A new family of lipolytic enzymes?
Aeromonas sp. produce a lipolytic enzyme that also has the ability to carry out acyl transfer to alcohol acceptors in aqueous media. The fact that there is only one glycine in this sequence indicates that the structure of the active site is likely to differ from those with solved three-dimensional s...
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Veröffentlicht in: | Trends in biochemical sciences (Amsterdam. Regular ed.) 1995-05, Vol.20 (5), p.178-179 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Aeromonas sp. produce a lipolytic enzyme that also has the ability to carry out acyl transfer to alcohol acceptors in aqueous media. The fact that there is only one glycine in this sequence indicates that the structure of the active site is likely to differ from those with solved three-dimensional structures. There is evidence for the Escherichia coli thioesterase I and the Vibrio mimicus arylesterase that the first serine of this sequence is the nucleophile, as it is with the Aeromonas lipase. Proteins from E. coli, V. mimicus, Vibrio parahaemolyticus and Xenorhabdus luminescens are all known to have lipolytic activity. |
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ISSN: | 0968-0004 1362-4326 |
DOI: | 10.1016/S0968-0004(00)89002-7 |