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Literature summary for 2.3.2.13 extracted from
- Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus (2018), Fish Shellfish Immunol., 80, 546-549 .
Inhibitors
| 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 [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
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | dependent on | Pacifastacus leniusculus | |
| Ca2+ | dependent on | Cavia porcellus | |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cavia porcellus | A0A286XL02 | - |
- |
| Pacifastacus leniusculus | Q964D3 | from from Lake Erken, Schweden | - |
Source Tissue
| 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 and Products (Substrate)
| 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
| 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 [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Pacifastacus leniusculus |
| 22 | - |
assay at room temperature | Cavia porcellus |
Temperature Range [°C]
| 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 [1/s]
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
- |
Pacifastacus leniusculus |
| 8.5 | - |
- |
Cavia porcellus |
pH Range
| 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
| 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 [mM/s]
| 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 | |
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