Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase

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

EC NUMBER
COMMENTARY
1.1.1.30
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyrate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
show the reaction diagram
enzyme is completely dependent on the presence of phospholipid for activity
-
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
show the reaction diagram
; ordered Bi Bi mechanism, NAD+ first substrate, NADH last product to leave
-
-
-
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
show the reaction diagram
the enzyme shows a dynamical reaction mechanism. In the catalytic site, a water molecule is trapped by the catalytic Tyr155 and Ser142 residues in the vicinity of the bound NAD+ and acetate, substrate binding structure, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Butanoate metabolism
-
ketogenesis
-
ketolysis
-
Metabolic pathways
-
Synthesis and degradation of ketone bodies
-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxybutanoate:NAD+ oxidoreductase
Also oxidizes other 3-hydroxymonocarboxylic acids.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-D-hydroxybutyrate dehydrogenase
-
-
-
-
3-HBDH
-
-
-
-
3-hydroxybutyrate dehydrogenase
-
-
-
-
acetoacetyl-CoA reductase
-
-
BDH
-
-
-
-
BDH
Acidovorax sp.
Q767A0
-
BDH1
Ralstonia pickettii T1
Q2PEN3
;
-
BDH2
Ralstonia pickettii T1
Q2PEN2
;
-
BDH3
A8R3J3
-
BDH3
Ralstonia pickettii T1
A8R3J3
-
-
beta-hydroxybutyrate dehydrogenase
-
-
-
-
beta-hydroxybutyrate dehydrogenase
-
-
beta-hydroxybutyric acid dehydrogenase
-
-
-
-
beta-hydroxybutyric dehydrogenase
-
-
-
-
D(-)-3-hydroxybutyrate dehydrogenase
Acidovorax sp.
Q767A0
-
D-(-)-3-hydroxybutyrate dehydrogenase
-
-
-
-
D-(-)-3-hydroxybutyrate dehydrogenase
Q2PEN2, Q2PEN3
-
D-(-)-3-hydroxybutyrate dehydrogenase
Ralstonia pickettii T1
Q2PEN2, Q2PEN3
-
-
D-3-hydroxybutyrate dehydrogenase
-
-
-
-
D-3-hydroxybutyrate dehydrogenase
-
-
D-3-hydroxybutyrate dehydrogenase
-
-
D-3-hydroxybutyrate dehydrogenase
-
-
D-3-hydroxybutyrate dehydrogenase
-
-
D-3-hydroxybutyrate dehydrogenase
-, Q9AE70
-
D-beta-hydroxybutyrate dehydrogenase
-
-
-
-
D-beta-hydroxybutyrate dehydrogenase
-
-
D-beta-hydroxybutyrate dehydrogenase
-
-
DHRS6
-
-
HBDH
Q9AE70
-
NAD-beta-hydroxybutyrate dehydrogenase
-
-
-
-
hydroxybutyrate oxidoreductase
-
-
-
-
additional information
-
the enzyme belongs to the SDR family
additional information
-
the enzyme belongs to the family of short-chain dehydrogenases/reductases
CAS REGISTRY NUMBER
COMMENTARY
9028-38-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Acidovorax sp.
strain SA1
SwissProt
Manually annotated by BRENDA team
strain T
-
-
Manually annotated by BRENDA team
Bacillus cereus T
strain T
-
-
Manually annotated by BRENDA team
enzyme shows hysteresis, lag phase in progress curve
-
-
Manually annotated by BRENDA team
recombinant enzyme
SwissProt
Manually annotated by BRENDA team
strain T1
SwissProt
Manually annotated by BRENDA team
Ralstonia pickettii T1
strain T1
SwissProt
Manually annotated by BRENDA team
Ralstonia pickettii T1
T1
UniProt
Manually annotated by BRENDA team
Ralstonia pickettii T1
T1
SwissProt
Manually annotated by BRENDA team
Zoogloea ramigera I-16-M
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Gln94, His144, Lys152, and Gln196 form hydrogen bonds with carboxyl and/or ketone group of acetoacetate, Trp187, Trp257 form hydrophobic interactions with the carbon atoms of acetoacetate, and Ser142 and Tyr155 are directly related to the catalytic mechanism
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
10 mM, more than 10fold increase in activity
Ca2+
Zoogloea ramigera I-16-M
-
10 mM 20% increase in activity
Ca2+
Acidovorax sp.
Q767A0
stabilizes the enzyme at 10 mM
Cd2+
-
10 mM, 2fold increase in activity
Cu2+
-
10 mM, 2fold increase in activity
Mg2+
-
10 mM, more than 10fold increase
Mg2+
Zoogloea ramigera I-16-M
-
10 mM 41% increase in activity
Mg2+
-
0.1 mM, 2fold increase in activity, crude extracts
Mg2+
Acidovorax sp.
Q767A0
stabilizes the enzyme at 10 mM
Mn2+
-
10 mM, more than 10fold increase in activity
Mn2+
Acidovorax sp.
Q767A0
stabilizes the enzyme at 10 mM
Zn2+
-
10 mM, 2fold increase in activity
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.38
-
2,4-Dichlorophenoxyacetic acid
-
pH 8.0, 25C, versus NAD+
5.74
-
2,4-Dichlorophenoxyacetic acid
-
pH 8.0, 25C, versus (R)-3-hydroxybutanoate
5.6
-
Cacodylate
-
-
80
-
dimethyl malonate
-
-
0.81
-
DL-2-Hydroxybutyrate
-
-
0.9
-
DL-lactate
-
-
3.8
-
malonate
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
Zoogloea ramigera I-16-M
-
acetoacetate reduction
5.9
8.6
-
acetoacetate reduction, 50% activity at pH 5.0, 66% at pH 8.6
6.5
8.5
A8R3J3, Q2PEN2, Q2PEN3, -
optimal pH of BDH3 is 8.5 in the oxidation reaction and 6.5 in the reduction reaction
7.6
9
-
oxidation of beta-hydroxybutyrate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
-
assay at
30
-
-
reduction reaction
35
-
-
isoenzyme from heavy mitochondria
35
-
-
for heavy mitochondria
37
-
-
assay at
40
-
-
isoenzyme from light mitochondria
40
-
-
for light mitochondria at euthermic state
55
-
Acidovorax sp.
Q767A0
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
60
-
30% of maximal activity at 20C, 63% of maximal activity at 60C
25
49
-
80% activity at 25C and at 49C
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, Tris-HCl buffer, 50-100 mM Mg2+, Mn2+, Ba2+, or Ca2+, enzyme loses all activity in the presence of phosphate buffer or EDTA within 2 min
-
-20C, several months, 0%, 4C, lyophilized, 2 month, 0% inactivation, 4C, 0.1 M sodium phosphate buffer pH 7-8, 5 days, 50% inactivation, stability increases in the presence of 1-10 mM EDTA
-
-20C, 20 mM phosphate buffer, pH 7.0, 20% glycerol
A8R3J3, Q2PEN2, Q2PEN3, -
-20C, crude extract, partially purified enzyme, several weeks, 0% inactivation
-
-20C, 1 mg enzyme/ml, 0.2 mM potassium phosphate pH 8.0, 10% glycerol, 10 mM 2-mercaptoethanol, 6 months, 0% inactivation, 0C, 0.1 mg enzyme/ml, 1 day, 50% inactivation
Zoogloea ramigera I-16-M
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
the enzyme is a useful marker in the assay of diabetes mellitus and/or ketoacidosis
synthesis
-
the engineered enzyme mutant H144L/W187F is used for production of 4-hydroxyvaleric acid, a monomer of bio-polyester and a precursor of bio-fuels, from levulinic acid