EC Number   |
General Information |
Reference |
|---|
  1.1.1.433 | evolution |
in diverse anaerobic bacteria including Firmicutes, Tenericutes, Spirochaetes, and Thermotogae bacteria, a sulfoquinone degradation pathway contains a mutarotase SqvB, an isomerase SqvD, a transketolase SqwGH, a homologue of ribose-5-phosphate isomerase SqwI, a metal-dependent alcohol dehydrogenase SqwF, and a member of the sulfite/sulfonate exporter family SqwE. This suggests a pathway involving isomerization of sulfoquinone to 6-deoxy-6-sulfofructose by SqvD, cleavage of 6-deoxy-6-sulfofructose by SqwGH, reduction of an aldehyde-containing sulfonate by SqwF, followed by export of the sulfonate end-product by SqwE |
763789 |
| 1.1.1.433 | evolution |
sulfoacetaldehyde reductase from the human gut fermenting bacterium Bifidobacterium kashiwanohense (BkTauF) belongs to the M-ADH family, but is distantly related to BwSarD (28% sequence identity), a sulfoacetaldehyde reductase from human gut sulfite-reducing bacterium Bilophila wadsworthia belonging to the metal-dependent alcohol dehydrogenase superfamily (M-ADH). Conservation of active site residues (D192, Q196, F252, T257, H261, F265 and H275) in close homologues of BkTauF |
-, 762832 |
| 1.1.1.433 | evolution |
sulfoacetaldehyde reductase SarD, from human gut sulfite-reducing bacterium Bilophila wadsworthia belongs to the metal-dependent alcohol dehydrogenase superfamily (M-ADH). Sulfoacetaldehyde reductase from the human gut fermenting bacterium Bifidobacterium kashiwanohense (BkTauF) belongs to the M-ADH family, but is distantly related to BwSarD (28% sequence identity) |
-, 762832 |
| 1.1.1.433 | metabolism |
the enzyme is involved in a pathway for taurine dissimilation, in which isethionate is generated as an intermediate, and further degraded to acetate and H2S instead of being secreted |
-, 762832 |
| 1.1.1.433 | more |
the BktauF structure and sequence shows conservation in secondary structure, and metal-coordinating residues except that Gln196 is atypical in the M-ADH family, with His being more common at that position. The putative isethionate-binding site adjacent to the catalytic Zn2+ is very open, which precluded molecular docking, active site structure analysis, overview. The position of isethionate is constrained by the requirements of the M-ADH catalytic mechanism, which requires coordination of the hydroxyl O-atom to Zn2+, and hydride transfer from C1 of isethionate to C4 of the NAD+. Phe252, Thr257 and Phe265 surrounding the active-site cavity are identified as potential substrate-interacting residues |
-, 762832 |
| 1.1.1.433 | physiological function |
hydroxyethylsulfonate (isethionate (Ise)) is generated by the sulfoacetaldehyde reductases from human gut bacteria. Isethionate is thought to be derived from aminoethylsulfonate (taurine), as a byproduct of taurine nitrogen assimilation by certain anaerobic bacteria inhabiting the taurine-rich mammalian gut. Sulfoacetaldehyde reductases in Bifidobacteria have a possible role in isethionate production as a byproduct of taurine nitrogen assimilation |
-, 762832 |
| 1.1.1.433 | physiological function |
in the taurine desulfonation pathway, an initial deamination of taurine to sulfoacetaldehyde by a taurine:pyruvate aminotransferase is followed by reduction of sulfoacetaldehyde to isethionate (2-hydroxyethanesulfonate) by NADH-dependent reductase SarD. Isethionate is then cleaved to sulfite and acetaldehyde by glycyl radical enzyme isethionate sulfite-lyase IslA |
-, 762283 |
| 1.1.1.433 | physiological function |
involved in taurine degradation in human gut. TauF catalyzes NADH-dependent reduction of sulfoacetaldehyde, generating isethionate that is subsequently cleaved by sulfonate C-S lyase IseG |
-, 761972 |
