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The lipase/acyltransferase from Candida parapsilosis: molecular cloning and characterization of purified recombinant enzymes.
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- Author(s): Neugnot V;Neugnot V; Moulin G; Dubreucq E; Bigey F
- Source:
European journal of biochemistry [Eur J Biochem] 2002 Mar; Vol. 269 (6), pp. 1734-45.
- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
- Publication Information:
Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Original Publication: Berlin, New York, Springer.
- Subject Terms:
- Abstract:
Candida parapsilosis has been previously shown to produce a lipase (i.e. able to catalyze efficiently the hydrolysis of insoluble lipid esters such as triacylglycerols) that preferentially catalyses transfer reactions such as alcoholysis in the presence of suitable nucleophiles other than water, even in aqueous media with high (> 0.9) water thermodynamic activity. The present work describes the cloning and the overexpression of the gene coding for this enzyme. Two ORFs (CpLIP1 and CpLIP2) were isolated. The deduced 465-amino-acid protein sequences contained the consensus motif (G-X-S-X-G) which is conserved among lipolytic enzymes. Only one of the two deduced proteins (CpLIP2) contained peptide sequences obtained from the purified lipase/acyltransferase. Homology investigations showed that CpLIP2 has similarities principally with 11 lipases produced by C. albicans (42-61%) and the lipase A from Candida antarctica (31%) but not with the other lipases sequenced so far. Both CpLIP1 and CpLIP2 were expressed in Saccharomyces cerevisiae, but only CpLIP2 coded for an active protein. The substrate specificity and the catalytic behavior of purified recombinant CpLIP2, with or without a C-terminal histidine tag, were not changed compared to those of the native lipase.
- Molecular Sequence:
GENBANK AJ320260
- Accession Number:
0 (DNA Primers)
0 (Multienzyme Complexes)
0 (Recombinant Proteins)
EC 2.3.- (Acyltransferases)
EC 3.1.1.3 (Lipase)
- Publication Date:
Date Created: 20020316 Date Completed: 20020531 Latest Revision: 20190620
- Publication Date:
20231215
- Accession Number:
10.1046/j.1432-1327.2002.02828.x
- Accession Number:
11895444
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