EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.313 | gene isfD, genetic structure | Chromohalobacter salexigens |
1.1.1.433 | expression in Escherichia coli | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | gene sarD, genetic structure | Bilophila wadsworthia |
1.1.1.433 | gene tauF, genetic structure, sequence comparisons, recombinant expression as His6-MBP-tagged enzyme in Escherichia coli strain BL21(DE3) from HMT-GGG-BkTauF plasmid | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.433 | purifed recombinant BkTauF in the apo form and in a binary complex with NAD+, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM Tris, pH 7.5, 200 mM KCl, 1 mM DTT, with reservoir solution containing 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 25% w/v PEG 3350, 22°C, method optimization, X-ray diffraction structure determination and analysis at 1.9 and 3.0 A resolution, respectively, molecular replacement using structure with PDB ID 1VHD as a search model, modeling | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | structures in the apo form and in a binary complex with NAD+ at 1.9 and 3.0 A resolution, respectively | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.433 | F252A | site-directed mutagenesis, the mutant shows 78% reduced activity for isethionate oxidation compared to wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | F252A | mutant retains approximately 28% of the wild-type activity | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | F265A | almost complete loss of activity | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | F265A | site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | T257A | almost complete loss of activity | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | T257A | site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.433 | EDTA | complete inhibition; complete loss of activity. Activity is recovered up to 85% by addition of Zn2+ and 15% by addition of Fe2+ | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.433 | additional information | - |
additional information | Michaelis-Menten kinetics | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.06 | - |
NADH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.06 | - |
NADH | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.08 | - |
NAD+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.08 | - |
NAD+ | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.5 | - |
2-sulfoacetaldehyde | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.5 | - |
2-sulfoacetaldehyde | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.73 | - |
NADPH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.77 | - |
NADP+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 4.44 | - |
isethionate | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 4.44 | - |
isethionate | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.433 | Fe2+ | activates, can partially substitute for Zn2+ | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | additional information | catalytic activity of BkTauF is abolished by chelation with EDTA, and recovered up to 85% by addition of Zn2+ and 15% by addition of Fe2+, suggesting that the physiological metal cofactor for BkTauF is Zn2+ | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | Zn2+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | Zn2+ | required | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.1.433 | 83000 | - |
gel filtration | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | 83000 | - |
recombinant enzyme, gel filtration | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens | - |
isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens DSM 3043 | - |
isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens ATCC BAA-138 | - |
isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens NCIMB 13768 | - |
isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens 1H11 | - |
isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | Chromohalobacter salexigens CIP 106854 | - |
isethionate + NADP+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | Bilophila wadsworthia | - |
isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | Bifidobacterium catenulatum subsp. kashiwanohense | - |
isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | Bilophila wadsworthia 3_1_6 | - |
isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | - |
isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADPH + H+ | Bifidobacterium catenulatum subsp. kashiwanohense | - |
isethionate + NADP+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADPH + H+ | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | - |
isethionate + NADP+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.313 | Chromohalobacter salexigens | Q1R183 | - |
- |
1.1.1.313 | Chromohalobacter salexigens 1H11 | Q1R183 | - |
- |
1.1.1.313 | Chromohalobacter salexigens ATCC BAA-138 | Q1R183 | - |
- |
1.1.1.313 | Chromohalobacter salexigens CIP 106854 | Q1R183 | - |
- |
1.1.1.313 | Chromohalobacter salexigens DSM 3043 | Q1R183 | - |
- |
1.1.1.313 | Chromohalobacter salexigens NCIMB 13768 | Q1R183 | - |
- |
1.1.1.433 | Bifidobacterium catenulatum subsp. kashiwanohense | - |
- |
- |
1.1.1.433 | Bifidobacterium catenulatum subsp. kashiwanohense | A0A0A7I0A5 | - |
- |
1.1.1.433 | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | - |
- |
- |
1.1.1.433 | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | A0A0A7I0A5 | - |
- |
1.1.1.433 | Bilophila wadsworthia | E5Y946 | - |
- |
1.1.1.433 | Bilophila wadsworthia 3_1_6 | E5Y946 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.433 | recombinant His6-MBP-tagged enzyme from Escherichia coli strain BL21(DE3) by streptomycin sulfate, dialysis, amylose affinity chromatography, followed by MBP-tag cleavage through TEV protease, dialysis, and nickel affinity chromatography, anion exchange chromatography, and gel filtration | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens | isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens DSM 3043 | isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens ATCC BAA-138 | isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens NCIMB 13768 | isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens 1H11 | isethionate + NADP+ | - |
r | |
1.1.1.313 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Chromohalobacter salexigens CIP 106854 | isethionate + NADP+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | - |
Bilophila wadsworthia | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | the reduction reaction direction is preferred by the enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | - |
Bilophila wadsworthia 3_1_6 | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADH + H+ | the reduction reaction direction is preferred by the enzyme | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | isethionate + NAD+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | isethionate + NADP+ | - |
r | |
1.1.1.433 | 2-sulfoacetaldehyde + NADPH + H+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | isethionate + NADP+ | - |
r | |
1.1.1.433 | 3-hydroxypropane-1-sulfonate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropane-1-sulfonate + NAD+ | low activity | Bifidobacterium catenulatum subsp. kashiwanohense | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropane-1-sulfonate + NAD+ | low activity | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropane-1-sulfonate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropionate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropionate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | ? + NADH + H+ | - |
? | |
1.1.1.433 | 3-hydroxypropionic acid + NAD+ | moderate to low activity | Bifidobacterium catenulatum subsp. kashiwanohense | ? + NADH + H+ | - |
? | |
1.1.1.433 | isethionate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | 2-sulfoacetaldehyde + NADH + H+ | - |
r | |
1.1.1.433 | isethionate + NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | 2-sulfoacetaldehyde + NADH + H+ | - |
r | |
1.1.1.433 | isethionate + NADP+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | 2-sulfoacetaldehyde + NADPH + H+ | - |
r | |
1.1.1.433 | additional information | substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine | Bifidobacterium catenulatum subsp. kashiwanohense | ? | - |
- |
|
1.1.1.433 | additional information | no substrates: ethanol, ethylene glycol, or ethanolamine | Bifidobacterium catenulatum subsp. kashiwanohense | ? | - |
- |
|
1.1.1.433 | additional information | substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | ? | - |
- |
|
1.1.1.433 | additional information | no substrates: ethanol, ethylene glycol, or ethanolamine | Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.433 | dimer | 2 * 41000, SDS-PAGE | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | homodimer | 2 * 41000, recombinant enzyme, SDS-PAGE | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.313 | IsfD | - |
Chromohalobacter salexigens |
1.1.1.433 | AH68_00250 | - |
Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | BkTauF | - |
Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | BwSarD | - |
Bilophila wadsworthia |
1.1.1.433 | sarD | - |
Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | sarD | - |
Bilophila wadsworthia |
1.1.1.433 | tauF | - |
Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | tauF | - |
Bilophila wadsworthia |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.433 | 30 | - |
assay at | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.433 | 0.8 | - |
NADP+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.97 | - |
isethionate | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.97 | - |
isethionate | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 1.3 | - |
NAD+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 1.3 | - |
NAD+ | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 18.67 | - |
NADH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 18.67 | - |
NADH | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 18.99 | - |
NADPH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 22.83 | - |
2-sulfoacetaldehyde | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 22.83 | - |
2-sulfoacetaldehyde | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.433 | 7.5 | - |
sulfoacetaldehyde reduction | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | 10 | - |
assay at | Bifidobacterium catenulatum subsp. kashiwanohense |
1.1.1.433 | 10 | - |
isethionate oxidation | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.313 | NADP+ | - |
Chromohalobacter salexigens | |
1.1.1.313 | NADPH | - |
Chromohalobacter salexigens | |
1.1.1.433 | additional information | NADH/NAD+ is preferred before NADPH/NADP+ by the enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | additional information | enzyme accepts NADP+/NADPH, reaction of EC 1.1.1.313 | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | NAD+ | - |
Bilophila wadsworthia | |
1.1.1.433 | NAD+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | NADH | - |
Bilophila wadsworthia | |
1.1.1.433 | NADH | - |
Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | NADH | preferred cofactor | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | NADP+ | - |
Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | NADPH | - |
Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.313 | evolution | the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family | Chromohalobacter salexigens |
1.1.1.313 | metabolism | in the pathway, taurine is imported by a taurine ABC transporter (TauABC), and converted into sulfoacetaldehyde by taurine:oxoglutarate aminotransferase (Toa), generating glutamate as an intermediate for nitrogen metabolism. The NADPH-dependent sulfoacetaldehyde reductase (IsfD), belonging to the SDR family, generates isethionate as a waste produce, which is exported by the putative isethionate exporter (IsfE) | Chromohalobacter salexigens |
1.1.1.313 | 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 | Chromohalobacter salexigens |
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 | Bifidobacterium catenulatum subsp. kashiwanohense |
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) | Bilophila wadsworthia |
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 | Bilophila wadsworthia |
1.1.1.433 | 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 | Bifidobacterium catenulatum subsp. kashiwanohense |
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 | Bilophila wadsworthia |
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 | Bifidobacterium catenulatum subsp. kashiwanohense |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.433 | 0.22 | - |
isethionate | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 0.22 | - |
isethionate | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 1.04 | - |
NADP+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 15.8 | - |
NAD+ | pH 10, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 16.25 | - |
NAD+ | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 26.01 | - |
NADPH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 45.66 | - |
2-sulfoacetaldehyde | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 46.1 | - |
2-sulfoacetaldehyde | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 301 | - |
NADH | pH 7.5, temperature not specified in the publication | Bifidobacterium catenulatum subsp. kashiwanohense | |
1.1.1.433 | 311.17 | - |
NADH | pH 10.0, 30°C, recombinant wild-type enzyme | Bifidobacterium catenulatum subsp. kashiwanohense |