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Literature summary extracted from

  • Silink, M.; Reddel, R.; Bethel, M.; Rowe, P.B.
    Gamma-glutamyl hydrolase conjugase. Purification and properties of the bovine hepatic enzyme (1975), J. Biol. Chem., 250, 5982-5994.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.4.19.9 stability against various dialysis procedures Bos taurus
3.4.19.9 zinc is essential for stability Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.19.9 Cd2+
-
 Bos taurus
3.4.19.9 concanavalin A
-
 Bos taurus
3.4.19.9 Cu2+
-
 Bos taurus
3.4.19.9 Dextran sulfate
-
 Bos taurus
3.4.19.9 DNA
-
 Bos taurus
3.4.19.9 Fe3+
-
 Bos taurus
3.4.19.9 heparin
-
 Bos taurus
3.4.19.9 Hg2+
-
 Bos taurus
3.4.19.9 Mn2+
-
 Bos taurus
3.4.19.9 NEM
-
 Bos taurus
3.4.19.9 PCMB
-
 Bos taurus
3.4.19.9 RNA
-
 Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.19.9 0.0017
-
 Pteroyltriglutamate
-
 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.19.9 lysosome
-
 Bos taurus 5764
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.19.9 Zinc contains 4.15-4.47 zinc atoms per molecule of enzyme Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.19.9 108000
-
 gel filtration Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.9 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.19.9 glycoprotein
-
 Bos taurus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.9
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.19.9 liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.19.9 additional information
-
-
 Bos taurus

Storage Stability

EC Number Storage Stability Organism
3.4.19.9 4°C, 5.0 mM 2-mercaptoethanol, 40% loss of activity after 24 h Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.9 polyglutamylfolate + H2O bond cleavage occurs with equal facility at internal points of the peptide chain Bos taurus ?
-
 ?
3.4.19.9 polyglutamylfolate + H2O longer chain gamma-glutamyl peptides are preferentially attacked by the enzyme Bos taurus ?
-
 ?
3.4.19.9 polyglutamylfolate + H2O peptide bond cleavage occurs only at gamma-glutamyl bonds and the presence of a COOH-terminal gamma bond is essential for enzyme action Bos taurus ?
-
 ?
3.4.19.9 polyglutamylfolate + H2O the cleavage of diglutamyl peptides is extremely slow Bos taurus ?
-
 ?
3.4.19.9 polyglutamylfolate + H2O the cleavage of gamma bonds is independent of the NH2-terminal pteroyl moiety Bos taurus ?
-
 ?
3.4.19.9 pteroyltriglutamate + H2O
-
 Bos taurus ?
-
 ?
3.4.19.9 pteroyltriglutamate + H2O
-
 Bos taurus pteroylglutamate + glutamate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.9 70
-
-
 Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.19.9 65
-
 little thermal denaturation below Bos taurus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.19.9 additional information
-
 additional information pteroyltriglutamate: 732 gamma-glutamyl bonds are cleaved per min per mol of enzyme Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.9 3.9
-
 sodium acetate buffer Bos taurus
3.4.19.9 4.5
-
 sodium citrate buffer Bos taurus