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Literature summary for 2.3.2.13 extracted from
- Bioengineering of microbial transglutaminase for biomedical applications (2019), Appl. Microbiol. Biotechnol., 103, 2973-2984 .
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | developments in mTGase engineering together with its role in biomedical applications including biomaterial fabrication for tissue engineering and biotherapeutics, overview | Streptomyces mobaraensis |
| food industry | the enzyme is widely exploited in the meat processing industries. Enzyme mTGase is also widely applied in other food and textile industries by catalysing the formation of isopeptide bonds between peptides or protein substrates | Streptomyces mobaraensis |
| medicine | developments in mTGase engineering together with its role in biomedical applications including biomaterial fabrication for tissue engineering and biotherapeutics, biomedical engineering, overview | Streptomyces mobaraensis |
| synthesis | the enzyme is used for biomaterial fabrication for tissue engineering, e.g. from gelatin, evaluation, overview | Streptomyces mobaraensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | development of enzyme engineering to improve, alter, or customise the functional properties of mTGase, e.g. thermoengineering for better heat stability and heat sensitivity, overview. The N-termius of mTGase is an important region that influences the thermal properties of the enzyme due to the fact that all single-point mutations related to the altered thermal properties are located in this area, random mutagenesis. Semirational mutagenesis is also successful to isolate mTGase variants with increased thermostabilities. Seven hot spot residues, which are reported to be the thermostabilizing sites, are mutated for the generation of mutant libraries to screen for thermostable variants. Later, variants with single amino acid substitution comprising of the highest thermostabilities are mixed by DNA shuffling to generate a secondary library for screening. Finally, the variants with improved thermostabilities are isolated via standard assay. For production of soluble enzyme, introduction of a fusion partner with the extension of the N-terminal region to contain few LacZ residues followed by the first 20 residues of enzyme purine nucleoside phosphorylase is done. This strategy results in the accumulation of high levels of mTGase in the cytoplasm. The thermoinducible expression system yields a lower protein yield but produces the enzyme with a higher specificity as no major modification is done to the enzyme making it preferable compared to constitutive expression system | Streptomyces mobaraensis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protein glutamine + alkylamine | Streptomyces mobaraensis | - |
protein N5-alkylglutamine + NH3 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces mobaraensis | P81453 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme also catalyzes the deamination of amines. Glutamine is recognised as the acyl donor substrate by TGases due to the gamma-carboxyamide group. N-Benzyloxycarbonyl-L-glutaminylglycine (CBZ-Gln-Gly) is the standard glutamine peptide substrate used for TGases. Acyl acceptor substrates and acyl donor substrates, overview. The mTGase enzyme was reported to recognise L-isomer of lysine slightly more than its D-isomer when incorporated into a Z-Gln-Gly motif | Streptomyces mobaraensis | ? | - |
- |
|
| protein glutamine + alkylamine | - |
Streptomyces mobaraensis | protein N5-alkylglutamine + NH3 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| microbial transglutaminase | - |
Streptomyces mobaraensis |
| MTGase | - |
Streptomyces mobaraensis |
| transglutaminase | - |
Streptomyces mobaraensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the removal of the pro-sequence region using proteases results in the active site of the mature enzyme to be revealed to initiate the reaction | Streptomyces mobaraensis |
| additional information | mTGase structure-function relationship, overview. The active site is a single cysteine (C64) residing at the bottom cleft of the crystal structure (PDB ID 3IU0) where it forms a catalytic triad with the aspartic acid (D255) and histidine (H274) residues. The pro-sequence region is vital for enzyme folding and inhibition of enzyme activation within the cells to avoid detrimental cross-linking of cytosolic proteins. The enzyme structure has a wide active site cleft position that accommodates the alpha-helix pro-sequence. This unique attribute explains the broad substrate specificity for acyl donors which allows for additional flexibility in the active site to accommodate a less specific substrate, overview | Streptomyces mobaraensis |
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