Any feedback?
Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase
for references in articles please use BRENDA:EC2.3.2.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.2.13 protein-glutamine gamma-glutamyltransferaseIUBMB Comments
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
Specify your search results
Word Map
- 2.3.2.13
- celiac
- coagulation
- clot
- fibrinogen
-
crosslinking
- gluten
-
serological
- bleeding
- thrombin
- autoimmune
- children
- autoantibody
- platelet
-
gluten-free
- keratinocytes
-
anti-tissue
- gliadin
- collagen
- duodenal
- igg
- bowel
-
deamidated
- fibronectin
-
villous
- keratin
-
fibrinolysis
- plasminogen
-
isopeptide
- involucrin
- enteropathy
- prothrombin
-
cornified
- plasmin
-
hemostatic
-
endoscopy
-
marsh
-
gelation
-
texture
- ichthyosis
-
fibrinopeptide
-
cryoprecipitate
-
gastroenterology
-
rheological
- leiden
-
malabsorption
- filaggrin
- nutrition
- analysis
- agriculture
- diagnostics
-
antifibrinolytic
- medicine
- synthesis
- food industry
- biotechnology
- histiocytomas
-
sealant
-
2-antiplasmin
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transglutaminase, factor xiii, tissue transglutaminase, tgase, factor xiiia, transglutaminase 2, microbial transglutaminase, mtgase, tgase 2, protein 4.2, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
ping-pong mechanism
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
liver transglutaminase, Q155 and Q159 are putative sites in bovine beta-lactoglobulin that incorporate putrescine
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism and structure
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
putative incorporation site of putrescine in beta-casein
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
modified double displacement mechanism i.e. modified ping pong reaction
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
complex kinetic mechanism with substrate Z-Gln-Gly involving Gln hydrolysis, intramolecular transpeptidation, intermolecular transpeptidation, transamidation by added nucleophile
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism of regulation by guanine nucleotides and Ca2+/Mg2+, GTPase cycle
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
mechanism, Ca2+ binding in both sites two and three cooperate in opening a channel through the enzyme
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
model for binding and reaction of small peptide substrates, via Michaelis-complex
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
the first step in both types of modifications is the acylation of the active site cysteine (Cys277) of TG2 by a protein-bound glutamine residue, resulting in the liberation of ammonia and the formation of a thioester intermediate between TG2 and the glutamine bearing protein substrate. In TG2 catalyzed transamidation, the thioester intermediate is attacked by a nucleophilic primary amine, either a small molecule amine such as putrescine or the epsilon-amino group of protein-bound lysine residues. This results in the formation of relatively stable isopeptide bonds
-
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
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
ping-pong mechanism
-
-
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
-
-
-
-