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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Vydáno v:	J Bacteriol
Hlavní autoři:	Brumlik, M J, van der Goot, F G, Wong, K R, Buckley, J T
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1997
Témata:	Research Article
On-line přístup:	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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