ggt - Escherichia coli K-12
Glutathione hydrolase proenzyme
> ggt - Escherichia coli K-12 [Glutathione hydrolase proenzyme]
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Metadata
Organism Source: 83333 - Escherichia coli K-12
EC Number: 2.3.2.2 / 3.4.19.13
Cluster:
Registry Model:
Reactions
| reaction id | name | note |
|---|---|---|
| KEGG:R00494 | glutathione gamma-glutamylaminopeptidase | Glutathione + H2O <=> Cys-Gly + L-Glutamate |
| KEGG:R01262 | glutathione:L-amino-acid 5-glutamyltransferase | Glutathione + L-Amino acid <=> Cys-Gly + (5-L-Glutamyl)-L-amino acid |
| KEGG:R01687 | (5-L-glutamyl)-peptide:taurine 5-glutamyltransferase | (5-L-Glutamyl)-peptide + Taurine <=> Peptide + 5-L-Glutamyl-taurine |
| KEGG:R03867 | (5-glutamyl)-peptide:amino-acid 5-glutamyltransferase | Leukotriene C4 + Amino acid <=> Leukotriene D4 + 5-L-Glutamyl amino acid |
| KEGG:R03916 | (5-glutamyl)-peptide:amino-acid 5-glutamyltransferase | R-S-Glutathione + H2O <=> R-S-Cysteinylglycine + L-Glutamate |
| KEGG:R03970 | (5-glutamyl)-peptide:amino-acid 5-glutamyltransferase | 3-Cyano-L-alanine + L-Glutamate <=> gamma-Glutamyl-beta-cyanoalanine + H2O |
| KEGG:R03971 | gamma-glutamyl-beta-aminopropiononitrile amidohydrolase | 3-Aminopropiononitrile + L-Glutamate <=> gamma-Glutamyl-beta-aminopropiononitrile + H2O |
| KEGG:R04159 | (5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase | (5-L-Glutamyl)-peptide + Amino acid <=> Peptide + 5-L-Glutamyl amino acid |
| KEGG:R04935 | (5-L-glutamyl)-peptide:Se-methylselenocysteine 5-glutamyltransferase | (5-L-Glutamyl)-peptide + Se-Methyl-L-selenocysteine <=> Peptide + gamma-Glutamyl-Se-methylselenocysteine |
| BioCyc:RXN-12618 | GLUTATHIONE + WATER --> CYS-GLY + GLT | |
| BioCyc:RXN-18092 | GLUTATHIONE + GLYCYLGLYCINE --> CPD-19395 + CYS-GLY | |
| BioCyc:GAMMA-GLUTAMYLTRANSFERASE-RXN | 5-L-GLUTAMYL-PEPTIDE + Amino-Acids --> 5-L-GLUTAMYL-AMINO-ACID + Peptides-holder + 2 PROTON | |
| Rhea:RHEA:23905 | an N-terminal (5-L-glutamyl)-[peptide] + an α-amino acid => 5-L-glutamyl amino acid + an N-terminal L-α-aminoacyl-[peptide] | |
| Rhea:RHEA:23906 | 5-L-glutamyl amino acid + an N-terminal L-α-aminoacyl-[peptide] => an N-terminal (5-L-glutamyl)-[peptide] + an α-amino acid | |
| Rhea:RHEA:23907 | an N-terminal (5-L-glutamyl)-[peptide] + an α-amino acid <=> 5-L-glutamyl amino acid + an N-terminal L-α-aminoacyl-[peptide] | |
| Rhea:RHEA:28808 | glutathione + H2O => L-cysteinylglycine + L-glutamate | |
| Rhea:RHEA:28809 | L-cysteinylglycine + L-glutamate => glutathione + H2O | |
| Rhea:RHEA:28810 | glutathione + H2O <=> L-cysteinylglycine + L-glutamate | |
| Rhea:RHEA:59469 | an S-substituted glutathione + H2O => an S-substituted L-cysteinylglycine + L-glutamate | |
| Rhea:RHEA:59470 | an S-substituted L-cysteinylglycine + L-glutamate => an S-substituted glutathione + H2O | |
| Rhea:RHEA:59471 | an S-substituted glutathione + H2O <=> an S-substituted L-cysteinylglycine + L-glutamate | |
| BioCyc:RXN-19578 | CPDQT-434 + WATER --> CPD-21170 + GLT | Hydrolysis of a γ-glutamyl bond.A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH.Commonly studied with folylpoly-γ-glutamate as substrate, with which the initial cleavagemay release glutamate or poly-γ-glutamate of two or more residues, according to the speciesof origin of the enzyme. Final products are pteroyl-α-glutamate (folic acid) and free glutamate.Highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid (leaving group).Action on γ-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it isnot known whether an N-terminal γ-Glu residue can be hydrolysed.Type example of peptidase family C26. Formerly EC 3.4.22.12 |
| BioCyc:RXN-9157 | GLUTATHIONE + CPD-9699 --> CPD-9700 + CYS-GLY | |
| BioCyc:RXN-19607 | CPD-21162 + WATER --> CPD-21201 + GLT | |
| BioCyc:RXN-19602 | CPD-21194 + WATER --> CPD-21195 + GLT | |
| BioCyc:RXN66-336 | LEUKOTRIENE-C4 + Amino-Acids-20 --> 5-L-GLUTAMYL-L-AMINO-ACID + CPD66-21 | |
| BioCyc:RXN-19574 | CPD-21172 + WATER --> CPD-21171 + GLT | Hydrolysis of a γ-glutamyl bond.A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH.Commonly studied with folylpoly-γ-glutamate as substrate, with which the initial cleavagemay release glutamate or poly-γ-glutamate of two or more residues, according to the speciesof origin of the enzyme. Final products are pteroyl-α-glutamate (folic acid) and free glutamate.Highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid (leaving group).Action on γ-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it isnot known whether an N-terminal γ-Glu residue can be hydrolysed.Type example of peptidase family C26. Formerly EC 3.4.22.12 |
| BioCyc:RXN-13675 | CPD-14704 + WATER --> CPD-14705 + GLT | |
| BioCyc:RXN-19608 | S-METHYLGLUTATHIONE + WATER --> CPD-21202 + GLT | |
| BioCyc:RXN-6641 | S-Substituted-Glutathione + WATER --> CPD-6262 + GLT | |
| BioCyc:RXN-6601 | GLUTATHIONE + Amino-Acids-20 --> 5-L-GLUTAMYL-L-AMINO-ACID + CYS-GLY | |
| BioCyc:RXN-19572 | CPD-21160 + WATER --> CPD-21166 + GLT | Hydrolysis of a γ-glutamyl bond.A lysosomal or secreted, thiol-dependent peptidase, most active at acidic pH.Commonly studied with folylpoly-γ-glutamate as substrate, with which the initial cleavagemay release glutamate or poly-γ-glutamate of two or more residues, according to the speciesof origin of the enzyme. Final products are pteroyl-α-glutamate (folic acid) and free glutamate.Highly specific for the γ-glutamyl bond, but not for the C-terminal amino acid (leaving group).Action on γ-glutamyl bonds is independent of an N-terminal pteroyl moiety, but it isnot known whether an N-terminal γ-Glu residue can be hydrolysed.Type example of peptidase family C26. Formerly EC 3.4.22.12 |
| BioCyc:RXN-19604 | CPD-21199 + WATER --> CPD-21107 + GLT | |
| BioCyc:RXN-19732 | CPD-21344 + WATER --> CPD-21345 + GLT | |
| BioCyc:RXN-19627 | CPD-21241 + WATER --> CPD-21134 + GLT | |
| BioCyc:RXN-22398 | CPD-24389 + WATER --> CPD-24391 + GLT |
Pathways
| pathway id | name |
|---|