The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine donor substrate of the intrinsic transglutaminase.
Transglutaminase (TGase) from Streptomyces mobaraensis is an extra-cellular enzyme that cross-links proteins to high molecular weight aggregates. Screening for intrinsic substrates now revealed the dual Streptomyces subtilisin inhibitor-like inhibitor Streptomyces subtilisin and transglutaminase activating metalloprotease (TAMEP) inhibitor (SSTI), equally directed against subtilisin and the TGase activating metalloprotease TAMEP, is both a glutamine and a lysine donor protein. Reactivity of glutamines is lost during culture, most likely by TGase mediated deamidation, and, accordingly, cross-linking only occurred if SSTI from early cultures was used. Interestingly, release of buried endo-glutamines by the lipoamino acid N-lauroylsarcosine could restore SSTI reactivity. Formation of lipoamino acids by Streptomycetes suggests such compounds could also modulate in vivo TGase mediated SSTI cross-linking.
Schmidt
Susan
S
Department of Chemical Engineering and Biotechnology, University for Applied Sciences of Darmstadt, Schnittspahnstrasse 12, D-64287 Darmstadt, Germany.
Adolf
Frank
F
Fuchsbauer
Hans-Lothar
HL
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D045726:Metalloproteases / Q000037:antagonists & inhibitors / Q000378:metabolism; D012521:Sarcosine / Q000031:analogs & derivatives / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity; D011503:Transglutaminases / Q000378:metabolism*
D001426:Bacterial Proteins; C018150:subtilisin inhibitor protein, Streptomyces; D005973:Glutamine; C025231:sarkosyl; D011503:Transglutaminases; D045726:Metalloproteases; D008239:Lysine; D012521:Sarcosine