GST_ASADI
ID GST_ASADI Reviewed; 15 AA.
AC P83246;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
DE AltName: Full=adGST;
DE Flags: Fragment;
OS Asaphis dichotoma.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Cardiida; Tellinoidea; Psammobiidae; Asaphis.
OX NCBI_TaxID=184428 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND CIRCULAR
RP DICHROISM ANALYSIS.
RC TISSUE=Gut, and Liver;
RX PubMed=12139969; DOI=10.1016/s0003-9861(02)00223-0;
RA Yang H.-L., Nie L.-J., Zhu S.-G., Zhou X.-W.;
RT "Purification and characterization of a novel glutathione S-transferase
RT from Asaphis dichotoma.";
RL Arch. Biochem. Biophys. 403:202-208(2002).
CC -!- FUNCTION: Has a strong specific activity toward 1-chloro-2,4-
CC dinitrobenzene and ethacrynic acid. {ECO:0000269|PubMed:12139969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:12139969};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:12139969};
CC KM=0.106 mM for glutathione {ECO:0000269|PubMed:12139969};
CC Vmax=0.1446 mmol/min/mg enzyme toward CDNB
CC {ECO:0000269|PubMed:12139969};
CC Vmax=0.033 mmol/min/mg enzyme toward GSH
CC {ECO:0000269|PubMed:12139969};
CC pH dependence:
CC Optimum pH is 8.5 with 1-chloro-2,4-dinitrobenzene as substrate.
CC {ECO:0000269|PubMed:12139969};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12139969}.
CC -!- MASS SPECTROMETRY: Mass=23138; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12139969};
CC -!- MISCELLANEOUS: In A.dichotoma there are at least two isozymes of
CC glutathione S-transferase. {ECO:0000269|PubMed:12139969}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000250|UniProtKB:P20137}.
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DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Transferase.
FT CHAIN 1..>15
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185923"
FT BINDING 7
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT NON_TER 15
FT /evidence="ECO:0000303|PubMed:12139969"
SQ SEQUENCE 15 AA; 1767 MW; CB3E4BF92D3CB0B9 CRC64;
PSYKLHYFDL RAAGE