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https://doi.org/10.1186/1471-2091-13-4
Title: | Identification of avian wax synthases | Authors: | Biester, E.-M Hellenbrand, J Gruber, J Hamberg, M Frentzen, M |
Keywords: | alcohol derivative complementary DNA ester palmitoyl coenzyme A hydrolase synthetase triacylglycerol unclassified drug wax ester wax synthase animal cell animal experiment article barn owl bird catalysis chicken controlled study enzyme activity enzyme specificity eukaryote goose in vitro study in vivo study nonhuman nucleotide sequence owl prokaryote protein analysis protein expression protein function protein localization protein processing protein synthesis sequence analysis transcription initiation yeast cell Acyltransferases Amino Acid Motifs Amino Acid Sequence Animals Avian Proteins Cell Membrane Chickens Exocrine Glands Geese Gene Expression Profiling Lipids Molecular Sequence Data Organ Specificity Phylogeny Saccharomyces cerevisiae Sequence Alignment Sequence Homology, Amino Acid Strigiformes Substrate Specificity Anser Anseriformes Aves Eukaryota Galliformes Strigiformes Tytonidae |
Issue Date: | 2012 | Citation: | Biester, E.-M, Hellenbrand, J, Gruber, J, Hamberg, M, Frentzen, M (2012). Identification of avian wax synthases. BMC Biochemistry 13 (1) : 4. ScholarBank@NUS Repository. https://doi.org/10.1186/1471-2091-13-4 | Rights: | Attribution 4.0 International | Abstract: | Background: Bird species show a high degree of variation in the composition of their preen gland waxes. For instance, galliform birds like chicken contain fatty acid esters of 2,3-alkanediols, while Anseriformes like goose or Strigiformes like barn owl contain wax monoesters in their preen gland secretions. The final biosynthetic step is catalyzed by wax synthases (WS) which have been identified in pro- and eukaryotic organisms. Results: Sequence similarities enabled us to identify six cDNAs encoding putative wax synthesizing proteins in chicken and two from barn owl and goose. Expression studies in yeast under in vivo and in vitro conditions showed that three proteins from chicken performed WS activity while a sequence from chicken, goose and barn owl encoded a bifunctional enzyme catalyzing both wax ester and triacylglycerol synthesis. Mono- and bifunctional WS were found to differ in their substrate specificities especially with regard to branched-chain alcohols and acyl-CoA thioesters. According to the expression patterns of their transcripts and the properties of the enzymes, avian WS proteins might not be confined to preen glands. Conclusions: We provide direct evidence that avian preen glands possess both monofunctional and bifunctional WS proteins which have different expression patterns and WS activities with different substrate specificities. © 2012Biester et al; licensee BioMed Central Ltd. | Source Title: | BMC Biochemistry | URI: | https://scholarbank.nus.edu.sg/handle/10635/181613 | ISSN: | 14712091 | DOI: | 10.1186/1471-2091-13-4 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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