DB code: D00531

CATH domain	3.40.30.10 : Glutaredoxin	Catalytic domain
CATH domain	1.20.1050.10 : Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
E.C.	2.5.1.18
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	Pfam
Q8MU52	Glutathione S-transferase	EC 2.5.1.18 PfGST	PF00043 (GST_C) PF02798 (GST_N) [Graphical View]

KEGG enzyme name
Glutathione transferase Glutathione S-transferase Glutathione S-alkyltransferase Glutathione S-aryltransferase S-(Hydroxylalkyl)-glutathione liase Glutathione S-aralkyltransferase Glutathione S-alkyl transferase GST

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
Q8MU52	GST_PLAFA	RX + GLUTATHIONE = HX + R-S-GLUTATHIONE.	Homodimer. In the absence of ligands two homodimers may interact to form a tetramer.

KEGG Pathways
Map code	Pathways	E.C.
MAP00480	Glutathione metabolism
MAP00980	Metabolism of xenobiotics by cytochrome P450
MAP00982	Drug metabolism - cytochrome P450

Compound table
	Substrates		Products		Intermediates
KEGG-id	C01322	C00051	C01318	C02320
E.C.
Compound	RX	Glutathione	HX	R-S-Glutathione
Type	halide	amino acids,carboxyl group,peptide/protein,sulfhydryl group	halide	amide group,carboxyl group,peptide/protein,sulfide group
ChEBI		16856 16856
PubChem		124886 25246407 124886 25246407

1oktA01	Unbound	Unbound	Unbound	Unbound
1oktB01	Unbound	Unbound	Unbound	Unbound
1pa3A01	Unbound	Unbound	Unbound	Unbound
1pa3B01	Unbound	Unbound	Unbound	Unbound
1q4jA01	Unbound	Unbound	Unbound	Bound:GTX
1q4jB01	Unbound	Unbound	Unbound	Bound:GTX
2aawA01	Unbound	Unbound	Unbound	Bound:GTX
2aawC01	Unbound	Unbound	Unbound	Bound:GTX
3fr3A01	Unbound	Unbound	Unbound	Analogue:GDS
3fr3B01	Unbound	Unbound	Unbound	Analogue:GDS
3fr6A01	Unbound	Unbound	Unbound	Unbound
3fr6B01	Unbound	Unbound	Unbound	Unbound
3fr9A01	Bound:GSH	Unbound	Unbound	Unbound
3fr9B01	Bound:GSH	Unbound	Unbound	Unbound
3frcA01	Unbound	Unbound	Unbound	Analogue:0HG
3frcB01	Unbound	Unbound	Unbound	Analogue:0HG
1oktA02	Unbound	Unbound	Unbound	Unbound
1oktB02	Unbound	Unbound	Unbound	Unbound
1pa3A02	Unbound	Unbound	Unbound	Unbound
1pa3B02	Unbound	Unbound	Unbound	Unbound
1q4jA02	Unbound	Unbound	Unbound	Unbound
1q4jB02	Unbound	Unbound	Unbound	Unbound
2aawA02	Unbound	Unbound	Unbound	Unbound
2aawC02	Unbound	Unbound	Unbound	Unbound
3fr3A02	Unbound	Unbound	Unbound	Unbound
3fr3B02	Unbound	Unbound	Unbound	Unbound
3fr6A02	Unbound	Unbound	Unbound	Unbound
3fr6B02	Unbound	Unbound	Unbound	Unbound
3fr9A02	Unbound	Unbound	Bound:_CL	Unbound
3fr9B02	Unbound	Unbound	Bound:_CL	Unbound
3frcA02	Unbound	Unbound	Unbound	Unbound
3frcB02	Unbound	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
literature [8], [9], [11] & [13]

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1oktA01	TYR 9
1oktB01	TYR 9
1pa3A01	TYR 9
1pa3B01	TYR 9
1q4jA01	TYR 9
1q4jB01	TYR 9
2aawA01	TYR 9
2aawC01	TYR 9
3fr3A01	TYR 9
3fr3B01	TYR 9
3fr6A01	TYR 9
3fr6B01	TYR 9
3fr9A01	TYR 9
3fr9B01	TYR 9
3frcA01	TYR 9
3frcB01	TYR 9
1oktA02
1oktB02
1pa3A02
1pa3B02
1q4jA02
1q4jB02
2aawA02
2aawC02
3fr3A02
3fr3B02
3fr6A02
3fr6B02
3fr9A02
3fr9B02
3frcA02
3frcB02

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[1]
[3]	p.652-3
[4]
[8]	p.13823-5, Fig.3, Fig.4
[12]

References
[1]
Resource
Comments	Review
Medline ID
PubMed ID	1782341
Journal	Chem Res Toxicol
Year	1991
Volume	4
Pages	131-40
Authors	Armstrong RN
Title	Glutathione S-transferases: reaction mechanism, structure, and function.
Related PDB
Related UniProtKB
[2]
Resource
Comments	Review
Medline ID
PubMed ID	1771176
Journal	Pharmacol Ther
Year	1991
Volume	51
Pages	35-46
Authors	van Bladeren PJ, van Ommen B
Title	The inhibition of glutathione S-transferases: mechanisms, toxic consequences and therapeutic benefits.
Related PDB
Related UniProtKB
[3]
Resource
Comments	Review
Medline ID
PubMed ID	8143720
Journal	Eur J Biochem
Year	1994
Volume	220
Pages	645-61
Authors	Dirr H, Reinemer P, Huber R
Title	X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
Related PDB
Related UniProtKB
[4]
Resource
Comments	Review
Medline ID
PubMed ID	9074797
Journal	Chem Res Toxicol
Year	1997
Volume	10
Pages	2-18
Authors	Armstrong RN
Title	Structure, catalytic mechanism, and evolution of the glutathione transferases.
Related PDB
Related UniProtKB
[5]
Resource
Comments	Review
Medline ID
PubMed ID	16399376
Journal	Methods Enzymol
Year	2005
Volume	401
Pages	1-8
Authors	Mannervik B, Board PG, Hayes JD, Listowsky I, Pearson WR
Title	Nomenclature for mammalian soluble glutathione transferases.
Related PDB
Related UniProtKB
[6]
Resource
Comments	Review
Medline ID
PubMed ID	17897613
Journal	Acta Trop
Year	2008
Volume	105
Pages	99-112
Authors	Torres-Rivera A, Landa A
Title	Glutathione transferases from parasites: a biochemical view.
Related PDB
Related UniProtKB
[7]
Resource
Comments	Review
Medline ID
PubMed ID	18691123
Journal	Curr Protein Pept Sci
Year	2008
Volume	9
Pages	325-37
Authors	Dourado DF, Fernandes PA, Ramos MJ
Title	Mammalian cytosolic glutathione transferases.
Related PDB
Related UniProtKB
[8]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND CATALYTIC ACTIVITY.
Medline ID
PubMed ID	14623980
Journal	Proc Natl Acad Sci U S A
Year	2003
Volume	100
Pages	13821-6
Authors	Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K
Title	X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
Related PDB	1okt
Related UniProtKB	Q8MU52
[9]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE.
Medline ID
PubMed ID	12972411
Journal	J Biol Chem
Year	2004
Volume	279
Pages	1336-42
Authors	Perbandt M, Burmeister C, Walter RD, Betzel C, Liebau E
Title	Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum.
Related PDB	1pa3 1q4j
Related UniProtKB	Q8MU52
[10]
Resource
Comments
Medline ID
PubMed ID	16399390
Journal	Methods Enzymol
Year	2005
Volume	401
Pages	241-53
Authors	Deponte M, Becker K
Title	Glutathione S-transferase from malarial parasites: structural and functional aspects.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID	15888443
Journal	J Biol Chem
Year	2005
Volume	280
Pages	26121-8
Authors	Liebau E, De Maria F, Burmeister C, Perbandt M, Turella P, Antonini G, Federici G, Giansanti F, Stella L, Lo Bello M, Caccuri AM, Ricci G
Title	Cooperativity and pseudo-cooperativity in the glutathione S-transferase from Plasmodium falciparum.
Related PDB
Related UniProtKB
[12]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SELF-ASSOCIATION, AND MUTAGENESIS OF TYR-9; LYS-15; GLN-71; CYS-101 AND TYR-211.
Medline ID
PubMed ID	16385005
Journal	Protein Sci
Year	2006
Volume	15
Pages	281-9
Authors	Hiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K
Title	Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Related PDB	2aaw
Related UniProtKB	Q8MU52
[13]
Resource
Comments
Medline ID
PubMed ID	17941979
Journal	BMC Struct Biol
Year	2007
Volume	7
Pages	67
Authors	Tripathi T, Rahlfs S, Becker K, Bhakuni V
Title	Glutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID	19531494
Journal	J Biol Chem
Year	2009
Volume	284
Pages	22133-9
Authors	Liebau E, Dawood KF, Fabrini R, Fischer-Riepe L, Perbandt M, Stella L, Pedersen JZ, Bocedi A, Petrarca P, Federici G, Ricci G
Title	Tetramerization and cooperativity in Plasmodium falciparum glutathione S-transferase are mediated by atypic loop 113-119.
Related PDB	3fr3 3fr6 3fr9 3frc
Related UniProtKB

Comments
There are various classes in GST enzymes. This enzyme is similar to none of the known GST classes (see [8]). This enzyme family, GST, which catalyzes the conjugation of glutathione (GSH) to a variety of hydrophobic compounds, has an active-site that is composed of two binding sites: the G site, which binds reduced GSH, whilst the H site, which can bind a various kinds of compounds or substrates (see [8]). The H site of GST enzymes is more variable than the G site, due to a number of those substrates (see [8]). Moreover, this enzyme has dual functions: one is conjugation of GSH to substrates, the other is peroxidase activity (see [11]).

Comments

There are various classes in GST enzymes. This enzyme is similar to none of the known GST classes (see [8]).
This enzyme family, GST, which catalyzes the conjugation of glutathione (GSH) to a variety of hydrophobic compounds, has an active-site that is composed of two binding sites: the G site, which binds reduced GSH, whilst the H site, which can bind a various kinds of compounds or substrates (see [8]). The H site of GST enzymes is more variable than the G site, due to a number of those substrates (see [8]).
Moreover, this enzyme has dual functions: one is conjugation of GSH to substrates, the other is peroxidase activity (see [11]).

Created	Updated
2008-03-30	2015-01-13