| Identification | Back Directory | [Name]
EC 2.3.2.13 | [CAS]
80146-85-6 | [Synonyms]
akuthibatg
EC 2.3.2.13
akuthibatg-k
TRANSGLUTAMINASE
transglutaminasec
FACTOR XIII-A, HUMAN
tissuetransglutaminase
polyaminetransglutaminase
transglutaminase from guinea pig liver
protein-glutamine-γ-glutamyltransferase
GlutaMyltransferase,glutaMinylpeptide-
glutaminylpeptidegamma-glutamyltransferas
glutaminylpeptidegammaglutamyltransferase
Glutamyltransferase, glutaminylpeptide .gamma.-
PROTEIN-GLUTAMINE: AMINE GAMMA-GLUTAMYLTRANSFERASE
Protein-Glutamine-γ-Glutamyltransferase, Protein-glutamine:amine γ-glutamyltransferase | [EINECS(EC#)]
232-554-6 | [Molecular Formula]
C27H44O3H2O | [MDL Number]
MFCD00132446 |
| Chemical Properties | Back Directory | [storage temp. ]
−20°C
| [solubility ]
H2O: soluble1.0mg/mL, clear | [form ]
lyophilized powder
| [color ]
White to yellow | [Uses]
transglutaminase is an enzyme said to activate the skin’s physiological functions. |
| Hazard Information | Back Directory | [Biochem/physiol Actions]
Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptides. Liver transglutaminase is a nonzymogenic enzyme. |
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