Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism

Détails

ID Serval
serval:BIB_C5330022BA7E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism
Périodique
Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids
Auteur(s)
Cheng  Q., Sanglard  D., Vanhanen  S., Liu  H. T., Bombelli  P., Smith  A., Slabas  A. R.
ISSN
1388-1981
ISSN-L
1879-2618
Statut éditorial
Publié
Date de publication
08/2005
Peer-reviewed
Oui
Volume
1735
Numéro
3
Pages
192-203
Notes
Journal Article Research Support, Non-U.S. Gov't --- Old month value: Aug 15
Résumé
The industrial yeasts Candida tropicalis or Candida cloacae are able to grow on a variety of long chain alkanes and fatty acids as the sole carbon source. The complete oxidation of these substrates involves two sequential oxidative pathways: omega-oxidation, comprising the P450 alkane oxidase, a flavin-dependent membrane-bound long chain fatty alcohol oxidase [FAO] and a possible separate aldehyde oxidase [F.M. Dickinson, C. Wadforth, Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis, Biochem. J. 282 (1992) 325-331], and the beta-oxidation pathway, which utilises acylCoA substrates. We recently purified the membrane-bound long chain fatty alcohol oxidase FAO1 and confirmed it is also a c-type haemoprotein. Multiple isoforms may exist for many of these long chain fatty alcohol oxidases and the in vivo requirements for individual genes with respect to specific substrates are still being elucidated. In vitro reconstitution experiments have demonstrated that in Candida maltosa, the cytochrome P450 52A3 gene product can completely oxidise alkanes to dicarboxylic acids [U. Scheller, T. Zimmer, D. Becher, F. Schauer, W. Schunck, Oxygenation Cascade in Conversion of n-Alkanes to, -Dioic Acids Catalyzed by Cytochrome P450 52A3, J. Biol. Chem. 273 (1998) 32528-32534], potentially obviating requirements for a long chain alcohol oxidase. Here, we directly determine in vivo the role of the long chain alcohol oxidase (FAOT) in C. tropicalis, grown on a variety of substrates, followed by gene deletion. The faot double knockout has no detectable faot activity and is incapable of growth on octadecane, but it grows well on oleic acid, palmitic acid and shorter chain alkanes/fatty acids. A spontaneous mutation[s] may have occurred in the faot double gene knockout of C. tropicalis resulting in its inability to grow on oleic acid and hexadecane. The mutations demonstrate that different pathways of octadecane, hexadecane, oleic acid and palmitic acid utilisation exist in C. tropicalis.
Mots-clé
Alcohol Oxidoreductases/chemistry/*metabolism Alkanes/metabolism Amino Acid Sequence Binding Sites Candida tropicalis/*enzymology/genetics Conserved Sequence Fatty Acids, Nonesterified/*metabolism Fungal Proteins/chemistry/*metabolism Heme/metabolism Hemeproteins/chemistry/*metabolism Kinetics Mitochondria/metabolism Models, Biological Molecular Sequence Data Palmitic Acid Plasmids Polymerase Chain Reaction Sequence Alignment Sequence Homology, Amino Acid Substrate Specificity
Pubmed
Web of science
Création de la notice
25/01/2008 15:40
Dernière modification de la notice
03/03/2018 21:15
Données d'usage