transglutaminases
Also known as transglutaminase, protein-glutamine gamma-glutamyltransferase, fibrinoligase, glutaminylpeptide gamma-glutamyltransferase, protein-glutamine:amine gamma-glutamyltransferase, R-glutaminyl-peptide:amine gamma-glutamyl transferase
Transglutaminases are enzymes that in nature primarily catalyze the formation of an isopeptide bond between γ-carboxamide groups ( -(C=O)NH2 ) of glutamine residue side chains and the ε-amino groups ( -NH2 ) of lysine residue side chains with subsequent release of ammonia ( NH3 ). Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). The rea
Key facts
- Enzyme.name
- Transglutaminase
- Enzyme.image
- Coagulation factor XIII 1EVU.png
- Enzyme.caption
- Transglutaminase example: coagulation factor XIII from human blood. PDB code: 1EVU.
- Enzyme.EC_number
- 2.3.2.13
- Enzyme.CAS_number
- 80146-85-6
- Protein family.Name
- Transglutaminase, bacterial
- Protein family.Pfam
- PF09017
- Protein family.Symbol
- Transglut_prok
- Protein family.InterPro
- IPR015107
- Protein family.CATH
- 3iu0
- Protein family.SCOP
- 1iu4
- Protein family.SMART
- SM00460
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Article
10 sectionsContents
- Examples
- Biological role
- Role in disease
- Structural studies
- Industrial and culinary applications
- Molecular gastronomy
- Synonyms
- See also
- References
- Further reading
Transglutaminases are enzymes that in nature primarily catalyze the formation of an isopeptide bond between γ-carboxamide groups ( -(C=O)NH2 ) of glutamine residue side chains and the ε-amino groups ( -NH2 ) of lysine residue side chains with subsequent release of ammonia ( NH3 ). Lysine and glutamine residues must be bound to a peptide or a protein so that this cross-linking (between separate molecules) or intramolecular (within the same molecule) reaction can happen. Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). The reaction is Gln-(C=O)NH2 + NH2-Lys → Gln-(C=O)NH-Lys + NH3 Transglutaminases can also join a primary amine ( RNH2 ) to the side chain carboxyamide group of a protein/peptide bound glutamine residue thus forming an isopeptide bond Gln-(C=O)NH2 + RNH2 → Gln-(C=O)NHR + NH3
These enzymes can also deamidate glutamine residues to glutamic acid residues in the presence of water Gln-(C=O)NH2 + H2O → Gln-COOH + NH3 Transglutaminase isolated from Streptomyces mobaraensis -bacteria for example, is a calcium-independent enzyme. Mammalian transglutaminases among other transglutaminases require Ca2+ ions as a cofactor.