Inhibition of bacterial transglutaminase by its heat-treated pro-enzyme

Transglutaminases form a unique family of cross-linking enzymes which may be interesting for pharmaceutical and technical purposes. Bacterial transglutaminase, differing from the eucaryotic counterparts in being independent from Ca 2+ ions, is excreted by several Streptomyces species. Until now an e...

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Bibliographic Details
Published in:Microbiological research 2005-01, Vol.160 (3), p.265-271
Main Authors: Pfleiderer, Christa, Mainusch, Martina, Weber, Johannes, Hils, Martin, Fuchsbauer, Hans-Lothar
Format: Article
Language:English
Subjects:
Culture Media
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - isolation & purification
Enzyme Inhibitors - metabolism
Enzyme Precursors - metabolism
Enzyme Stability
Hot Temperature
Pro-transglutaminase
Recombinant Proteins
Streptomyces - enzymology
Streptomyces mobaraensis
Transglutaminase
Transglutaminase inhibitor
Transglutaminases - antagonists & inhibitors
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Summary:Transglutaminases form a unique family of cross-linking enzymes which may be interesting for pharmaceutical and technical purposes. Bacterial transglutaminase, differing from the eucaryotic counterparts in being independent from Ca 2+ ions, is excreted by several Streptomyces species. Until now an endogenous factor regulating activated transglutaminase could not be detected. Here, we investigated whether an inhibitor of transglutaminase is excreted into the culture fluid of Streptomyces mobaraensis. We could demonstrate that heat-resistant inhibitory activity is produced after 24 h of growth reaching a maximum after 72 h. A two-step ion exchange chromatography purification procedure revealed co-elution of the heat-treated inhibitor with pro-transglutaminase. Experiments with wild-type and recombinant pro-transglutaminase confirmed that the precursor protein indeed inhibits the activity of the mature enzyme.
ISSN:0944-5013
1618-0623
DOI:10.1016/j.micres.2005.01.001