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Information on EC 1.1.1.313 - sulfoacetaldehyde reductase (NADPH)
for references in articles please use BRENDA:EC1.1.1.313
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.313 sulfoacetaldehyde reductase (NADPH)
IUBMB Comments
Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433, sulfoacetaldehyde reductase (NADH).
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
nadph-dependent sulfoacetaldehyde reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
isethionate formation, reductase D
IsfD
IsfD2
NADPH-dependent sulfoacetaldehyde reductase
IsfD
-
-
-
-
IsfD
-
isoform, this enzyme represents the major portion of the IsfD activity described for taurine-grown cells
IsfD
-
isoform, this enzyme represents the major portion of the IsfD activity described for taurine-grown cells
-
IsfD2
-
isoform, this enzyme is responsible for the low activity observed in extracts of ammonium-grown cells
IsfD2
-
isoform, this enzyme is responsible for the low activity observed in extracts of ammonium-grown cells
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
sulfoacetaldehyde degradation III
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SYSTEMATIC NAME
IUBMB Comments
isethionate:NADP+ oxidoreductase
Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433, sulfoacetaldehyde reductase (NADH).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminoacetaldehyde + CO2 + NADPH + H+
L-serine + NADP+
Substrates: overall reaction, the enzyme also shows high serine 3-dehydrogenase activity, EC 1.1.1.276
Products: -
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r
3-hydroxypropionate + NADPH + H+
? + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
Substrates: -
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ir
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
-
Substrates: -
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ir
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
4-oxobutyrate + NADPH + H+
?
-
Substrates: -
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ir
additional information
?
-
-
Substrates: NADH is not a substrate
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?
additional information
?
-
-
Substrates: NADH is not a substrate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
Products: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
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r
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
Substrates: -
Products: -
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
binding structure analysis from crystal structure (PDB ID 6IXJ)
NADPH
the side chains of T13, R36, R37 form hydrogen bond interactions with the 20-phosphate group of NADPH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by formaldehyde, acetaldehyde, betaine aldehyde, propionaldehyde, DL-glyceraldehyde, phosphonoacetaldehyde, glyoxylate, 2-oxobutyrate, 4-oxobutyrate and 3-sulfopropanaldehyde
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2-sulfoacetaldehyde
-
in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23Ā°C
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
IsfD shows a broad pH optimum from about pH 6.5 to pH 9.5. There is a steep increase in activity from pH 4.5 (negligible activity) and an equally steep decrease above pH 9.5
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
IsfD is detected at low levels in extracts of ammonium-grown cells
brenda
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IsfD is detected at low levels in extracts of ammonium-grown cells
-
brenda
-
IsfD is detected at high levels in extracts of taurine-grown cells
brenda
-
IsfD is detected at high levels in extracts of taurine-grown cells
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
among the dehydrogenases and reductases from taurine metabolism, only IsfD belongs to the short-chain dehydrogenase/reductase (SDR) superfamily. IsfD is closely related to YdfG from Escherichia coli (49% identical residues at 97% query cover) that has been characterized at first as serine dehydrogenase but functions also as malonic semialdehyde reductase in vivo
evolution
sulfoacetaldehyde reductase (IsfD) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily, involved in nitrogen assimilation from aminoethylsulfonate (taurine) in certain environmental and human commensal bacteria. Biochemical investigations of the substrate scope of IsfD, and bioinformatics analysis of IsfD homologs, suggest that IsfD is related to the promiscuous 3-hydroxyacid dehydrogenases with diverse metabolic functions
evolution
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
evolution
-
the enzyme sulfoacetaldehyde reductase IsfD belongs to the short-chain dehydrogenase/reductase (SDR) family
-
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)
metabolism
IsfD-dependent metabolic pathway and genome neighborhood of IsfD, overview
metabolism
the enzyme catalyzes the reversible reduction in sulfoacetaldehyde to the corresponding alcohol isethionate. This is a key step in detoxification of the carbonyl intermediate formed in bacterial nitrogen assimilation from the alpha-aminoalkanesulfonic acid taurine. Bacterial taurine degradation is widespread, bacterial pathways for the degradation of taurine, overview
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)
-
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)
-
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)
-
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)
-
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)
-
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
physiological function
IsfD catalyzes the reversible NADPH-dependent reduction of sulfoacetaldehyde, which is generated by transamination of taurine, forming hydroxyethylsulfonate (isethionate) as a waste product
physiological function
like other aldehydes, sulfoacetaldehyde is potentially toxic and can be oxidized to sulfoacetate. In most taurine-degrading bacteria, however, it is reduced to the corresponding alcohol isethionate. In case this alcohol is excreted as the end product of taurine catabolism, the sulfur and carbon atoms are not assimilated. Although catalyzing serine and 3-hydroxypropionate oxidation as well, the role of IsfD in taurine metabolism and sulfoacetaldehyde reduction to isethionate is clearly corroborated by the operon-like association of the corresponding gene isfD together with genes encoding taurine uptake by transporter TauABC and deamination by transaminase Toa in Klebsiella oxytoca. There are physiological roles of IsfD-related SDR 3-hydroxyacid dehydrogenases
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
-
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
-
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
-
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
-
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
-
additional information
structure-function analysis of IsfD, overview
additional information
the bound isethionate is oriented with its hydroxyl group facing the tyrosine residue of the catalytic tetrad (Y154) and its sulfonate group forming hydrogen bond network with Y148, R195, Q244 and a water molecule. The side chains of I142, I186 and F191 further stabilize the conformation of the substrate through hydrophobic interactions. Active site structure and structure comparisons, overview
Show AA Sequence and Transmembrane Helices (344 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
additional information
IsfD forms a homotetramer in both crystal and solution states, with the C-terminal tail of each subunit interacting with the C-terminal tail of the diagonally opposite subunit, forming an antiparallel beta-sheet that constitutes part of the substrate-binding site. The sulfonate group of isethionate is stabilized by a hydrogen bond network formed by the residues Y148, R195, Q244 and a water molecule. In addition, F249 from the diagonal subunit restrains the conformation of Y148 to further stabilize the orientation of the sulfonate group. Quaternary, subunit structure of IsfD and the structure-based sequence alignments of IsfD with selected SDR members, overview
homotetramer
in the tetrameric structure of IsfD, the respective diagonal subunits cross-interact strongly via their C-terminal tails. The latter region with beta-sheets 8 and 9 protrudes away from the main subunit body and reaches the active site of the opposite subunit. Thus, stabilization of the substrate-binding loop in the closed conformation is accomplished. In particular, C-terminal residue F248 is located close to side chains of active site amino acids I142 and Y148 of the diagonal subunit. This important interaction results in a proper positioning of Y148 for hydrogen bonding with the sulfonate group of isethionate. Enzyme structure comparisons, detailed overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His-tagged enzyme IsfD in a ternary complex with NADPH and isethionate, hanging drop vapor diffusion method, mixing of protein in 10 mM HEPES, pH 7.4, 50 mM KCl, 1 mM TCEP (tris(2-carboxyethyl)phosphine), with reservoir solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 5.5, 30% w/v PEG 4000, 5 mM NADPH, and 0.4 M isethionate, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using 2NWQ as a search model, structure comparisons, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I142A
site-directed mutagenesis, the mutant shows 33.6% of wild-type activity
I186A
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
T13A
site-directed mutagenesis, the mutant shows 7.8% of wild-type activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by streptomycin sulfate precipitation, cobalt affinity chromatography, His-tag cleavage by TEV protease, dialysis, anion exchange chromatography, ultrafiltration, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene isfD, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) from plasmid HMT-IsfD
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krejcķk, Z.; Hollemeyer, K.; Smits, T.H.; Cook, A.M.
Isethionate formation from taurine in Chromohalobacter salexigens: purification of sulfoacetaldehyde reductase
Microbiology
156
1547-1555
2010
Chromohalobacter salexigens, Chromohalobacter salexigens DSM 3043
brenda
Zhou, Y.; Wei, Y.; Lin, L.; Xu, T.; Ang, E.L.; Zhao, H.; Yuchi, Z.; Zhang, Y.
Biochemical and structural investigation of sulfoacetaldehyde reductase from Klebsiella oxytoca
Biochem. J.
476
733-746
2019
Klebsiella oxytoca (D3U1D9)
brenda
Rohwerder, T.
New structural insights into bacterial sulfoacetaldehyde and taurine metabolism
Biochem. J.
477
1367-1371
2020
Klebsiella oxytoca (D3U1D9)
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
Chromohalobacter salexigens (Q1R183), Chromohalobacter salexigens 1H11 (Q1R183), Chromohalobacter salexigens ATCC BAA-138 (Q1R183), Chromohalobacter salexigens CIP 106854 (Q1R183), Chromohalobacter salexigens DSM 3043 (Q1R183), Chromohalobacter salexigens NCIMB 13768 (Q1R183)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.313)
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Release 2023.1 (January 2023)
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