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Information on EC 1.1.1.61 - 4-hydroxybutyrate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.61
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.61 4-hydroxybutyrate dehydrogenase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.61
- coa
- kluyveri
- succinate-semialdehyde
-
ralstonia
- eutropha
- succinyl-coa
- polyhydroxyalkanoates
-
coa-dependent
- propionyl-coas
-
poly3-hydroxybutyrate-co-4-hydroxybutyrate
- 3-hydroxybutyrate
- poly-3-hydroxybutyrate
-
luria-bertani
-
coa-transferase
- 1,4-butanediol
-
bioplastics
-
nadp+-dependent
- analysis
showSynonyms
4-hydroxybutyrate dehydrogenase, ghbdh, succinate semialdehyde reductase, gamma-hydroxybutyrate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4HBD
-
-
-
-
gamma-hydroxybutyrate dehydrogenase
GHBDH
PGN 0724 protein
succinate semialdehyde reductase
uncharacterized oxidoreductase YihU
gamma-hydroxybutyrate dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
4-aminobutanoate degradation V, succinate fermentation to butanoate
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutanoate:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-60-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxypropane sulfonate + NAD+
? + NADH + H+
Substrates: -
Products: -
Products: -
r
4-hydroxybutanoate + NADP+
succinate semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
Substrates: succinic semialdehyde is the preferred substrate
Products: -
Products: -
r
3-hydroxypropane sulfonate + NAD+
? + NADH
Substrates: -
Products: -
Products: -
?
3-hydroxypropane sulfonate + NAD+
? + NADH
Substrates: -
Products: -
Products: -
?
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
Substrates: -
Products: -
Products: -
?
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
methylglyoxal + NAD+
? + NADH
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NAD(P)H + H+
4-hydroxybutanoate + NAD(P)+
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NAD(P)H + H+
4-hydroxybutanoate + NAD(P)+
Substrates: important in oxidative stress tolerance
Products: -
Products: -
?
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
-
Substrates: -
Products: -
Products: -
r
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
succinic semialdehyde + NADH + H+
4-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: no activity with D-glycerate and 3-hydroxypropanoate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-glycerate and 3-hydroxypropanoate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxybutanoate + NAD+
succinate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
4-hydroxybutanoate + NADP+
succinate semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
gamma-hydroxybutyrate + NAD+
succinic semialdehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
succinate semialdehyde + NAD(P)H + H+
4-hydroxybutanoate + NAD(P)+
Substrates: important in oxidative stress tolerance
Products: -
Products: -
?
succinic semialdehyde + NADH + H+
gamma-hydroxybutyrate + NAD+
Substrates: succinic semialdehyde is the preferred substrate
Products: -
Products: -
r
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADH + H+
4-hydroxybutanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
succinate semialdehyde + NADPH + H+
4-hydroxybutanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
the NADH-dependent succinic semialdehyde reductase activity is 4fold higher than that with NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+)
additional information
no significant differences in the activity are observed when using different divalent metals (Mg2+, Mn2+, Ca2+, Co2+, and Zn2+)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
succinate semialdehyde
product inhibition, mixed type inhibition with respect to NAD+, competititve with respect to 4-hydroxybutanoate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nudix hydrolase
at optimal pH 9.0, the GHBDH reaction is activated about 2fold by saturating purified nudix hydrolases, namely Bacillus methanolicus activator (ACT, UniProt: I3EA59) and Escherichia coli NudF (UniProt Q93K97) proteins. At physiological pH values of about 7.0, ACT activates by more than 3.5-fold
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
3-hydroxypropane sulfonate
in 100 mM Tris-HCl buffer (pH 8.8), at 37Ā°C
102
gamma-hydroxybutyrate
in 100 mM Tris-HCl buffer (pH 8.8), at 37Ā°C
0.15
succinate semialdehyde
-
with NADH as cosubstrate, at pH 8.0 and 37Ā°C
4.3
Succinic semialdehyde
in 100 mM MOPS-KOH buffer (pH 7.2), at 37Ā°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1329
succinate semialdehyde
-
with NADH as cosubstrate, at pH 8.0 and 37Ā°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0084
succinate semialdehyde
substrate 4-hydroxybutanoate, pH 9, 23Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Show AA Sequence and Transmembrane Helices (118 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40500
-
calculated from the predicted amino acid sequence of the native enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of ammonium sulfate, glycerol, 2-mercaptoethanol, dithiothreitol, glutathione, or EDTA reduces activity during storage
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified using cobalt-based immobilized TALON metal affinity chromatography resins with a gravity-flow column
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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 as a histidine-tagged recombinant protein in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
dipstick assay for the detection of gamma-hydroxybutyrate in alcoholic beverages
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nirenberg, M.W.; Jakoby, W.B.
Enzymatic utilization of gamma-hydroxybutyric acid
J. Biol. Chem.
235
954-960
1960
Pseudomonas sp.
brenda
Wolff, R.A.; Kenealy W.R.
Purification and characterization of the oxygen-sensitive 4-hydroxybutanoate dehydrogenase from Clostridium kluyveri
Protein Expr. Purif.
6
206-212
1995
Clostridium kluyveri
brenda
Breitkreuz, K.E.; Allan, W.L.; Van Cauwenberghe, O.R.; Jakobs, C.; Talibi, D.; Andre, B.; Shelp, B.J.
A novel gamma-hydroxybutyrate dehydrogenase: identification and expression of an Arabidopsis cDNA and potential role under oxygen deficiency
J. Biol. Chem.
278
41552-41556
2003
Arabidopsis thaliana (Q9LSV0), Arabidopsis thaliana
brenda
Bravo, D.T.; Harris, D.O.; Parsons, S.M.
Reliable, sensitive, rapid and quantitative enzyme-based assay for gamma-hydroxybutyric acid (GHB)
J. Forensic Sci.
49
379-387
2004
Cupriavidus necator
brenda
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)
brenda
Yoshida, Y.; Sato, M.; Nagano, K.; Hasegawa, Y.; Okamoto, T.; Yoshimura, F.
Production of 4-hydroxybutyrate from succinate semialdehyde in butyrate biosynthesis in Porphyromonas gingivalis
Biochim. Biophys. Acta
1850
2582-2591
2015
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Taxon, E.S.; Halbers, L.P.; Parsons, S.M.
Kinetics aspects of Gamma-hydroxybutyrate dehydrogenase
Biochim. Biophys. Acta Proteins Proteom.
1868
140376
2020
Cupriavidus necator (Q59104), Cupriavidus necator
brenda
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