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Literature summary extracted from

  • Deweid, L.; Avrutina, O.; Kolmar, H.
    Microbial transglutaminase for biotechnological and biomedical engineering (2019), Biol. Chem., 400, 257-274 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.2.13 biotechnology the microbial transglutaminase is used for biotechnological and biomedical engineering, protein engineering by post-translational modification towards the generation of multifunctional conjugates. Biotechnological applications, detailed overview. Transglutaminase-mediated surface immobilization, a widely-used technique to increase stability of labile and cost-intensive enzymes and enable their reuse Streptomyces mobaraensis
2.3.2.13 medicine the microbial transglutaminase is used for biotechnological and biomedical engineering, protein engineering by post-translational modification towards the generation of multifunctional conjugates. Biotechnological applications, detailed overview. Construction of protein-polymer and of antibody-drug conjugations for pharmaceutical applications Streptomyces mobaraensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.2.13 crystal structure analysis, PDB ID 4P8I Bacillus subtilis
2.3.2.13 crystal structure analysis, PDB ID 5M6Q Kutzneria albida
2.3.2.13 crystal structure analysis, PDB IDs 3IU0 and 1IU4 Streptomyces mobaraensis

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.13 additional information peptidyl-linker sequences used that facilitate modification by microbial transglutaminase, overview Streptomyces mobaraensis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.13 cytoplasm immature pro-enzyme Streptomyces mobaraensis 5737
-
2.3.2.13 extracellular the immature enzyme is secreted, and extracellulary, the zymogen is processed by an endogenous metalloprotease called TGase-activating protease (TAMEP) and a tripeptidyl aminopeptidase (SM-TAP) Streptomyces mobaraensis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.13 Ca2+ required Streptomyces mobaraensis
2.3.2.13 Ca2+ required Kutzneria albida
2.3.2.13 Ca2+ required Bacillus subtilis

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 Streptomyces mobaraensis
-
 protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine Kutzneria albida
-
 protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine Bacillus subtilis
-
 protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine Bacillus subtilis 168
-
 protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine Kutzneria albida DSM 43870
-
 protein N5-alkylglutamine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Bacillus subtilis P40746
-
-
2.3.2.13 Bacillus subtilis 168 P40746
-
-
2.3.2.13 Kutzneria albida W5WHY8
-
-
2.3.2.13 Kutzneria albida DSM 43870 W5WHY8
-
-
2.3.2.13 Streptomyces mobaraensis P81453
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.13 proteolytic modification the immature enzyme is secreted, and extracellulary, the zymogen is processed by an endogenous metalloprotease called TGase-activating protease (TAMEP) and a tripeptidyl aminopeptidase (SM-TAP). SM-TAP procession is not essential for activity as TAMEP-treated and fully processed zymogen exhibits similar catalytic activity Streptomyces mobaraensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 additional information SM-TAP procession of the pro-form zymogen is not essential for activity as TAMEP-treated and fully processed enzyme and the zymogen exhibit similar catalytic activity Streptomyces mobaraensis ?
-
-
2.3.2.13 protein glutamine + alkylamine
-
 Streptomyces mobaraensis protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Kutzneria albida protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Bacillus subtilis protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Bacillus subtilis 168 protein N5-alkylglutamine + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Kutzneria albida DSM 43870 protein N5-alkylglutamine + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.13 ? x * 28000 Bacillus subtilis
2.3.2.13 ? x * 26400 Kutzneria albida
2.3.2.13 monomer 1 * 37900, mature enzyme, 1 * 42500, enzyme pro-form Streptomyces mobaraensis

Synonyms

EC Number Synonyms Comment Organism
2.3.2.13 KALB
-
 Kutzneria albida
2.3.2.13 KALB_7456
-
 Kutzneria albida
2.3.2.13 microbial transglutaminase
-
 Streptomyces mobaraensis
2.3.2.13 microbial transglutaminase
-
 Kutzneria albida
2.3.2.13 microbial transglutaminase
-
 Bacillus subtilis
2.3.2.13 TGL
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.13 50
-
-
 Streptomyces mobaraensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.13 6 7
-
 Streptomyces mobaraensis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.3.2.13 Streptomyces mobaraensis
-
-
 8

General Information

EC Number General Information Comment Organism
2.3.2.13 additional information mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview Streptomyces mobaraensis
2.3.2.13 additional information mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview Kutzneria albida
2.3.2.13 additional information mechanism of mTG-catalyzed isopeptide bond formation between protein-bound glutamine and lysine residues. Structure-function analysis, substrate specificity, overview Bacillus subtilis