Evolution of functional diversity as observed through structural studies of glutathione transferases

Michael W. Parker; William J. McKinstry; Aaron J. Oakley; Galina Polekhina; Jamie Rossjohn; Gareth Chelvanayagam; Philip G. Board; Carmine Di Ilio; Anna Maria Caccuri; Giorgio Ricci; Mario Lo Bello

Evolution of functional diversity as observed through structural studies of glutathione transferases

Michael W. Parker^*, William J. McKinstry, Aaron J. Oakley, Galina Polekhina, Jamie Rossjohn, Gareth Chelvanayagam, Philip G. Board, Carmine Di Ilio, Anna Maria Caccuri, Giorgio Ricci, Mario Lo Bello

^*Corresponding author for this work

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

2 Citations (Scopus)

Abstract

Most enzymes bind specifically to one or to a few closely related substrates. However, this is not the case for the enzyme superfamily of glutathione S-transferases (GSTs). The enzyme's ability to recognise a diverse range of substrates is due, in part, to the existence of isoforms. We have determined the crystal structures of GSTs from four classes and from a diverse range of organisms ranging from bacteria to human. These studies are revealing the molecular basis and evolutionary development of how GSTs recognise and react with a structurally diverse array of toxins.

Original language	English
Pages (from-to)	8-12
Number of pages	5
Journal	Chemico-Biological Interactions
Volume	133
Issue number	1-3
Publication status	Published - 28 Feb 2001

Cite this

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title = "Evolution of functional diversity as observed through structural studies of glutathione transferases",

abstract = "Most enzymes bind specifically to one or to a few closely related substrates. However, this is not the case for the enzyme superfamily of glutathione S-transferases (GSTs). The enzyme's ability to recognise a diverse range of substrates is due, in part, to the existence of isoforms. We have determined the crystal structures of GSTs from four classes and from a diverse range of organisms ranging from bacteria to human. These studies are revealing the molecular basis and evolutionary development of how GSTs recognise and react with a structurally diverse array of toxins.",

keywords = "Crystallography, Evolution, Glutathione transferase, Structure",

author = "Parker, {Michael W.} and McKinstry, {William J.} and Oakley, {Aaron J.} and Galina Polekhina and Jamie Rossjohn and Gareth Chelvanayagam and Board, {Philip G.} and {Di Ilio}, Carmine and Caccuri, {Anna Maria} and Giorgio Ricci and {Lo Bello}, Mario",

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language = "English",

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T1 - Evolution of functional diversity as observed through structural studies of glutathione transferases

AU - Parker, Michael W.

AU - McKinstry, William J.

AU - Oakley, Aaron J.

AU - Polekhina, Galina

AU - Rossjohn, Jamie

AU - Chelvanayagam, Gareth

AU - Board, Philip G.

AU - Di Ilio, Carmine

AU - Caccuri, Anna Maria

AU - Ricci, Giorgio

AU - Lo Bello, Mario

PY - 2001/2/28

Y1 - 2001/2/28

N2 - Most enzymes bind specifically to one or to a few closely related substrates. However, this is not the case for the enzyme superfamily of glutathione S-transferases (GSTs). The enzyme's ability to recognise a diverse range of substrates is due, in part, to the existence of isoforms. We have determined the crystal structures of GSTs from four classes and from a diverse range of organisms ranging from bacteria to human. These studies are revealing the molecular basis and evolutionary development of how GSTs recognise and react with a structurally diverse array of toxins.

AB - Most enzymes bind specifically to one or to a few closely related substrates. However, this is not the case for the enzyme superfamily of glutathione S-transferases (GSTs). The enzyme's ability to recognise a diverse range of substrates is due, in part, to the existence of isoforms. We have determined the crystal structures of GSTs from four classes and from a diverse range of organisms ranging from bacteria to human. These studies are revealing the molecular basis and evolutionary development of how GSTs recognise and react with a structurally diverse array of toxins.

KW - Crystallography

KW - Evolution

KW - Glutathione transferase

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=0003139175&partnerID=8YFLogxK

M3 - Article

SN - 0009-2797

VL - 133

SP - 8

EP - 12

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

IS - 1-3

ER -

Evolution of functional diversity as observed through structural studies of glutathione transferases

Abstract

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