tyr, Ser, Arg and Cys residues have been implicated in catalysis in other GST classes. A model structure for the N-terminal domain implicates Ser 14 as a significant active site residue and its mutation to Ala inactivates GSTZ1-1 with DCA and chlorofluroacetate. In contrast the mutations Tyr9Phe and Cys16Ala give rise to increased activity with DCA.

AB - Zeta class of glutathione transferases are responsible for several novel glutathione-dependent reactions including the isomerization of maleylacetoacetate to fumarylacetoacetate and the biotransformation of α halo acids such as dichloroacetic acid (DCA). N-terminal domain Tyr, Ser, Arg and Cys residues have been implicated in catalysis in other GST classes. A model structure for the N-terminal domain implicates Ser 14 as a significant active site residue and its mutation to Ala inactivates GSTZ1-1 with DCA and chlorofluroacetate. In contrast the mutations Tyr9Phe and Cys16Ala give rise to increased activity with DCA.

KW - Dichloroacetic acid

KW - Glutathione transferase zeta

KW - Mutagenesis

UR - http://www.scopus.com/inward/record.url?scp=0003206680&partnerID=8YFLogxK

M3 - Article

SN - 0009-2797

VL - 133

SP - 185

EP - 187

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

IS - 1-3

ER -

Evaluation of possible active site residues in GSTZ 1-1

Abstract

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