Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Akhtar, T.A.; McQuinn, R.P.; Naponelli, V.; Gregory, J.F.; Giovannoni, J.J.; Hanson, A.D.
    Tomato gamma-glutamylhydrolases: expression, characterization, and evidence for heterodimer formation (2008), Plant Physiol., 148, 775-785.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.9 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
3.4.19.9 when coexpressed in Escherichia coli, LeGGH1 forms heterodimers with an intermediate bond cleavage preference Solanum lycopersicum
3.4.19.9 when coexpressed in Escherichia coli, LeGGH2 forms heterodimers with an intermediate bond cleavage preference Solanum lycopersicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.9 0.00098
-
p-aminobenzoylpentaglutamate
-
Solanum lycopersicum
3.4.19.9 0.0012
-
folic acid pentaglutamate
-
Solanum lycopersicum
3.4.19.9 0.00131
-
p-aminobenzoylpentaglutamate
-
Solanum lycopersicum
3.4.19.9 0.00138
-
folic acid pentaglutamate
-
Solanum lycopersicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.19.9 36300
-
calculated from sequence Solanum lycopersicum
3.4.19.9 36400
-
calculated from sequence Solanum lycopersicum
3.4.19.9 36700
-
calculated from sequence Solanum lycopersicum
3.4.19.9 39000
-
SDS-PAGE Solanum lycopersicum
3.4.19.9 40000
-
SDS-PAGE Solanum lycopersicum
3.4.19.9 42000
-
SDS-PAGE Solanum lycopersicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.19.9 folic acid pentaglutamate + H2O Solanum lycopersicum PteGlu5 ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 p-aminobenzoylpentaglutamate + H2O Solanum lycopersicum pABAGlu5 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.9 Solanum lycopersicum B2Z9Y3 Ailsa Craig
-
3.4.19.9 Solanum lycopersicum B2Z9Y4 Ailsa Craig
-
3.4.19.9 Solanum lycopersicum B2Z9Y5 Ailsa Craig
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.9 recombinant proteins are purified by Ni2+ affinity chromatography Solanum lycopersicum
3.4.19.9 recombinant proteins are purified by Ni2+ affinity chromatography; in the case of LeGGH1, an additional cation exchange step is required Solanum lycopersicum

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.19.9 flower bud
-
Solanum lycopersicum
-
3.4.19.9 fruit and all other organs Solanum lycopersicum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.9 folic acid pentaglutamate + H2O PteGlu5 Solanum lycopersicum ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 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 ?
-
?
3.4.19.9 p-aminobenzoylpentaglutamate + H2O pABAGlu5 Solanum lycopersicum ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.19.9 heterodimer
-
Solanum lycopersicum
3.4.19.9 heterodimer the homodimer is catalytically inactive Solanum lycopersicum

Synonyms

EC Number Synonyms Comment Organism
3.4.19.9 gamma-glutamyl hydrolase
-
Solanum lycopersicum
3.4.19.9 GGH
-
Solanum lycopersicum
3.4.19.9 LeGGH1
-
Solanum lycopersicum
3.4.19.9 LeGGH2 expressed in fruit all other organs Solanum lycopersicum
3.4.19.9 LeGGH3 expressed mainly in flower buds, the homodimer is catalytically inactive Solanum lycopersicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.9 0.96
-
p-aminobenzoylpentaglutamate
-
Solanum lycopersicum
3.4.19.9 1.08
-
p-aminobenzoylpentaglutamate
-
Solanum lycopersicum
3.4.19.9 1.69
-
folic acid pentaglutamate
-
Solanum lycopersicum
3.4.19.9 2.13
-
folic acid pentaglutamate
-
Solanum lycopersicum