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Literature summary extracted from

  • St-Jacques, A.; Rachel, N.; Curry, D.; Gillet, S.; Clouthier, C.; Keillor, J.; Pelletier, J.; Chica, R.
    Specificity of transglutaminase-catalyzed peptide synthesis (2016), J. Mol. Catal. B, 123, 53-61 .
No PubMed abstract available

Application

EC Number Application Comment Organism
2.3.2.13 synthesis the enzyme can be a useful biocatalyst for the synthesis of desirable bioactive molecules Cavia porcellus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.13 recombinant overexpression of His-tagged isozyme TG2 in Escherichia coli Cavia porcellus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.13 additional information
-
 additional information kinetics Cavia porcellus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.13 Ca2+ dependent on Cavia porcellus

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 Cavia porcellus
-
 protein N5-alkylglutamine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Cavia porcellus H0VXN6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.13 recombinant His-tagged isozyme TG2 from Escherichia coli by nickel affinity chromatography and ultrafiltration Cavia porcellus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.2.13 protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 the catalytic reaction follows a modified ping-pong mechanism in which a glutamine-containing protein or peptide, the acyl-donor substrate, reacts with the catalytic cysteine residue to form a thioester bond. The resulting covalent acyl-enzyme intermediate then reacts with a second substrate, the acyl-acceptor, to yield the isopeptide-containing product and free enzyme in a transamidation reaction. Substrate specificity of the enzyme, detailed overview Cavia porcellus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.13 liver
-
 Cavia porcellus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 CBZ-D-Ala-coumarin-7-yl ester + hydroxylamine
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-Gly-coumarin-7-yl ester + hydroxylamine
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-Gly-GABA-coumarin-7-yl ester + hydroxylamine
-
 Cavia porcellus 7-hydroxycoumarin + ?
-
 ?
2.3.2.13 CBZ-Gly-NH2 + AlaNH2
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-Gly-NH2 + GlyNH2
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-Gly-NH2 + L-leucine methyl ester
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-L-Ala-coumarin-7-yl ester + hydroxylamine
-
 Cavia porcellus ?
-
 ?
2.3.2.13 CBZ-Phe-GABA-coumarin-7-yl ester + hydroxylamine
-
 Cavia porcellus 7-hydroxycoumarin + ?
-
 ?
2.3.2.13 additional information wild-type TG2 can catalyze synthesis of CBZ-protected dipeptides. Its donor substrate specificity is narrow, aromatic ester derivatives of Gly and D-Ala serve as donor substrates. A hydrophobic cavity formed by Trp332 and Phe334 dictates substrate specificity. TG2 enzymes exhibit broad specificity towards the acyl-acceptor substrate. Guinea pig liver transglutaminase (gTG2) catalyzes the cross-linking of peptides and proteins via the formation of gamma-glutamyl-epsilon-lysyl isopeptide bonds. gTG2-catalyzed peptide bond formation between various amino acid-derived donor and acceptor substrates is analyzed. gTG2 forms Gly-Xaa and D-Ala-Gly dipeptide products, confirming that the enzyme's natural transamidation activity can be co-opted for peptide synthesis, LC-MS analysis. An aromatic ester of Gly is the most efficient acyl-donor substrate tested, aromatic esters of D-Ala and L-Ala show 50fold lower reactivity or no reactivity, respectively. The native acyl-acceptor substrate is generally a lysine-containing protein or peptide, many nonnatural primary amines, such as glycinamide, and anilines, such as N,N-dimethyl-1,4-phenylenediamine, can also react. TG2 displays narrow specificity for its acyl-donor substrates. The side chain of a protein or peptide-bound L-Gln residue is the native substrate while the side chain of the similar amino acid L-Asn is not reactive. In addition to amides, gamma-glutamyl aromatic ester derivatives of L-Glu, such as Ncarbobenzyloxy-L-glutamyl(gamma-p-nitrophenyl ester)glycine, have also been shown to be acyl-donor substrates of TG2 and are used to measure the enzyme's activity. N-Carbobenzyloxyglycyl-coumarin-7-yl ester (CBZ-Gly-7HC), is also a donor substrate of TG2. Construction of acyl-enzyme intermediates, structure analysis, and structural basis, overview Cavia porcellus ?
-
-
2.3.2.13 N-CBZ-Glu-Gly + hydroxylamine
-
 Cavia porcellus CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Cavia porcellus protein N5-alkylglutamine + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.13 gTG2
-
 Cavia porcellus
2.3.2.13 TG2
-
 Cavia porcellus
2.3.2.13 transglutaminase
-
 Cavia porcellus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.13 37
-
 assay at Cavia porcellus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.13 7
-
 assay at Cavia porcellus

General Information

EC Number General Information Comment Organism
2.3.2.13 additional information molecular dynamics simulations are developed to model the binding modes of donor substrates in the gTG2 active site. The inability of gTG2 to efficiently catalyze peptide synthesis from donors containing alanine results from the narrow substrate binding tunnel, which prevents bulkier donors from adopting a catalytically productive binding mode. Molecular homology modeling of TG2 using the structure of inhibitor-complexed human enzyme as template (PDB ID: 2Q3Z). Donor substrate specificity of gTG2-catalyzed peptide synthesis, overview Cavia porcellus
2.3.2.13 physiological function tissue transglutaminase (TG2) catalyzes the Ca2+-dependent cross-linking of peptides and proteins via the formation of gamma-glutamyl-epsilon-lysyl isopeptide bonds Cavia porcellus