Information on EC 1.2.1.73 - sulfoacetaldehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.2.1.73
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RECOMMENDED NAME
GeneOntology No.
sulfoacetaldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfoacetaldehyde degradation II
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Taurine and hypotaurine metabolism
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-
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SYSTEMATIC NAME
IUBMB Comments
2-sulfoacetaldehyde:NAD+ oxidoreductase
This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoacetaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Oceanospirillum sp., CCUG 52065, a marine gammaproteobacterium, strain MED92, gene safD encoding an inducible enzyme
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Manually annotated by BRENDA team
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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 + H2O + NAD(P)+
sulfoacetate + NAD(P)H + H+
show the reaction diagram
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the enzyme is specific for sulfoacetaldehyde, NAD+ is the highly preferred cofactor to NADP+
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-
?
2-sulfoacetaldehyde + H2O + NAD(P)+
sulfoacetate + NADH + H+
show the reaction diagram
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
show the reaction diagram
additional information
?
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the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-sulfoacetaldehyde + H2O + NAD+
sulfoacetate + NADH + H+
show the reaction diagram
additional information
?
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-
the organism assimilates taurine-nitrogen and excrete sulfoacetate. The pathway involved an ABC transporter, taurine:pyruvate aminotransferase, a sulfoacetaldehyde dehydrogenase, and exporter(s) of sulfoacetate, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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low activity an inhibition at higher concentration
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
2-sulfoacetaldehyde
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pH 9.0, 22°C
0.092 - 0.12
NAD+
4.5 - 12
NADP+
0.49
Sulfoacetaldehyde
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pH 9.0, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7
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purified enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 10.5
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50% of maximal activity at pH 7.2, 70% at pH 8.0, and 80% at pH 9.5-10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49100
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
50000
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
190000
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gel filtration
196500
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sequence calculation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SafD is stable in Tris-HCl buffer, pH 9.0
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 610fold to homogeneity by anion exchange and hydrophobic interaction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene safD, DNA and amino acid sequence determination and analysis, genetic organization
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.73)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)