Please use this identifier to cite or link to this item: 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
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