GSTA3 protein (human) - STRING database

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GSTA3

Glutathione S-transferase A3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively; Soluble glutathione S-transferases (222 aa)

Predicted Functional Partners:

GGH

0.902

GSTA2

0.875

GSTA1

0.872

GSTT2B

0.839

GSTO1

0.831

GPX7

0.827

GSTM5

0.822

GSTO2

0.819

MGST1

0.803

GGT1

0.802

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
GGH	GSTA1	ENSP00000260118	ENSP00000335620	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase A1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.903
GGH	GSTA2	ENSP00000260118	ENSP00000420168	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase A2; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.902
GGH	GSTA3	ENSP00000260118	ENSP00000211122	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase A3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively; Soluble glutathione S-transferases	0.902
GGH	GSTM5	ENSP00000260118	ENSP00000256593	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase Mu 5; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Soluble glutathione S-transferases	0.902
GGH	GSTO2	ENSP00000260118	ENSP00000345023	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase omega-2; Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA); Belongs to the GST superfamily. Omega family	0.900
GGH	GSTT2B	ENSP00000260118	ENSP00000290765	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Glutathione S-transferase theta-2B; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity; Soluble glutathione S-transferases	0.904
GGH	MGST1	ENSP00000260118	ENSP00000379512	Gamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family	Microsomal glutathione S-transferase 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity; Microsomal glutathione S-transferases	0.902
GGT1	GPX7	ENSP00000383232	ENSP00000354677	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family	0.728
GGT1	GSTA1	ENSP00000383232	ENSP00000335620	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase A1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.686
GGT1	GSTA2	ENSP00000383232	ENSP00000420168	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase A2; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.694
GGT1	GSTA3	ENSP00000383232	ENSP00000211122	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase A3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively; Soluble glutathione S-transferases	0.802
GGT1	GSTM5	ENSP00000383232	ENSP00000256593	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase Mu 5; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Soluble glutathione S-transferases	0.664
GGT1	GSTO1	ENSP00000383232	ENSP00000358727	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase omega-1; Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid; Soluble glutathione S-transferases	0.676
GGT1	GSTO2	ENSP00000383232	ENSP00000345023	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase omega-2; Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA); Belongs to the GST superfamily. Omega family	0.674
GGT1	GSTT2B	ENSP00000383232	ENSP00000290765	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Glutathione S-transferase theta-2B; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a sulfatase activity; Soluble glutathione S-transferases	0.709
GGT1	MGST1	ENSP00000383232	ENSP00000379512	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	Microsomal glutathione S-transferase 1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has a wide substrate specificity; Microsomal glutathione S-transferases	0.672
GPX7	GGT1	ENSP00000354677	ENSP00000383232	Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family	Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...]	0.728
GPX7	GSTA1	ENSP00000354677	ENSP00000335620	Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family	Glutathione S-transferase A1; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.768
GPX7	GSTA2	ENSP00000354677	ENSP00000420168	Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family	Glutathione S-transferase A2; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles; Belongs to the GST superfamily. Alpha family	0.774
GPX7	GSTA3	ENSP00000354677	ENSP00000211122	Glutathione peroxidase 7; It protects esophageal epithelia from hydrogen peroxide- induced oxidative stress. It suppresses acidic bile acid-induced reactive oxigen species (ROS) and protects against oxidative DNA damage and double-strand breaks; Belongs to the glutathione peroxidase family	Glutathione S-transferase A3; Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)- pregnene-3,20-dione, precursors to testosterone and progesterone, respectively; Soluble glutathione S-transferases	0.827

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