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