Information on EC 1.1.1.308 - sulfopropanediol 3-dehydrogenase

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The expected taxonomic range for this enzyme is: Cupriavidus pinatubonensis

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EC NUMBER
COMMENTARY hide
1.1.1.308
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RECOMMENDED NAME
GeneOntology No.
sulfopropanediol 3-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O = (R)-3-sulfolactate + 2 NADH + 2 H+
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-sulfopropanediol degradation
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SYSTEMATIC NAME
IUBMB Comments
(R)-2,3-dihydroxypropane-1-sulfonate:NAD+ 3-oxidoreductase
The enzyme is involved in degradation of (R)-2,3-dihydroxypropanesulfonate.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JMP134, i.e. Ralstonia eutropha str. JMP134
UniProt
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
(R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O
(R)-sulfolactate + 2 NADH + 2 H+
show the reaction diagram
degradation of (R)-2,3-dihydroxypropanesulfonate
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-
?
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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
(R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O
(R)-sulfolactate + 2 NADH + 2 H+
show the reaction diagram
Q46N53
degradation of (R)-2,3-dihydroxypropanesulfonate
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46
(R)-2,3-dihydroxypropane-1-sulfonate
pH 9.0, 30°C
0.16
NAD+
pH 9.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 10
activity decreases rapidly with decreasing pH. At pH 6.5 the enzyme is almost inactive
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 10
pH 9-10: optimum. Activity decreases rapidly with decreasing pH. At pH 6.5 the enzyme is almost inactive
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46881
x * 46881, calculated from sequence
47000
x * 47000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x * 46881, calculated from sequence; x * 47000, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.308)
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)