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Literature summary for 2.3.2.13 extracted from

  • Pfleiderer, C.; Mainusch, M.; Weber, J.; Hils, M.; Fuchsbauer, H.L.
    Inhibition of bacterial transglutaminase by its heat-treated pro-enzyme (2005), Microbiol. Res., 160, 265-271.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information enzyme precursor protein is inhibitory to mature enzyme, even after heat treatment. Precursor is secreted to culture medium; heat-treated pro-enzyme acts effectively as inhibitor of mature form Streptomyces mobaraensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42500
-
x * 45000, SDS-PAGE, x * 42500, calculated Streptomyces mobaraensis
42500
-
x * 45000, SDS-PAGE of pro-enzyme, x * 42500, caculated Streptomyces mobaraensis
45000
-
x * 45000, SDS-PAGE, x * 42500, calculated Streptomyces mobaraensis
45000
-
x * 45000, SDS-PAGE of pro-enzyme, x * 42500, caculated Streptomyces mobaraensis

Organism

Organism UniProt Comment Textmining
Streptomyces mobaraensis
-
-
-
Streptomyces mobaraensis
-
expression in Escherichia coli
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification pro-enzyme acts effectively as inhibitor of mature form Streptomyces mobaraensis
proteolytic modification enzyme precursor protein is inhibitory to mature enzyme, even after heat treatment. Precursor is secreted to culture medium Streptomyces mobaraensis

Source Tissue

Source Tissue Comment Organism Textmining
culture medium
-
Streptomyces mobaraensis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N,N-dimethyl-1,4-phenylenediamine + Cbz-Gln-Gly
-
Streptomyces mobaraensis ?
-
?

Subunits

Subunits Comment Organism
? x * 45000, SDS-PAGE, x * 42500, calculated Streptomyces mobaraensis
? x * 45000, SDS-PAGE of pro-enzyme, x * 42500, caculated Streptomyces mobaraensis