title: Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus.
abstract: Aldehyde dehydrogenases (ALDHs) have been well established in all three domains of life and were shown to play essential roles, e.g., in intermediary metabolism and detoxification. In the genome of Sulfolobus solfataricus, five paralogs of the aldehyde dehydrogenases superfamily were identified, however, so far only the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) and α-ketoglutaric semialdehyde dehydrogenase (α-KGSADH) have been characterized. Detailed biochemical analyses of the remaining three ALDHs revealed the presence of two succinic semialdehyde dehydrogenase (SSADH) isoenzymes catalyzing the NAD(P)(+)-dependent oxidation of succinic semialdehyde. Whereas SSO1629 (SSADH-I) is specific for NAD(+), SSO1842 (SSADH-II) exhibits dual cosubstrate specificity (NAD(P)(+)). Physiological significant activity for both SSO-SSADHs was only detected with succinic semialdehyde and α-ketoglutarate semialdehyde. Bioinformatic reconstructions suggest a major function of both enzymes in γ-aminobutyrate, polyamine as well as nitrogen metabolism and they might additionally also function in pentose metabolism. Phylogenetic studies indicated a close relationship of SSO-SSALDHs to GAPNs and also a convergent evolution with the SSADHs from E. coli. Furthermore, for SSO1218, methylmalonate semialdehyde dehydrogenase (MSDH) activity was demonstrated. The enzyme catalyzes the NAD(+)- and CoA-dependent oxidation of methylmalonate semialdehyde, malonate semialdehyde as well as propionaldehyde (PA). For MSDH, a major function in the degradation of branched chain amino acids is proposed which is supported by the high sequence homology with characterized MSDHs from bacteria. This is the first report of MSDH as well as SSADH isoenzymes in Archaea.
authors.affiliation: Molecular Enzyme Technology and Biochemistry, Biofilm Centre, Faculty of Chemistry, University of Duisburg-Essen, Universitätsstraße 5, Essen, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Esser
authors.forename: T
authors.initials: T
authors.lastname: Kouril
authors.forename: F
authors.initials: F
authors.lastname: Talfournier
authors.forename: J
authors.initials: J
authors.lastname: Polkowska
authors.forename: T
authors.initials: T
authors.lastname: Schrader
authors.forename: C
authors.initials: C
authors.lastname: Bräsen
authors.forename: B
authors.initials: B
authors.lastname: Siebers
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000378:metabolism; D007700:Kinetics; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating) / Q000235:genetics / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism; D010427:Pentose Phosphate Pathway; D010802:Phylogeny; D011073:Polyamines / Q000378:metabolism; D050644:Succinate-Semialdehyde Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics; D005680:gamma-Aminobutyric Acid / Q000031:analogs & derivatives / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D007656:Ketoglutaric Acids; D011073:Polyamines; D005680:gamma-Aminobutyric Acid; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D050644:Succinate-Semialdehyde Dehydrogenase; D050646:Methylmalonate-Semialdehyde Dehydrogenase (Acylating); C009338:succinic semialdehyde; D009584:Nitrogen