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Literature summary for 2.3.2.13 extracted from

  • Seitz, J.; Keppler, C.; Huntemann, S.; Rausch, U.; Aumuller, G.
    Purification and molecular characterization of a secretory transglutaminase from coagulating gland of the rat (1991), Biochim. Biophys. Acta, 1078, 139-146.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inactivation above 10 mM Rattus norvegicus
additional information transglutaminase of coagulating gland, not inhibited by GTP Rattus norvegicus
NH4+ complete inhibition of coagulating gland transglutaminase with more than 1 mM NH4Cl or 20 mM (NH4)2SO4 Rattus norvegicus
Sodium citrate above 10 mM, complete inactivation Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ requirement Rattus norvegicus
Ca2+ 0.5 mM, maximum activity of transglutaminase from coagulating gland Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65000
-
transglutaminase C, gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
mature male Wistar
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein coagulating gland transglutaminase, glycosylated with mannosyl-residues, no terminal position, substituted with saturated acyl residues and phosphoinositol Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
coagulating gland secretion, not immunologically related to tissue-type enzyme or blood factor XIIIa Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
putrescine + N,N'-dimethylcasein
-
Rattus norvegicus ?
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pI: 8.5-8.7, purified enzyme Rattus norvegicus
additional information
-
pI: 7.6, crude enzyme Rattus norvegicus