1.1.1.433: sulfoacetaldehyde reductase (NADH)
This is an abbreviated version!
For detailed information about sulfoacetaldehyde reductase (NADH), go to the full flat file.
Reaction
Synonyms
AH68_00250, BkTauF, BwSarD, HMPREF0179_02714, sarD, sqwF, tauF
ECTree
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General Information
General Information on EC 1.1.1.433 - sulfoacetaldehyde reductase (NADH)
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evolution
metabolism
physiological function
additional information
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
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)
evolution
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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
evolution
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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)
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evolution
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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
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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
metabolism
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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
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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
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
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
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
physiological function
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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
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physiological function
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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
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physiological function
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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
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physiological function
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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
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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
additional information
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
additional information
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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
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