The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity.
Vibrio and Aeromonas spp. secrete an unusual 35-kDa lipase that shares several properties with mammalian lecithin-cholesterol acyltransferase. The Aeromonas hydrophila lipase contains two cysteine residues that form an intramolecular disulfide bridge. Here we show that changing either of the cystein...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | J Bacteriol |
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| Κύριοι συγγραφείς: | , , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
American Society for Microbiology (ASM)
1997
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC179086/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9150203/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.179.10.3116-3121.1997 |
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