Information on EC 1.1.1.61 - 4-hydroxybutyrate dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.1.61
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxybutyrate dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation V
-
-
succinate fermentation to butanoate
-
-
CO2 fixation in Crenarchaeota
-
-
Butanoate metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoate:NAD+ oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4HBD
-
-
-
-
gamma-hydroxybutyrate dehydrogenase
-
-
-
-
gamma-hydroxybutyrate dehydrogenase
-
gamma-hydroxybutyrate dehydrogenase
Escherichia coli K12 BW25113
-
-
GHBDH
Escherichia coli K12 BW25113
-
-
uncharacterized oxidoreductase YihU
-
uncharacterized oxidoreductase YihU
Escherichia coli K12 BW25113
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-60-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12 BW25113
UniProt
Manually annotated by BRENDA team
Escherichia coli K12 BW25113
strain K12 BW25113
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxypropane sulfonate + NAD+
? + NADH
show the reaction diagram
Escherichia coli, Escherichia coli K12 BW25113
-
-
?
3-hydroxypropane sulfonate + NAD+
? + NADH + H+
show the reaction diagram
-
-
r
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
r
4-hydroxybutanoate + NADP+
succinate semialdehyde + NADPH + H+
show the reaction diagram
-
-
-
?
ethanol + NADP+
ethanal + NADPH + H+
show the reaction diagram
-
-
-
?
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
show the reaction diagram
-
-
r
methylglyoxal + NAD+
? + NADH
show the reaction diagram
Escherichia coli, Escherichia coli K12 BW25113
-
-
?
succinate semialdehyde + NAD(P)H + H+
4-hydroxybutanoate + NAD(P)+
show the reaction diagram
important in oxidative stress tolerance
-
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
show the reaction diagram
Escherichia coli, Escherichia coli K12 BW25113
-
-
r
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
show the reaction diagram
succinic semialdehyde is the preferred substrate
-
r
methylglyoxal + NAD+
? + NADH + H+
show the reaction diagram
-
-
r
additional information
?
-
no activity with D-glycerate and 3-hydroxypropanoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
r
4-hydroxybutanoate + NADP+
succinate semialdehyde + NADPH + H+
show the reaction diagram
-
-
-
?
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
show the reaction diagram
P0A9V8
-
-
r
succinate semialdehyde + NAD(P)H + H+
4-hydroxybutanoate + NAD(P)+
show the reaction diagram
Q9LSV0
important in oxidative stress tolerance
-
?
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
show the reaction diagram
P0A9V8
succinic semialdehyde is the preferred substrate
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
; the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu
-
monomeric units contains two atoms
Fe
-
monomeric unit contains one atom
additional information
no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
10 mM leads to 50% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
3-hydroxypropane sulfonate
; in 100 mM Tris-HCl buffer (pH 8.8), at 37C
0.055
4-hydroxybutanoate
-
-
102
4-hydroxybutyrate
-
14
ethanol
-
pH 8.5, 23C
2.19
gamma-hydroxybutyrate
-
pH 8.5, 23C
102
gamma-hydroxybutyrate
in 100 mM Tris-HCl buffer (pH 8.8), at 37C
9
methylglyoxal
; in 100 mM Tris-HCl buffer (pH 8.8), at 37C
0.56
Succinic semialdehyde
-
-
4.3
Succinic semialdehyde
; in 100 mM MOPS-KOH buffer (pH 7.2), at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.062
substrate: gamma-hydroxybutyrate
0.067
substrate: methylglyoxal
0.2
substrate: succinic semialdehyde
9
substrate: 3-hydroxypropane sulfonate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.1
-
reduction of 4-hydroxybutanoate
7
-
reduction of 4-hydroxybutanoate
9.4
-
oxidation of 4-hydroxybutanoate
10.5
-
oxidation of 4-hydroxybutanoate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
calculated from predicted amino acid sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30300
calculated from predicted amino acid sequence
656170
40500
-
calculated from the predicted amino acid sequence of the native enzyme
656423
66000
-
fusion protein, SDS-PAGE, calculated mass
656423
86000
-
gel filtration
287171
143000
gel filtration; gel filtration
698903
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 41600, SDS-PAGE
homotetramer
4 * 31154, calculated from amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-80
-
stable for indefinite timespan
656423
4
-
stable for at least 21 days, 60% of activity after 3.5 months
656423
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of ammonium sulfate, glycerol, 2-mercaptoethanol, dithiothreitol, glutathione, or EDTA reduces activity during storage
-
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
complementation experiments with a succinic semialdehyde dehydrogenase deficient yeast strain uga2, complemented yeast is able to use gamma-aminobutyrate as nitrogen source
expressed in Escherichia coli pLysS as stable fusion protein
-
expressed as a histidine-tagged recombinant protein in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
dipstick assay for the detection of gamma-hydroxybutyrate in alcoholic beverages