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Information on EC 1.1.1.433 - sulfoacetaldehyde reductase (NADH)
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EC Tree
1.1.1.433 sulfoacetaldehyde reductase (NADH)IUBMB Comments
The enzymes from the bacteria Bilophila wadsworthia and Clostridium sp. MSTE9 catalyse the reaction only in the reduction direction. In the bacterium Bifidobacterium kashiwanohense the optimal reaction pH for sulfoacetaldehyde reduction is 7.5, while that for isethionate oxidation is 10.0. cf. EC 1.1.1.313, sulfoacetaldehyde reductase (NADPH).
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
bktauf, bwsard, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AH68_00250
BkTauF
BwSarD
HMPREF0179_02714
sarD
sqwF
tauF
BkTauF
-
-
-
-
sarD
-
-
-
-
sqwF
-
-
-
-
tauF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isethionate + NAD+ = 2-sulfoacetaldehyde + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
isethionate:NAD+ oxidoreductase
The enzymes from the bacteria Bilophila wadsworthia and Clostridium sp. MSTE9 catalyse the reaction only in the reduction direction. In the bacterium Bifidobacterium kashiwanohense the optimal reaction pH for sulfoacetaldehyde reduction is 7.5, while that for isethionate oxidation is 10.0. cf. EC 1.1.1.313, sulfoacetaldehyde reductase (NADPH).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypropionic acid + NAD+
? + NADH + H+
moderate to low activity
-
-
?
isethionate + NADP+
2-sulfoacetaldehyde + NADPH + H+
-
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
the reduction reaction direction is preferred by the enzyme
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
the reduction reaction direction is preferred by the enzyme
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
?
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
?
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
-
-
r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
-
-
r
3-hydroxypropane-1-sulfonate + NAD+
? + NADH + H+
-
-
-
?
3-hydroxypropane-1-sulfonate + NAD+
? + NADH + H+
low activity
-
-
?
3-hydroxypropane-1-sulfonate + NAD+
? + NADH + H+
low activity
-
-
?
3-hydroxypropane-1-sulfonate + NAD+
? + NADH + H+
-
-
-
?
3-hydroxypropionate + NAD+
? + NADH + H+
-
-
-
?
3-hydroxypropionate + NAD+
? + NADH + H+
-
-
-
?
isethionate + NAD+
2-sulfoacetaldehyde + NADH + H+
-
-
-
r
isethionate + NAD+
2-sulfoacetaldehyde + NADH + H+
-
-
-
r
additional information
?
-
-
substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine
-
-
-
additional information
?
-
substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine
-
-
-
additional information
?
-
-
no substrates: ethanol, ethylene glycol, or ethanolamine
-
-
-
additional information
?
-
no substrates: ethanol, ethylene glycol, or ethanolamine
-
-
-
additional information
?
-
-
substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine
-
-
-
additional information
?
-
substrate specificity, no activity with ethanol, ethylene glycol, and ethanolamine
-
-
-
additional information
?
-
-
no substrates: ethanol, ethylene glycol, or ethanolamine
-
-
-
additional information
?
-
no substrates: ethanol, ethylene glycol, or ethanolamine
-
-
-
additional information
?
-
no substrate: acetaldehyde
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
?
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
?
2-sulfoacetaldehyde + NADH + H+
isethionate + NAD+
-
-
-
r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
-
-
r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
-
-
r
additional information
?
-
no substrate: acetaldehyde
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
NADH/NAD+ is preferred before NADPH/NADP+ by the enzyme
-
additional information
NADH/NAD+ is preferred before NADPH/NADP+ by the enzyme
-
additional information
-
enzyme accepts NADP+/NADPH, reaction of EC 1.1.1.313
-
additional information
enzyme accepts NADP+/NADPH, reaction of EC 1.1.1.313
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
activates, can partially substitute for Zn2+
Zn2+
additional information
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+
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+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
complete inhibition; complete loss of activity. Activity is recovered up to 85% by addition of Zn2+ and 15% by addition of Fe2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.77
NADP+
pH 10.0, 30°C, recombinant wild-type enzyme
0.73
NADPH
pH 10.0, 30°C, recombinant wild-type enzyme
0.5
2-sulfoacetaldehyde
pH 10.0, 30°C, recombinant wild-type enzyme
0.5
2-sulfoacetaldehyde
pH 7.5, temperature not specified in the publication
4.44
isethionate
pH 10.0, 30°C, recombinant wild-type enzyme
4.44
isethionate
pH 10, temperature not specified in the publication
0.08
NAD+
pH 10.0, 30°C, recombinant wild-type enzyme
0.08
NAD+
pH 10, temperature not specified in the publication
0.06
NADH
pH 10.0, 30°C, recombinant wild-type enzyme
0.06
NADH
pH 7.5, temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
NADP+
pH 10.0, 30°C, recombinant wild-type enzyme
18.99
NADPH
pH 10.0, 30°C, recombinant wild-type enzyme
22.83
2-sulfoacetaldehyde
pH 10.0, 30°C, recombinant wild-type enzyme
22.83
2-sulfoacetaldehyde
pH 7.5, temperature not specified in the publication
0.97
isethionate
pH 10.0, 30°C, recombinant wild-type enzyme
0.97
isethionate
pH 10, temperature not specified in the publication
1.3
NAD+
pH 10.0, 30°C, recombinant wild-type enzyme
1.3
NAD+
pH 10, temperature not specified in the publication
18.67
NADH
pH 10.0, 30°C, recombinant wild-type enzyme
18.67
NADH
pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.04
NADP+
pH 10.0, 30°C, recombinant wild-type enzyme
26.01
NADPH
pH 10.0, 30°C, recombinant wild-type enzyme
45.66
2-sulfoacetaldehyde
pH 10.0, 30°C, recombinant wild-type enzyme
46.1
2-sulfoacetaldehyde
pH 7.5, temperature not specified in the publication
0.22
isethionate
pH 10.0, 30°C, recombinant wild-type enzyme
0.22
isethionate
pH 10, temperature not specified in the publication
15.8
NAD+
pH 10, temperature not specified in the publication
16.25
NAD+
pH 10.0, 30°C, recombinant wild-type enzyme
301
NADH
pH 7.5, temperature not specified in the publication
311.17
NADH
pH 10.0, 30°C, recombinant wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
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
-
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
-
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
-
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
-
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
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
-
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
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
-
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
-
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
-
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
-
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
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0A7I0A5_9BIFI
375
0
40468
TrEMBL
-
SARD_BILW3
Bilophila wadsworthia (strain 3_1_6)
387
0
40853
Swiss-Prot
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
83000
83000
recombinant enzyme, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homodimer
2 * 41000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 41000, recombinant enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
structures in the apo form and in a binary complex with NAD+ at 1.9 and 3.0 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F252A
F265A
T257A
F252A
F265A
T257A
F252A
site-directed mutagenesis, the mutant shows 78% reduced activity for isethionate oxidation compared to wild-type enzyme
F252A
mutant retains approximately 28% of the wild-type activity
F265A
almost complete loss of activity
F265A
site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme
T257A
almost complete loss of activity
T257A
site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme
F252A
-
site-directed mutagenesis, the mutant shows 78% reduced activity for isethionate oxidation compared to wild-type enzyme
-
F252A
-
mutant retains approximately 28% of the wild-type activity
-
F265A
-
site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme
-
T257A
-
site-directed mutagenesis, the mutant shows highly reduced activity for isethionate oxidation compared to wild-type enzyme
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tauF, genetic structure, sequence comparisons, recombinant expression as His6-MBP-tagged enzyme in Escherichia coli strain BL21(DE3) from HMT-GGG-BkTauF plasmid
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xing, M.; Wei, Y.; Zhou, Y.; Zhang, J.; Lin, L.; Hu, Y.; Hua, G.; N. Nanjaraj Urs, A.; Liu, D.; Wang, F.; Guo, C.; Tong, Y.; Li, M.; Liu, Y.; Ang, E.; Zhao, H.; Yuchi, Z.; Zhang, Y.
Radical-mediated C-S bond cleavage in C2 sulfonate degradation by anaerobic bacteria
Nat. Commun.
10
1609
2019
Bilophila wadsworthia (E5Y946), Bilophila wadsworthia 3_1_6 (E5Y946)
brenda
Peck, S.C.; Denger, K.; Burrichter, A.; Irwin, S.M.; Balskus, E.P.; Schleheck, D.
A glycyl radical enzyme enables hydrogen sulfide production by the human intestinal bacterium Bilophila wadsworthia
Proc. Natl. Acad. Sci. USA
116
3171-3176
2019
Bilophila wadsworthia (E5Y946), Bilophila wadsworthia 3_1_6 (E5Y946)
brenda
Zhou, Y.; Wei, Y.; Nanjaraj Urs, A.N.; Lin, L.; Xu, T.; Hu, Y.; Ang, E.L.; Zhao, H.; Yuchi, Z.; Zhang, Y.
Identification and characterization of a new sulfoacetaldehyde reductase from the human gut bacterium Bifidobacterium kashiwanohense
Biosci. Rep.
39
BSR20190715
2019
Bifidobacterium catenulatum subsp. kashiwanohense, Bifidobacterium catenulatum subsp. kashiwanohense (A0A0A7I0A5), Bilophila wadsworthia (E5Y946), Bilophila wadsworthia, Bilophila wadsworthia 3_1_6 (E5Y946), Bifidobacterium catenulatum subsp. kashiwanohense PV20-2, Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 (A0A0A7I0A5)
brenda
Liu, J.; Wei, Y.; Ma, K.; An, J.; Liu, X.; Liu, Y.; Ang, E.; Zhao, H.; Zhang, Y.
Mechanistically diverse pathways for sulfoquinovose degradation in bacteria
ACS Catal.
11
14740-14750
2021
Clostridium sp. MSTE9
-
brenda
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