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Information on EC 1.1.1.61 - 4-hydroxybutyrate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P0A9V8

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Escherichia coli
UNIPROT: P0A9V8 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
4-hydroxybutyrate dehydrogenase, ghbdh, succinate semialdehyde reductase, gamma-hydroxybutyrate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-hydroxybutyrate dehydrogenase
-
uncharacterized oxidoreductase YihU
-
4HBD
-
-
-
-
gamma-hydroxybutyrate dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoate:NAD+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-60-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxypropane sulfonate + NAD+
? + NADH
show the reaction diagram
-
-
-
?
methylglyoxal + NAD+
? + NADH
show the reaction diagram
-
-
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
show the reaction diagram
-
-
-
r
3-hydroxypropane sulfonate + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
r
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
show the reaction diagram
-
-
-
r
methylglyoxal + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
r
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
show the reaction diagram
succinic semialdehyde is the preferred substrate
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
show the reaction diagram
-
-
-
r
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
show the reaction diagram
succinic semialdehyde is the preferred substrate
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
3-hydroxypropane sulfonate
-
102
4-hydroxybutyrate
-
9
methylglyoxal
-
4.3
Succinic semialdehyde
-
1
3-hydroxypropane sulfonate
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
102
gamma-hydroxybutyrate
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
9
methylglyoxal
in 100 mM Tris-HCl buffer (pH 8.8), at 37°C
4.3
Succinic semialdehyde
in 100 mM MOPS-KOH buffer (pH 7.2), at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.062
substrate: gamma-hydroxybutyrate
0.067
substrate: methylglyoxal
0.2
substrate: succinic semialdehyde
9
substrate: 3-hydroxypropane sulfonate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a yihU deletion mutant displays reduced tolerance to the cytotoxic effects of exogenous addition of succinic semialdehyde
metabolism
the enzyme is involved in the metabolism of succinic semialdehyde, and other potentially toxic intermediates that may accumulate under stress conditions in Escherichia coli
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
143000
gel filtration
143000
gel filtration
31154
4 * 31154, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 31154, calculated from amino acid sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified using cobalt-based immobilized TALON metal affinity chromatography resins with a gravity-flow column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a histidine-tagged recombinant protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saito, N.; Robert, M.; Kochi, H.; Matsuo, G.; Kakazu, Y.; Soga, T.; Tomita, M.
Metabolite profiling reveals YihU as a novel hydroxybutyrate dehydrogenase for alternative succinic semialdehyde metabolism in Escherichia coli
J. Biol. Chem.
284
16442-16451
2009
Escherichia coli, Escherichia coli (P0A9V8), Escherichia coli K12 BW25113 (P0A9V8)
Manually annotated by BRENDA team