Information on EC 1.2.1.73 - sulfoacetaldehyde dehydrogenase

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The enzyme appears in viruses and cellular organisms

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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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.
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
strain CGA009
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Manually annotated by BRENDA team
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+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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low activity an inhibition at higher concentration
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
2-sulfoacetaldehyde
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pH 9.0, 22C
0.092 - 0.12
NAD+
4.5 - 12
NADP+
0.49
Sulfoacetaldehyde
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pH 9.0, 22C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.7
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
190000
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gel filtration
196500
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sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 50000, SDS-PAGE, 4 * 49100, sequence calculation
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