EzCatDB: D00531
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DB codeD00531
CATH domainDomain 13.40.30.10 : GlutaredoxinCatalytic domain
Domain 21.20.1050.10 : Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
E.C.2.5.1.18


Enzyme Name
UniProtKBKEGG

Q8MU52
Protein nameGlutathione S-transferaseGlutathione transferase
Glutathione S-transferase
Glutathione S-alkyltransferase
Glutathione S-aryltransferase
S-(Hydroxylalkyl)-glutathione liase
Glutathione S-aralkyltransferase
Glutathione S-alkyl transferase
GST
SynonymsEC 2.5.1.18
PfGST
PfamPF00043 (GST_C)
PF02798 (GST_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00480Glutathione metabolism
MAP00980Metabolism of xenobiotics by cytochrome P450
MAP00982Drug metabolism - cytochrome P450

UniProtKB:Accession NumberQ8MU52
Entry nameGST_PLAFA
ActivityRX + GLUTATHIONE = HX + R-S-GLUTATHIONE.
SubunitHomodimer. In the absence of ligands two homodimers may interact to form a tetramer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01322C00051C01318C02320
CompoundRXGlutathioneHXR-S-Glutathione
Typehalideamino acids,carboxyl group,peptide/protein,sulfhydryl grouphalideamide group,carboxyl group,peptide/protein,sulfide group
ChEBI
16856


PubChem
25246407
124886


            
1oktA01UnboundUnboundUnboundUnbound
1oktB01UnboundUnboundUnboundUnbound
1pa3A01UnboundUnboundUnboundUnbound
1pa3B01UnboundUnboundUnboundUnbound
1q4jA01UnboundUnboundUnboundBound:GTX
1q4jB01UnboundUnboundUnboundBound:GTX
2aawA01UnboundUnboundUnboundBound:GTX
2aawC01UnboundUnboundUnboundBound:GTX
3fr3A01UnboundUnboundUnboundAnalogue:GDS
3fr3B01UnboundUnboundUnboundAnalogue:GDS
3fr6A01UnboundUnboundUnboundUnbound
3fr6B01UnboundUnboundUnboundUnbound
3fr9A01Bound:GSHUnboundUnboundUnbound
3fr9B01Bound:GSHUnboundUnboundUnbound
3frcA01UnboundUnboundUnboundAnalogue:0HG
3frcB01UnboundUnboundUnboundAnalogue:0HG
1oktA02UnboundUnboundUnboundUnbound
1oktB02UnboundUnboundUnboundUnbound
1pa3A02UnboundUnboundUnboundUnbound
1pa3B02UnboundUnboundUnboundUnbound
1q4jA02UnboundUnboundUnboundUnbound
1q4jB02UnboundUnboundUnboundUnbound
2aawA02UnboundUnboundUnboundUnbound
2aawC02UnboundUnboundUnboundUnbound
3fr3A02UnboundUnboundUnboundUnbound
3fr3B02UnboundUnboundUnboundUnbound
3fr6A02UnboundUnboundUnboundUnbound
3fr6B02UnboundUnboundUnboundUnbound
3fr9A02UnboundUnboundBound:_CLUnbound
3fr9B02UnboundUnboundBound:_CLUnbound
3frcA02UnboundUnboundUnboundUnbound
3frcB02UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [8], [9], [11] & [13]
pdbCatalytic residues
         
1oktA01TYR 9
1oktB01TYR 9
1pa3A01TYR 9
1pa3B01TYR 9
1q4jA01TYR 9
1q4jB01TYR 9
2aawA01TYR 9
2aawC01TYR 9
3fr3A01TYR 9
3fr3B01TYR 9
3fr6A01TYR 9
3fr6B01TYR 9
3fr9A01TYR 9
3fr9B01TYR 9
3frcA01TYR 9
3frcB01TYR 9
1oktA02            
1oktB02            
1pa3A02            
1pa3B02            
1q4jA02            
1q4jB02            
2aawA02            
2aawC02            
3fr3A02            
3fr3B02            
3fr6A02            
3fr6B02            
3fr9A02            
3fr9B02            
3frcA02            
3frcB02            

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]

[3]p.652-3
[4]

[8]p.13823-5, Fig.3, Fig.4
[12]


references
[1]
CommentsReview
PubMed ID1782341
JournalChem Res Toxicol
Year1991
Volume4
Pages131-40
AuthorsArmstrong RN
TitleGlutathione S-transferases: reaction mechanism, structure, and function.
[2]
CommentsReview
PubMed ID1771176
JournalPharmacol Ther
Year1991
Volume51
Pages35-46
Authorsvan Bladeren PJ, van Ommen B
TitleThe inhibition of glutathione S-transferases: mechanisms, toxic consequences and therapeutic benefits.
[3]
CommentsReview
PubMed ID8143720
JournalEur J Biochem
Year1994
Volume220
Pages645-61
AuthorsDirr H, Reinemer P, Huber R
TitleX-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
[4]
CommentsReview
PubMed ID9074797
JournalChem Res Toxicol
Year1997
Volume10
Pages2-18
AuthorsArmstrong RN
TitleStructure, catalytic mechanism, and evolution of the glutathione transferases.
[5]
CommentsReview
PubMed ID16399376
JournalMethods Enzymol
Year2005
Volume401
Pages1-8
AuthorsMannervik B, Board PG, Hayes JD, Listowsky I, Pearson WR
TitleNomenclature for mammalian soluble glutathione transferases.
[6]
CommentsReview
PubMed ID17897613
JournalActa Trop
Year2008
Volume105
Pages99-112
AuthorsTorres-Rivera A, Landa A
TitleGlutathione transferases from parasites: a biochemical view.
[7]
CommentsReview
PubMed ID18691123
JournalCurr Protein Pept Sci
Year2008
Volume9
Pages325-37
AuthorsDourado DF, Fernandes PA, Ramos MJ
TitleMammalian cytosolic glutathione transferases.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND CATALYTIC ACTIVITY.
PubMed ID14623980
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages13821-6
AuthorsFritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K
TitleX-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum.
Related PDB1okt
Related UniProtKBQ8MU52
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH S-HEXYL GLUTATHIONE.
PubMed ID12972411
JournalJ Biol Chem
Year2004
Volume279
Pages1336-42
AuthorsPerbandt M, Burmeister C, Walter RD, Betzel C, Liebau E
TitleNative and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum.
Related PDB1pa3,1q4j
Related UniProtKBQ8MU52
[10]
PubMed ID16399390
JournalMethods Enzymol
Year2005
Volume401
Pages241-53
AuthorsDeponte M, Becker K
TitleGlutathione S-transferase from malarial parasites: structural and functional aspects.
[11]
PubMed ID15888443
JournalJ Biol Chem
Year2005
Volume280
Pages26121-8
AuthorsLiebau 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
TitleCooperativity and pseudo-cooperativity in the glutathione S-transferase from Plasmodium falciparum.
[12]
CommentsX-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.
PubMed ID16385005
JournalProtein Sci
Year2006
Volume15
Pages281-9
AuthorsHiller N, Fritz-Wolf K, Deponte M, Wende W, Zimmermann H, Becker K
TitlePlasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Related PDB2aaw
Related UniProtKBQ8MU52
[13]
PubMed ID17941979
JournalBMC Struct Biol
Year2007
Volume7
Pages67
AuthorsTripathi T, Rahlfs S, Becker K, Bhakuni V
TitleGlutathione mediated regulation of oligomeric structure and functional activity of Plasmodium falciparum glutathione S-transferase.
[14]
PubMed ID19531494
JournalJ Biol Chem
Year2009
Volume284
Pages22133-9
AuthorsLiebau E, Dawood KF, Fabrini R, Fischer-Riepe L, Perbandt M, Stella L, Pedersen JZ, Bocedi A, Petrarca P, Federici G, Ricci G
TitleTetramerization and cooperativity in Plasmodium falciparum glutathione S-transferase are mediated by atypic loop 113-119.
Related PDB3fr3,3fr6,3fr9,3frc

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]).

createdupdated
2008-03-302015-01-13


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