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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...
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| Huvudupphovsmän: | , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1997
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC179086/ https://ncbi.nlm.nih.gov/pubmed/9150203 |
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