Characterization of new medium-chain alcohol dehydrogenases adds resolution to duplications of the class I/III and the sub-class I genes

Cederlund, Ella; Hedlund, Joel; Jönsson, Andreas; Shafqat, Jawed; Norin, Annika; Keung, Wing Ming; Persson, Bengt; Jörnvall, Hans

doi:10.1016/j.cbi.2011.02.006

Cited by 4 publications

(3 citation statements)

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“…It is a glutathione-dependent formaldehyde dehydrogenase (FDH), a highly conserved and ubiquitous detoxifying enzyme. Duplication of the ancestral ADH3 gene near the agnathan/gnathostome split originated ADH1, which evolved independently in the fish and tetrapod lines becoming the classical hepatic ethanol dehydrogenase [4,5]. In tetrapods, a second duplication of the gene coding for ADH3 generated ADH2, also hepatic but active at higher ethanol concentrations [6].…”

Section: Introductionmentioning

confidence: 99%

The Xenopusalcohol dehydrogenase gene family: characterization and comparative analysis incorporating amphibian and reptilian genomes

et al. 2014

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BackgroundThe alcohol dehydrogenase (ADH) gene family uniquely illustrates the concept of enzymogenesis. In vertebrates, tandem duplications gave rise to a multiplicity of forms that have been classified in eight enzyme classes, according to primary structure and function. Some of these classes appear to be exclusive of particular organisms, such as the frog ADH8, a unique NADP+-dependent ADH enzyme. This work describes the ADH system of Xenopus, as a model organism, and explores the first amphibian and reptilian genomes released in order to contribute towards a better knowledge of the vertebrate ADH gene family.ResultsXenopus cDNA and genomic sequences along with expressed sequence tags (ESTs) were used in phylogenetic analyses and structure-function correlations of amphibian ADHs. Novel ADH sequences identified in the genomes of Anolis carolinensis (anole lizard) and Pelodiscus sinensis (turtle) were also included in these studies. Tissue and stage-specific libraries provided expression data, which has been supported by mRNA detection in Xenopus laevis tissues and regulatory elements in promoter regions. Exon-intron boundaries, position and orientation of ADH genes were deduced from the amphibian and reptilian genome assemblies, thus revealing syntenic regions and gene rearrangements with respect to the human genome. Our results reveal the high complexity of the ADH system in amphibians, with eleven genes, coding for seven enzyme classes in Xenopus tropicalis. Frogs possess the amphibian-specific ADH8 and the novel ADH1-derived forms ADH9 and ADH10. In addition, they exhibit ADH1, ADH2, ADH3 and ADH7, also present in reptiles and birds. Class-specific signatures have been assigned to ADH7, and ancestral ADH2 is predicted to be a mixed-class as the ostrich enzyme, structurally close to mammalian ADH2 but with class-I kinetic properties. Remarkably, many ADH1 and ADH7 forms are observed in the lizard, probably due to lineage-specific duplications. ADH4 is not present in amphibians and reptiles.ConclusionsThe study of the ancient forms of ADH2 and ADH7 sheds new light on the evolution of the vertebrate ADH system, whereas the special features showed by the novel forms point to the acquisition of new functions following the ADH gene family expansion which occurred in amphibians.

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Section: Introductionmentioning

confidence: 99%

The Xenopusalcohol dehydrogenase gene family: characterization and comparative analysis incorporating amphibian and reptilian genomes

et al. 2014

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“…Digests were then subjected to peptide separation by HPLC on Vydac C8 with a 0–60% acetonitrile gradient. Eluted material was submitted to sequencer analysis in an ABI Procise HT N‐terminal sequencer with subsequent PTH detection by HPLC in the ABI 140C Microgradient system, as described …”

Section: Methodsmentioning

confidence: 99%

“…Eluted material was submitted to sequencer analysis in an ABI Procise HT N-terminal sequencer with subsequent PTH detection by HPLC in the ABI 140C Microgradient system, as described. 29 LC-electrospray MS/MS analysis: Alternatively, intact peptide digests, prepared as above, were separated with a C18 column (homemade; 25 cm, Silica Tip 360 lm OD, 75 mm ID, New Objective, Woburn, MA) at a 300 nL/min flow of 5-26% (A, 2% and B, 98% acetonitrile, both in 0.1% formic acid)) for 55 min followed by 95% B for 5 min in an Ultimate 3000 RSL Cnano LC-MS/MS system and on-line insertion into a Thermo Scientific Q Exactive Plus Orbitrap mass spectrometer (13 without use of the focusing device). Spectra were analyzed using the Mascot search engine v. 2.4 (Matrix Science Ltd., UK).…”

Section: Ms/ms and Edman Sequencer Analysismentioning

confidence: 99%

Systemic AA amyloidosis in the red fox (Vulpes vulpes)

et al. 2017

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Amyloid A (AA) amyloidosis occurs spontaneously in many mammals and birds, but the prevalence varies considerably among different species, and even among subgroups of the same species. The Blue fox and the Gray fox seem to be resistant to the development of AA amyloidosis, while Island foxes have a high prevalence of the disease. Herein, we report on the identification of AA amyloidosis in the Red fox (Vulpes vulpes). Edman degradation and tandem MS analysis of proteolyzed amyloid protein revealed that the amyloid partly was composed of full-length SAA. Its amino acid sequence was determined and found to consist of 111 amino acid residues. Based on inter-species sequence comparisons we found four residue exchanges (Ser31, Lys63, Leu71, Lys72) between the Red and Blue fox SAAs. Lys63 seems unique to the Red fox SAA. We found no obvious explanation to how these exchanges might correlate with the reported differences in SAA amyloidogenicity. Furthermore, in contrast to fibrils from many other mammalian species, the isolated amyloid fibrils from Red fox did not seed AA amyloidosis in a mouse model.

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