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Literature summary for 2.3.2.13 extracted from
- Characterisation of a novel cold-adapted calcium-activated transglutaminase implications for medicine and food processing (2020), FEBS Open Bio, 10, 495-506 .
Application
| Application | Comment | Organism |
|---|---|---|
| food industry | potential application of AcTG-1 as a biological cross-linker in the food industry, once binding occurs, fish fillets withstand further processing such as frying, boiling, freeze-thawing and chilling. The low-temperature activity and enzymatic properties of AcTG-1 appear to offer advantages over commercially available enzymatic glues in the food industry, overview | Gadus morhua |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| full-length gene is cloned from the head kidney by RT-PCR and rapid amplification of cDNA ends, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged soluble enzyme in Escherichia coli upon induction at low temperature. The recombinant AcTG-1 is not altered by proteolytic degradation | Gadus morhua |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | complete inhibition | Gadus morhua |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | absolutely required, several calcium-binding sites in the enzyme are identified, Asn392, Asp394, Glu441, making the enzyme an appropriate model for studying structure-function relationships in the calcium-dependent transglutaminase family | Gadus morhua | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein glutamine + alkylamine | Gadus morhua | - |
casein N5-alkylglutamine + NH3 | - |
? | |
| collagen glutamine + alkylamine | Gadus morhua | - |
collagen N5-alkylglutamine + NH3 | - |
? | |
| gelatin glutamine + alkylamine | Gadus morhua | - |
gelatin N5-alkylglutamine + NH3 | - |
? | |
| protein glutamine + alkylamine | Gadus morhua | - |
protein N5-alkylglutamine + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gadus morhua | V9I378 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged soluble enzyme from Escherichia coli by nickel affinity chromatography, the tag is cleaved off by TEV protease followed by ultrafiltration | Gadus morhua |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein glutamine + alkylamine | - |
Gadus morhua | casein N5-alkylglutamine + NH3 | - |
? | |
| collagen glutamine + alkylamine | - |
Gadus morhua | collagen N5-alkylglutamine + NH3 | - |
? | |
| gelatin glutamine + alkylamine | - |
Gadus morhua | gelatin N5-alkylglutamine + NH3 | - |
? | |
| additional information | the recombinant transglutaminase crosslinks casein, collagen and gelatin | Gadus morhua | ? | - |
- |
|
| N,N'-dimethyl casein glutamine + monodansylcadaverine | the enzymatic activity of AcTG-1 is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein upon exposure | Gadus morhua | ? | - |
? | |
| protein glutamine + alkylamine | - |
Gadus morhua | protein N5-alkylglutamine + NH3 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 80000, recombinant detagged enzyme, SDS-PAGE | Gadus morhua |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AcTG-1 | - |
Gadus morhua |
| transglutaminase | - |
Gadus morhua |
| transglutaminase 1 | - |
Gadus morhua |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
recombinant enzyme | Gadus morhua |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
65 | the transglutaminase is active between 0 and 65°C, but is completely inactivated after 20 min at 70°C. The enzyme displays cold-adapted features, such as temperature instability combined with high catalytic efficiency at low temperatures (8-16°C), and optimal activity at 50°C | Gadus morhua |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
20 | purified recombinant AcTG-1 is stable up to a temperature of 20°C. Above 20°C, AcTG-1 starts to lose activity and is completely inactivated at 70°C | Gadus morhua |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
recombinant enzyme | Gadus morhua |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 10 | activity range at 16°C, recombinant enzyme | Gadus morhua |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Gadus morhua | identification of a cold-adapted calcium-activated transglutaminase | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | transglutaminases form extensively crosslinked, generally insoluble protein polymers. These structures are important for organisms in the formation of skin barrier, hair growth, wound healing and blood clotting. Transglutaminases are a family of enzymes that catalyse the cross-linking of proteins by forming covalent bonds between glutamine (Q) and lysine (K) residues in different polypeptides. Such isopeptide bonds created by TG are highly resistant to proteolysis and increase the mechanical stability of the modified proteins | Gadus morhua |
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