Mechanistic insight into the elastin degradation process by the metalloprotease myroilysin from the deep-sea bacterium Myroides profundi D25.

ABSTRACT: Elastases have been widely studied because of their important uses as medicine and meat tenderizers. However, there are relatively few studies on marine elastases. Myroilysin, secreted by Myroides profundi D25 from deep-sea sediment, is a novel elastase. In this study, we examined the elastin degradation mechanism of myroilysin. When mixed with insoluble bovine elastin, myroilysin bound hydrophobically, suggesting that this elastase may interact with the hydrophobic domains of elastin. Consistent with this, analysis of the cleavage pattern of myroilysin on bovine elastin and recombinant tropoelastin revealed that myroilysin preferentially cleaves peptide bonds with hydrophobic residues at the P1 and/or P1' positions. Scanning electron microscopy (SEM) of cross-linked recombinant tropoelast

SUBMITTER: Yang J 

PROVIDER: S-EPMC4377995 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature