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Literature summary extracted from

  • Wodtke, R.; Schramm, G.; Pietzsch, J.; Pietsch, M.; Loeser, R.
    Synthesis and kinetic characterisation of water-soluble fluorogenic acyl donors for transglutaminase 2 (2016), ChemBioChem, 17, 1263-1281 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.13 iodoacetamide irreversible inhibition Cavia porcellus
2.3.2.13 N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide an selective Nepsilon-acryloyllysine derivative, irreversible inhibition Cavia porcellus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.13 additional information
-
additional information Michaelis-Menten kinetics, kinetic analysis of TGase 2-catalysed conversions of the glutamate-derived acyl donors, detailed overview Cavia porcellus
2.3.2.13 0.00114
-
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.00147
-
Z-Phe-gamma-Abu-7-hydroxycoumarin pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.00253
-
Z-Glu(HC)-Gly-OH pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.0066
-
Z-Glu(HMC)-Gly-OH pH 8.0, 30°C Cavia porcellus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.13 protein glutamine + alkylamine Cavia porcellus
-
protein N5-alkylglutamine + NH3
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Cavia porcellus H0VXN6
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.13 liver
-
Cavia porcellus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 additional information synthesis and kinetic characterisation of water-soluble fluorogenic acyl donors for transglutaminase 2, overview. Development of a fluorimetric TGase 2 activity assay with release of 7-hydroxycoumarin (HC) by TGase 2-catalysed hydrolysis or aminolysis of Z-Phe-gamma-Abu-HC resulting in a measureable increase in fluorescence. No activity with Z-Phe-gamma-Abu-7-amido-4-methylcoumarin and Z-Glu(AMC)-Gly-OH. Because the assay of TGase 2 requires the presence of an antioxidant to prevent oxidation of the active-site cysteine residue, both DTT and tris(2-carboxyethyl)phosphine (TCEP) are employed for investigations into the spontaneous reactivity of the compounds at a concentration of 0.5 mM. C-terminal extension with glycine results in kobs values that are increased by a factor of approximately four Cavia porcellus ?
-
-
2.3.2.13 peptide glutamine + aminoacetonitrile
-
Cavia porcellus ?
-
?
2.3.2.13 peptide glutamine + N-(biotinyl)cadaverine
-
Cavia porcellus ?
-
?
2.3.2.13 protein glutamine + alkylamine
-
Cavia porcellus protein N5-alkylglutamine + NH3
-
?
2.3.2.13 Z-Glu(HC)-Gly-OH + alkylamine
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Glu(HC)-Gly-OH + H2O
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Glu(HMC)-Gly-OH + alkylamine best substrate Cavia porcellus ?
-
?
2.3.2.13 Z-Glu(HMC)-Gly-OH + H2O best substrate Cavia porcellus ?
-
?
2.3.2.13 Z-Glu(HMC)-OH + alkylamine
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Glu(HMC)-OH + H2O
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + alkylamine
-
Cavia porcellus Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxy-4-methylcoumarin
-
?
2.3.2.13 Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin + H2O
-
Cavia porcellus Z-Phe-gamma-Abu-OH + 7-hydroxy-4-methylcoumarin
-
?
2.3.2.13 Z-Phe-gamma-Abu-7-hydroxycoumarin + alkylamine
-
Cavia porcellus Z-Phe-gamma-amino-N-alkylbutanamide + 7-hydroxycoumarin
-
?
2.3.2.13 Z-Phe-gamma-Abu-7-hydroxycoumarin + H2O
-
Cavia porcellus Z-Phe-gamma-Abu-OH + 7-hydroxycoumarin
-
?
2.3.2.13 Z-Phe-Glu(HC)-Gly-OH + alkylamine
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-Glu(HC)-Gly-OH + H2O
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-Glu(HMC)-Gly-OH + alkylamine
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-Glu(HMC)-Gly-OH + H2O
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-Glu(HMC)-OH + alkylamine
-
Cavia porcellus ?
-
?
2.3.2.13 Z-Phe-Glu(HMC)-OH + H2O
-
Cavia porcellus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.13 gpTGase 2
-
Cavia porcellus
2.3.2.13 TGase 2
-
Cavia porcellus
2.3.2.13 transglutaminase 2
-
Cavia porcellus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.13 30
-
assay at Cavia porcellus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.2.13 0.3
-
Z-Phe-gamma-Abu-7-hydroxycoumarin pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.32
-
Z-Glu(HMC)-Gly-OH pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.33
-
Z-Glu(HC)-Gly-OH pH 8.0, 30°C Cavia porcellus
2.3.2.13 0.52
-
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin pH 8.0, 30°C Cavia porcellus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.13 6.5
-
inhibition assay at Cavia porcellus
2.3.2.13 8
-
activity assay at Cavia porcellus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.2.13 additional information
-
additional information inhibition kinetics, irreversible enzyme inactivation usually results in steady-state rates that are equal to zero independent of inhibitor concentration Cavia porcellus
2.3.2.13 0.00573
-
N-[(5S)-6-[4-(6-methylpyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide pH 6.5, 30°C, with/versus substrate Z-Glu(HMC)-Gly-OH Cavia porcellus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.2.13 48.5
-
Z-Glu(HMC)-Gly-OH pH 8.0, 30°C Cavia porcellus
2.3.2.13 130.4
-
Z-Glu(HC)-Gly-OH pH 8.0, 30°C Cavia porcellus
2.3.2.13 204.1
-
Z-Phe-gamma-Abu-7-hydroxycoumarin pH 8.0, 30°C Cavia porcellus
2.3.2.13 456.1
-
Z-Phe-gamma-Abu-7-hydroxy-4-methylcoumarin pH 8.0, 30°C Cavia porcellus