Information on EC 1.1.1.313 - sulfoacetaldehyde reductase

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The expected taxonomic range for this enzyme is: Chromohalobacter salexigens

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EC NUMBER
COMMENTARY hide
1.1.1.313
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RECOMMENDED NAME
GeneOntology No.
sulfoacetaldehyde reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
isethionate + NADP+ = 2-sulfoacetaldehyde + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfoacetaldehyde degradation III
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Taurine and hypotaurine metabolism
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Metabolic pathways
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-sulfoacetaldehyde + NADPH + H+
isethionate + NADP+
show the reaction diagram
4-oxobutyrate + NADPH + H+
?
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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highly specific for NADPH. NADH is not a substrate.
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-oxobutyrate
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90% substrate inhibition at 20 mM
additional information
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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 hide
LITERATURE
IMAGE
0.13
2-sulfoacetaldehyde
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in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23°C
0.061
NADPH
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in 0.02 mMTris/H2SO4 buffer, pH 9.0, at 23°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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in Tris/H2SO4 buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27100
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estimated from amino acid sequence
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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IsfD is stable in Tris/H2SO4 buffer, pH 9.0
709846
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Mono Q column chromatography, phenyl Superose gel filtration
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.313)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)