Cloned (Comment) | Organism |
---|---|
when coexpressed in Escherichia coli, homodimer is catalytically inactive. LeGGH3 forms heterodimers with LeGGH1 or LeGGH2 that has one-half the activity of the matching homodimer | Solanum lycopersicum |
when coexpressed in Escherichia coli, LeGGH1 forms heterodimers with an intermediate bond cleavage preference | Solanum lycopersicum |
when coexpressed in Escherichia coli, LeGGH2 forms heterodimers with an intermediate bond cleavage preference | Solanum lycopersicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00098 | - |
p-aminobenzoylpentaglutamate | - |
Solanum lycopersicum | |
0.0012 | - |
folic acid pentaglutamate | - |
Solanum lycopersicum | |
0.00131 | - |
p-aminobenzoylpentaglutamate | - |
Solanum lycopersicum | |
0.00138 | - |
folic acid pentaglutamate | - |
Solanum lycopersicum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36300 | - |
calculated from sequence | Solanum lycopersicum |
36400 | - |
calculated from sequence | Solanum lycopersicum |
36700 | - |
calculated from sequence | Solanum lycopersicum |
39000 | - |
SDS-PAGE | Solanum lycopersicum |
40000 | - |
SDS-PAGE | Solanum lycopersicum |
42000 | - |
SDS-PAGE | Solanum lycopersicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
folic acid pentaglutamate + H2O | Solanum lycopersicum | PteGlu5 | ? | - |
? | |
additional information | Solanum lycopersicum | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase | ? | - |
? | |
additional information | Solanum lycopersicum | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate | ? | - |
? | |
additional information | Solanum lycopersicum | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5 | ? | - |
? | |
p-aminobenzoylpentaglutamate + H2O | Solanum lycopersicum | pABAGlu5 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Solanum lycopersicum | B2Z9Y3 | Ailsa Craig | - |
Solanum lycopersicum | B2Z9Y4 | Ailsa Craig | - |
Solanum lycopersicum | B2Z9Y5 | Ailsa Craig | - |
Purification (Comment) | Organism |
---|---|
recombinant proteins are purified by Ni2+ affinity chromatography | Solanum lycopersicum |
recombinant proteins are purified by Ni2+ affinity chromatography; in the case of LeGGH1, an additional cation exchange step is required | Solanum lycopersicum |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
flower bud | - |
Solanum lycopersicum | - |
fruit | and all other organs | Solanum lycopersicum | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
folic acid pentaglutamate + H2O | PteGlu5 | Solanum lycopersicum | ? | - |
? | |
additional information | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase | Solanum lycopersicum | ? | - |
? | |
additional information | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than p-aminobenzoylpentaglutamate | Solanum lycopersicum | ? | - |
? | |
additional information | folates typically have gamma-linked polyglutamyl tails that make them better enzyme substrates and worse transport substrates than the unglutamylated forms. The tail can be shortened or removed by the vacuolar enzyme gamma-glutamyl hydrolase. Cleaves PteGlu5 more efficiently than pABAGlu5 | Solanum lycopersicum | ? | - |
? | |
p-aminobenzoylpentaglutamate + H2O | pABAGlu5 | Solanum lycopersicum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | - |
Solanum lycopersicum |
heterodimer | the homodimer is catalytically inactive | Solanum lycopersicum |
Synonyms | Comment | Organism |
---|---|---|
gamma-glutamyl hydrolase | - |
Solanum lycopersicum |
GGH | - |
Solanum lycopersicum |
LeGGH1 | - |
Solanum lycopersicum |
LeGGH2 | expressed in fruit all other organs | Solanum lycopersicum |
LeGGH3 | expressed mainly in flower buds, the homodimer is catalytically inactive | Solanum lycopersicum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.96 | - |
p-aminobenzoylpentaglutamate | - |
Solanum lycopersicum | |
1.08 | - |
p-aminobenzoylpentaglutamate | - |
Solanum lycopersicum | |
1.69 | - |
folic acid pentaglutamate | - |
Solanum lycopersicum | |
2.13 | - |
folic acid pentaglutamate | - |
Solanum lycopersicum |