Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EDTA | complete inhibition at 10 mM | Cavia porcellus | |
EDTA | complete inhibition at 10 mM | Pacifastacus leniusculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics, comparison to the kinetics of commercial enzyme from guinea pig liver | Pacifastacus leniusculus | |
additional information | - |
additional information | kinetics, comparison to the kinetics of commercial enzyme from guinea pig liver | Cavia porcellus | |
0.00288 | - |
pentylamine | pH 8.5, 4°C | Pacifastacus leniusculus | |
0.0029 | - |
pentylamine | pH 8.5, 22°C | Pacifastacus leniusculus | |
0.0203 | - |
pentylamine | pH 8.5, 22°C | Cavia porcellus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Pacifastacus leniusculus | |
Ca2+ | dependent on | Cavia porcellus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein glutamine + alkylamine | Pacifastacus leniusculus | - |
protein N5-alkylglutamine + NH3 | - |
? | |
protein glutamine + alkylamine | Cavia porcellus | - |
protein N5-alkylglutamine + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cavia porcellus | A0A286XL02 | - |
- |
Pacifastacus leniusculus | Q964D3 | from from Lake Erken, Schweden | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Cavia porcellus | - |
hematopoietic cell | - |
Pacifastacus leniusculus | - |
liver | - |
Cavia porcellus | - |
additional information | signal crayfish is a 60 long-lived species and its natural habitat, fresh waters usually have a wide range of temperatures from below 7°C during winter and up to more than 20°C in summer | Pacifastacus leniusculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
casein glutamine + pentylamine | the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure | Pacifastacus leniusculus | casein N5-pentylglutamine + NH3 | - |
? | |
casein glutamine + pentylamine | the enzymatic activity of TGase is determined by measuring the fluorescence of MDC cross-linking to N,N'-dimethyl casein upon exposure | Cavia porcellus | casein N5-pentylglutamine + NH3 | - |
? | |
protein glutamine + alkylamine | - |
Pacifastacus leniusculus | protein N5-alkylglutamine + NH3 | - |
? | |
protein glutamine + alkylamine | - |
Cavia porcellus | protein N5-alkylglutamine + NH3 | - |
? | |
protein glutamine + alkylamine | transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates | Pacifastacus leniusculus | protein N5-alkylglutamine + NH3 | - |
? | |
protein glutamine + alkylamine | transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl)lysine bonds between appropriate substrates | Cavia porcellus | protein N5-alkylglutamine + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cold-active transglutaminase | - |
Pacifastacus leniusculus |
TGase | - |
Pacifastacus leniusculus |
TGase 1 | - |
Cavia porcellus |
transglutaminase | - |
Pacifastacus leniusculus |
transglutaminase 1 | - |
Cavia porcellus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Pacifastacus leniusculus |
22 | - |
assay at room temperature | Cavia porcellus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
4 | 37 | the guinea pig liver enzyme shows very low activity at 4°C and high activity at 37°C | Cavia porcellus |
4 | 22 | at 4°C, crayfish TGase shows high activity due to a decreasing Km value for pentylamine as a substrate, the kcat value is not affected at 22°C | Pacifastacus leniusculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0065 | - |
pentylamine | pH 8.5, 4°C | Pacifastacus leniusculus | |
0.0096 | - |
pentylamine | pH 8.5, 22°C | Pacifastacus leniusculus | |
0.064 | - |
pentylamine | pH 8.5, 22°C | Cavia porcellus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
- |
Pacifastacus leniusculus |
8.5 | - |
- |
Cavia porcellus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
2 | 10 | activity range, low activity at pH 2.0, high activity at pH 7.4-8.5, maximal activity at pH 8.5, 60% of maximal activity at pH 10.0, profile overview | Pacifastacus leniusculus |
2 | 10 | activity range, low activity at pH 2.0, high activity at pH 7.4-8.5, maximal activity at pH 8.5, 60% of maximal activity at pH 10.0, profile overview | Cavia porcellus |
General Information | Comment | Organism |
---|---|---|
evolution | crayfish TGase is adapted to have significant activity at low temperatures since crayfish are living in quite cold waters | Pacifastacus leniusculus |
additional information | comparison of the crayfish enzyme to the commercial enzyme from guinea pig liver, which is highly active at 37°C | Pacifastacus leniusculus |
additional information | comparison of the crayfish enzyme, which is highly active at 4°C, to the commercial enzyme from guinea pig liver | Cavia porcellus |
physiological function | transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl) lysine bonds between appropriate substrates. This reaction is essential for physiological cell functions, such as in blood coagulation, during cell differentiation and survival, skin formation, and signal transduction | Pacifastacus leniusculus |
physiological function | transglutaminases (TGases) catalyze a Ca2+-dependent acyl transfer reaction between the epsilon-amino group of lysine (acyl acceptors) and gamma-carboxamide groups of glutamine residues (acyl donors) and forms cross-links by catalyzing the isopeptide bond formation between Lys and Gln residues to form epsilon-(gamma-glutamyl) lysine bonds between appropriate substrates. This reaction is essential for physiological cell functions, such as in blood coagulation, during cell differentiation and survival, skin formation, and signal transduction | Cavia porcellus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.26 | - |
pentylamine | pH 8.5, 4°C | Pacifastacus leniusculus | |
3.15 | - |
pentylamine | pH 8.5, 22°C | Cavia porcellus | |
3.31 | - |
pentylamine | pH 8.5, 22°C | Pacifastacus leniusculus |