Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
isoenzyme from heavy mitochondria and isoenzyme from light mitochondria show no significant difference in activity
-
-
?
(R)-3-hydroxybutanoate + 3-acetylpyridine adenine dinucleotide
acetoacetate + 3-acetylpyridine adenine dinucleotideH2
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-, D0VWQ0
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
Zoogloea ramigera I-16-M
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
Q5KST5
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
model of the binding mode of the substrate D-3-hydroxybutyrate, Gln193 is the only residue of the substrate-binding loop that interacts directly with the substrate, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form, overview
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
Bacillus cereus T
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-, Q9AE70
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Q2PEN2, Q2PEN3
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Ralstonia pickettii T1
Q2PEN2, Q2PEN3
-
-
-
r
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
show the reaction diagram
-
-, the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
-
-
r
(R)-3-hydroxybutanoate + NADP+
acetoacetate + NADPH
show the reaction diagram
Q5KST5
activity with NADP+ is 2% of the activity with NAD+
-
-
?
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Acidovorax sp.
Q767A0
-
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Acidovorax sp.
Q767A0
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
-
-
r
2-hydroxypropansulfonate + NAD+
acetonylsulfonate + NADH
show the reaction diagram
-
-
-
r
2-methyl-3-hydroxybutyrate + NAD+
2-methylacetoacetate + NADH
show the reaction diagram
-
-
-
r
4-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
isoenzyme from heavy mitochondria shows 40% lower activity than enzyme fromlight mitochondria
-
-
?
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
A8R3J3, Q2PEN2, Q2PEN3, -
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
A8R3J3, Q2PEN2, Q2PEN3, -
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
A8R3J3, Q2PEN2, Q2PEN3, -
BDH3 is specialized to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
the reversible reactions occur by shuttle movements of a hydrogen negative ion from the C3 atom of the substrate to the C4 atom of NAD+ and from the C4 atom of NADH to the C3 atom of the product. The reaction may be further coupled to the withdrawal of a proton from the hydroxyl group of the substrate by the ionized Tyr155 residue
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Ralstonia pickettii T1
A8R3J3, Q2PEN2, Q2PEN3
BDH3 is specialized to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Ralstonia pickettii T1
A8R3J3, Q2PEN2, Q2PEN3
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Ralstonia pickettii T1
A8R3J3, Q2PEN2, Q2PEN3
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
A8R3J3, Q2PEN2, Q2PEN3, -
-
-
-
r
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Ralstonia pickettii T1
A8R3J3, Q2PEN2, Q2PEN3
-
-
-
r
L-threonine + NAD+
?
show the reaction diagram
Q5KST5
-
-
-
?
additional information
?
-
-
enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
-
-
-
additional information
?
-
-
a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, overview
-
-
-
additional information
?
-
-
no activity of the wild-type enzyme with levulinic acid, enzyme mutant H144L/W187F is active with levulinic acid producing 4-hydroxyvaleric acid
-
-
-
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
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-, D0VWQ0
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
Zoogloea ramigera I-16-M
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
show the reaction diagram
Bacillus cereus T
-
-
-
r
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
show the reaction diagram
-
the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
-
during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
show the reaction diagram
Acidovorax sp.
Q767A0
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
-
-
r
additional information
?
-
-
enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
-
-
-
additional information
?
-
-
a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
Zoogloea ramigera I-16-M
-
-
NAD+
Acidovorax sp.
Q767A0
-
NAD+
Q2PEN2, Q2PEN3
;
NAD+
-
; the substrate-binding loop, residues 187-210, is partially disordered in several subunits, in both the presence and absence of NAD+, closed conformation in the complex structure with NAD+, interactions of Val185, Thr187 and Leu189 with the cosubstrate induced the conformational change from open to closed, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form
NAD+
-
NAD+ is bound in a large cleft in the domain. The diphosphate group of NAD+ is covered by the small additional domain, which is supported by two extended arms allowing domain movement
NADH
Acidovorax sp.
Q767A0
-
NADH
Q2PEN2, Q2PEN3
;
NADP+
-
2% of the activity with NAD+
additional information
-
no activity with NADP+/NADPH
-
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(DL)-2-hydroxybutyrate
-
5 mM, pH 8.5, 25, 69% inhibition
(DL)-lactate
-
5 mM, pH 8.5, 25C, 65% inhibition
2,4-Dichlorophenoxyacetic acid
-
inhibits the enzyme, in vivo treatment of the animals with 2,4-dichlorophenoxyacetic acid leads to strong decrease of triglycerides level and HDL cholesterol and an increase in GOT level and LDL cholesterol, and necrosis of seminiferous tubules cells in testis, hyperplasia of hepatocytes in liver and presence of multinucleated giant cells in brain, overview
2-Hydroxybutyrate
Zoogloea ramigera I-16-M
-
10 mM, 57% inhibition
2-oxobutyrate
Zoogloea ramigera I-16-M
-
10 mM, 29% inhibition
3-hydroxybutyrate
-
substrate inhibition at concentrations above 20 mM, 50% inhibition at 200 mM, cyanylated enzyme is 3fold more active at high substrate concentration
4-mercapto-3-nitrobenzoate
-
derivatization of enzyme sulfhydryl groups, less than 1% residual activity
5,5'-dithiobis(2-nitrobenzoic acid)
Zoogloea ramigera I-16-M
-
0.15 mM, 63% inhibition
acetoacetate
-
substrate inhibition, above 5 mM, noncompetitive vs. NADH
acetoacetate
Zoogloea ramigera I-16-M
-
inhibition above 1 mM, 2 mM, 89% inhibition
acetoacetyl-CoA
Zoogloea ramigera I-16-M
-
1 mM, 29% inhibition
acetyl-CoA
Zoogloea ramigera I-16-M
-
1 mM, 82% inhibition
acetylphosphonate
-
16.7 mM, pH 7, 28% inhibition
ADP
-
2.85 mM, 0.025 mM NADH, 63% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5, noncompetitive vs. acetoacetate
ADP-ribose
-
competitive inhibition vs. coenzyme, noncompetitive vs. substrate
AMP
-
2.85 mM, 0.025 mM NADH, 55% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5
ATP
-
2.85 mM, 0.025 mM NADH, 79% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5, noncompetitive vs. acetoacetate
Butanedione
-
-
Butyrate
-
5 mM, pH 8.5, 25C, 22% inhibition
Butyrate
Zoogloea ramigera I-16-M
-
10 mM, 20% inhibition
Cacodylate
-
competitive
crotonate
Zoogloea ramigera I-16-M
-
10 mM, 20% inhibition
CuSO4
Zoogloea ramigera I-16-M
-
1 mM, 81% inhibition
D-lactate
-
5 mM, pH 8.5, 25, 85% inhibition, uncompetitive vs. coenzyme, competitive vs. substrate
Diamide
A8R3J3, Q2PEN2, Q2PEN3, -
-
diazenedicarboxylic acid bis(dimethylamide)
-
0.20 mM, activity can be recovered with dithiothreitol, enzyme contains a vicinal dithiol that is oxidized by diamide
diazenedicarboxylic acid bis(dimethylamide)
-
NAD+ protects against inhibition
dimethyl malonate
-
-
dimethyl phosphate
-
16.7 mM, pH 7, 12% inhibition
dimethylmalonate
-
15.3 mM, 50% inhibition, oxidation, 11.3% reduction
dimethylmalonate
-
7.6 mM, 50% inhibition, oxidation, 8.5 mM, reduction
dimethyloxyphosphinylacetate
-
competitive inhibitor vs. acetoacetate
DL-2-Hydroxybutyrate
-
-
EDTA
Acidovorax sp.
Q767A0
inhibition and destabilization of the enzyme at 10 mM
glucose
Acidovorax sp.
Q767A0
inhibits the enzyme when contained in the growth medium
Hg2+
Acidovorax sp.
Q767A0
inhibition at 1 mM, and destabilization at 10 mM
HgCl2
Zoogloea ramigera I-16-M
-
0.1 mM, 100% inhibition
HgCl2
-
enzyme extremely sensitive, NADH and Ca2+ protect
Hydroxymalonate
-
4.8 mM, 50% inhibition, oxidation, 7.8 reduction
Hydroxymalonate
-
1.8 mM, 50% inhibition, oxidation, 6.0 mM, reduction
Hydroxymalonate
-
-
KCl
-
80-100 mM, 50% inhibition
L-3-hydroxybutyrate
-
5 mM, pH 8.5, 25C, 23% inhibition; 5 mM, pH 8.5, 25C, 32% inhibition
L-3-hydroxybutyrate
Zoogloea ramigera I-16-M
-
5 mM, 73% inhibition
L-3-hydroxybutyrate
-
is a competitive inhibitor
LiCl
-
80-100 mM, 50% inhibition
malonate
Zoogloea ramigera I-16-M
-
10 mM, 66% inhibition, oxidation
malonate
-
9.5 mM, 50% inhibition, oxidation, 8.2 mM
malonate
-
3.7 mM, 50% inhibition, oxidation
methanephosphonic acid
-
3.3 mM, pH 7, 11% inhibition
methyl methylphosphonate
-
3.3 mM, pH 7, 13% inhibition
methyl phosphate
-
16.7 mM, pH 7, 21% inhibition
Methyl-2-methoxyphosphinylacetate
-
competitive inhibitor vs. acetoacetate
-
Methylmalonate
-
brain 3-hydroxybutyrate dehydrogenase, 0.5 mM 69% inhibition, 0.75 mM 83%, 1 mM 87%, 1.5 mM 3-hydroxybutyrate, liver 3-hydroxybutyrate dehydrogenase, 0.1 mM 37% inhibition, 0.25 mM 41%, 0.5 mM 45%, 1 mM 3-hydroxybutyrate, competitive inhibition
Methylmalonate
-
2.1 mM, 50% inhibition, oxidation
Methylmalonate
-
1.4 mM, 50% inhibition, oxidation, 0.8 mM reduction
Methylmalonate
-
-
MnCl2
Zoogloea ramigera I-16-M
-
1 mM, 50% inhibition
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
NAD+ protects against inhibition
NaCl
-
80-100 mM, 50% inhibition
NAD+
-
substrate inhibition, high concentrations, noncompetitive vs. beta-hydroxybutyrate
NADH
-
substrate inhibition, above 0.1 mM, competitive vs. acetoacetate
NADH
Zoogloea ramigera I-16-M
-
0.15 mM, 48% inhibition
NADH
-
competitive vs. NAD+
NH4Cl
-
80-100 mM, 50% inhibition
oxalate
-
16.7 mM, pH 7, 9% inhibition
p-chloromercuribenzoate
Zoogloea ramigera I-16-M
-
0.1 mM, 100% inhibition
p-chloromercuribenzoate
-
0.001 mM, extremely rapid inhibition, NAD+ and NADH protect against inhibition
p-chloromercuribenzoate
-
enzyme extremely sensitive, NADH and Ca2+ protect
Phenylarsine oxide
-
NAD+ and NADH protect against inhibition
Phenylglyoxal
-
extremely rapid inhibition
Phenylglyoxal
-
-
Propionate
-
5 mM, pH 8.5, 25C, 9% inhibition
pyruvate
Zoogloea ramigera I-16-M
-
4 mM, 5% inhibition
pyruvate
-
16.7 mM, pH 7.0, 22% inhibition
sodium acetonylphosphonate
-
3.3 mM, pH 7, 21% inhibition
sodium monomethyl acetylphosphonate
-
16.7 mM, pH 7, 60% inhibition
sodium monomethylacetonylphosphate
-
16.7 mM, pH 7, 30% inhibition
Sodium sulfide
-
competitive vs. beta-hydroxybutyrate
sodium sulfite
-
uncompetitive vs. NAD+ and acetoacetate, competitive vs. beta-hydroxybutyrate
succinate
Zoogloea ramigera I-16-M
-
10 mM, 12% inhibition
Zn2+
Acidovorax sp.
Q767A0
inhibition and destabilization of the enzyme at 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Zoogloea ramigera I-16-M
-
10 mM, 41% increase
3-hydroxybutyrate
Acidovorax sp.
Q767A0
induces the enzyme when contained in the growth medium
dithiothreitol
Zoogloea ramigera I-16-M
-
10 mM, 31% increase
dithiothreitol
Acidovorax sp.
Q767A0
-
EDTA
Zoogloea ramigera I-16-M
-
0.5 mM, 21% increase
glycerol
Acidovorax sp.
Q767A0
-
KCN
Zoogloea ramigera I-16-M
-
0.1 mM, 37% increase
phosphatidylcholine
-
required for formation of tight and functional complexes of enzyme with NAD+, coenzyme binding strengthens the interaction of the enzyme with phosphatidylcholine
phosphatidylcholine
-
-
phosphatidylcholine
-
-
phosphatidylcholine
-
state of phosphatidylcholine determines nature of activation, noncooperative for soluble phosphatidylcholine, cooperative for bilayer phosphatidylcholine
phosphatidylcholine
Zoogloea ramigera I-16-M
-
-
phosphatidylcholine
-
-
phosphatidylcholine
-
-
phosphatidylcholine
-
-
phosphatidylcholine
-
-
Phospholipids
-
absolutely dependent on
reduced glutathione
Zoogloea ramigera I-16-M
-
10 mM, 38% increase
succinate
Acidovorax sp.
Q767A0
induces the enzyme when contained in the growth medium
Lactate
Acidovorax sp.
Q767A0
induces the enzyme when contained in the growth medium
additional information
A8R3J3, Q2PEN2, Q2PEN3, -
BDH1 is abundant in cells grown on D-fructose, D-glucose, maltose, oxaloacetate, 2-oxoglutarate, L-alanine, L-arginine, L-methionine, poly-3-hydroxybutyrate, and nutrient broth, and poor in cells grown on pyruvate, gluconate, fumarate, L-malate, propionate, and n-butyrate; BDH2 is abundant in cells grown on acetate, ethanol, D-arabinose, D-ribose, oxaloacetate, 2-oxoglutarate, malaete, L-histidine, L-alanine, L-arginine, L-methionine, and poly-3-hydroxybutyrate, and scant in cells grown on pyruvate, n-butyrate, and oleate; BDH3 is produced only in cells grown on 3-hydroxybutyrate or poly-3-hydroxybutyrate as a carbon source. Expression of bdh3 may be coordinately regulated with a gene encoding putative 3-hydroxybutyrate permease
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.34
-
(R)-3-hydroxybutanoate
Q2PEN2, Q2PEN3
30C
0.49
-
(R)-3-hydroxybutanoate
Q2PEN2, Q2PEN3
30C
0.59
-
(R)-3-hydroxybutanoate
-
submitochondrial vesicles
0.6
-
(R)-3-hydroxybutanoate
-
wild type enzyme
0.71
-
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells
1.2
-
(R)-3-hydroxybutanoate
-
-
1.5
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, wild-type enzyme
1.6
-
(R)-3-hydroxybutanoate
-
isoenzyme from heavy mitochondria
1.6
-
(R)-3-hydroxybutanoate
-
pH 8.0, 25C
3.36
-
(R)-3-hydroxybutanoate
-
isoenzyme from light mitochondria
4
-
(R)-3-hydroxybutanoate
-
mutant enzyme H141A
9.1
-
(R)-3-hydroxybutanoate
-
30C, pH 9.0
10
-
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells, C242S mutant, C242 important for substrate binding
10.5
-
(R)-3-hydroxybutanoate
-
25C, pH 9.0
12.6
-
(R)-3-hydroxybutanoate
-
25C, pH 7.5
35
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme H141A
51
-
(R)-3-hydroxybutanoate
-
mutant enzyme Q91A
70
-
(R)-3-hydroxybutanoate
-
mutant enzyme Q133A
78
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme K149R
96
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme Q193A
131
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme Q91A
0.45
-
(R)-3-hydroxybutyrate
Acidovorax sp.
Q767A0
oxidation reaction, pH 8.5, 55C
0.633
-
(R)-3-hydroxybutyrate
-
euthermic state, liver
1.07
-
(R)-3-hydroxybutyrate
-
pH 8.1, 37C
2
-
(R)-3-hydroxybutyrate
-
euthermic state, brain
0.28
-
3-acetylpyridine adenine dinucleotide
-
-
0.00547
-
acetoacetate
-
-
0.146
-
acetoacetate
-
euthermic state, brain
0.149
-
acetoacetate
-
liver, soluble enzyme
0.15
-
acetoacetate
Zoogloea ramigera I-16-M
-
-
0.15
-
acetoacetate
-
euthermic state, liver
0.24
-
acetoacetate
Acidovorax sp.
Q767A0
reduction reaction, pH 5.0, 55C
0.25
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.26
-
acetoacetate
-
-
0.29
-
acetoacetate
-
pH 7.0, 37C
0.312
-
acetoacetate
-
heart, soluble enzyme
0.37
-
acetoacetate
-
wild-type
0.59
-
acetoacetate
-
-
1.1
-
acetoacetate
Q2PEN2, Q2PEN3
30C
1.1
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
1.1
-
acetoacetate
-
mutant T190S
1.3
-
acetoacetate
Q2PEN2, Q2PEN3
30C
1.3
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
1.3
-
acetoacetate
-
mutant L215V
7.7
-
acetoacetate
-
mutant T190C
8.3
-
acetoacetate
-
mutant L215A
8.7
-
acetoacetate
-
cyanylated enzyme
32
-
acetoacetate
-
mutant T190A
0.0391
-
beta-hydroxybutyrate
-
-
0.32
-
beta-hydroxybutyrate
Zoogloea ramigera I-16-M
-
-
0.8
-
beta-hydroxybutyrate
-
-
0.866
-
beta-hydroxybutyrate
-
liver, soluble enzyme
1.05
-
beta-hydroxybutyrate
-
heart 3-hydroxybutyrate dehydrogenase
1.32
-
beta-hydroxybutyrate
-
liver 3-hydroxybutyrate dehydrogenase
1.586
-
beta-hydroxybutyrate
-
heart, soluble enzyme
2.2
-
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
2.3
-
beta-hydroxybutyrate
-
-
2.3
-
beta-hydroxybutyrate
-
-
7.4
-
beta-hydroxybutyrate
-
-
21
-
beta-hydroxybutyrate
-
cyanylated enzyme
200
-
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, thiol group 1 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
260
-
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, thiol group 2 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
0.34
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.49
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.5
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.8
-
D-3-hydroxybutyrate
-
wild-type
0.88
-
D-3-hydroxybutyrate
-
H6-HBDH
1.2
-
D-3-hydroxybutyrate
-
mutant H6-W187Y
1.3
-
D-3-hydroxybutyrate
-
mutant H6-W187F
3.4
-
D-3-hydroxybutyrate
-
mutant L215V
3.7
-
D-3-hydroxybutyrate
-
mutant T190S
9.2
-
D-3-hydroxybutyrate
-
mutant L215A
25
-
D-3-hydroxybutyrate
-
mutant H6-H144A; mutant T190A
30
-
D-3-hydroxybutyrate
-
mutant H6-Q94A
31
-
D-3-hydroxybutyrate
-
mutant H6-K152R
36
-
D-3-hydroxybutyrate
-
mutant T190C
47
-
D-3-hydroxybutyrate
-
mutant H6-Q196A
51
-
D-3-hydroxybutyrate
-
mutant H6-Q196N
61
-
D-3-hydroxybutyrate
-
mutant H6-W257A
65
-
D-3-hydroxybutyrate
-
mutant H6-W257Y
83
-
D-3-hydroxybutyrate
-
mutant H6-Q196E; mutant H6-W257F
84
-
D-3-hydroxybutyrate
-
mutant H6-W187T
100
-
D-3-hydroxybutyrate
-
mutant H6-W187A
0.000445
-
NAD+
-
-
0.057
-
NAD+
Zoogloea ramigera I-16-M
-
-
0.0598
-
NAD+
-
25C, pH 9.0
0.064
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.067
-
NAD+
-
heart, soluble enzyme
0.071
-
NAD+
-
liver, soluble enzyme
0.089
-
NAD+
Acidovorax sp.
Q767A0
oxidation reaction, pH 8.5, 55C
0.1
-
NAD+
Q2PEN2, Q2PEN3
30C
0.1
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.12
-
NAD+
-
mutant H6-K152R; mutant H6-Q196A; mutant H6-Q196E
0.17
-
NAD+
-
H6-HBDH
0.175
-
NAD+
-
-
0.18
-
NAD+
-
23C, pH 8.0, wild-type enzyme
0.19
-
NAD+
-
mutant H6-Q94A
0.2
-
NAD+
-
mutant H6-Q196N
0.21
-
NAD+
-
pH 8.1, 37C
0.21
-
NAD+
-
isoenzyme from heavy mitochondria
0.21
-
NAD+
-
pH 8.0, 25C
0.21
-
NAD+
-
mutant H6-W187Y
0.238
-
NAD+
-
euthermic state, liver
0.24
-
NAD+
-
liver 3-hydroxybutyrate dehydrogenase
0.24
-
NAD+
-
mutant H6-W187F; wild-type
0.27
-
NAD+
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
0.27
-
NAD+
-
23C, pH 8.0, mutant enzyme Q193A
0.28
-
NAD+
-
23C, pH 8.0, mutant enzyme H141A
0.29
-
NAD+
-
mutant L215V
0.31
-
NAD+
Q2PEN2, Q2PEN3
30C
0.31
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.35
-
NAD+
-
mutant H6-H144A
0.36
-
NAD+
-
heart 3-hydroxybutyrate dehydrogenase
0.38
-
NAD+
-
23C, pH 8.0, mutant enzyme K149R
0.39
-
NAD+
-
isoenzyme from light mitochondria
0.49
-
NAD+
-
mutant H6-W257F
0.51
-
NAD+
-
23C, pH 8.0, mutant enzyme Q91A
0.53
-
NAD+
-
enzyme expressed in SF9 cells
0.55
-
NAD+
-
-
0.69
-
NAD+
-
mutant T190C
0.71
-
NAD+
-
mutant T190S
0.74
-
NAD+
-
mutant H6-W257Y
0.76
-
NAD+
-
mutant H6-W187A
0.8
-
NAD+
-
enzyme expressed in SF9 cells, C242S mutant
0.88
-
NAD+
-
mutant H6-W187T
0.902
-
NAD+
-
cyanylated enzyme
0.95
-
NAD+
-
submitochondrial vesicles
0.95
-
NAD+
-
-
0.95
-
NAD+
-
mutant H6-W257A
1.187
-
NAD+
-
euthermic state, brain
1.5
-
NAD+
-
mutant L215A
2.2
-
NAD+
-
mutant T190A
0.01
-
NADH
-
wild-type
0.014
-
NADH
-
liver, soluble enzyme
0.015
-
NADH
Zoogloea ramigera I-16-M
-
-
0.02
-
NADH
-
mutant T190S
0.029
-
NADH
-
heart, soluble enzyme
0.029
-
NADH
Acidovorax sp.
Q767A0
reduction reaction, pH 5.0, 55C
0.03
-
NADH
-
mutant L215V
0.058
-
NADH
-
euthermic state, brain
0.074
-
NADH
-
euthermic state, liver
0.08
-
NADH
-
-
0.091
-
NADH
-
-
0.1
-
NADH
-
mutant T190A
0.164
-
NADH
-
cyanylated enzyme
0.24
-
NADH
Q2PEN2, Q2PEN3
30C
0.24
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.27
-
NADH
-
pH 7.0, 37C
0.32
-
NADH
Q2PEN2, Q2PEN3
30C
0.32
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
0.5
-
NADH
-
mutant L215A
1.1
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
1.5
-
NADH
-
mutant T190C
388
-
L-threonine
-
-
additional information
-
additional information
-
dissociation constants for the cofactors and reaction kinetics at different physiological states in liver and brain
-
additional information
-
additional information
-
dissociation constants
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13
-
(R)-3-hydroxybutanoate
-
mutant enzyme H141A
167
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme H141A
180
-
(R)-3-hydroxybutanoate
Q2PEN2, Q2PEN3
30C
215
-
(R)-3-hydroxybutanoate
-
mutant enzyme Q133A
310
-
(R)-3-hydroxybutanoate
Q2PEN2, Q2PEN3
30C
333
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme Q193A
404
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme K149R
411
-
(R)-3-hydroxybutanoate
-
mutant enzyme Q91A
432
-
(R)-3-hydroxybutanoate
-
wild type enzyme
1382
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, wild-type enzyme
1390
-
(R)-3-hydroxybutanoate
-
23C, pH 8.0, mutant enzyme Q91A
4.5
-
acetoacetate
-
mutant T190A
5.1
-
acetoacetate
-
mutant T190C
30
-
acetoacetate
-
mutant L215A
87
-
acetoacetate
-
mutant L215V
100
-
acetoacetate
Q2PEN2, Q2PEN3
30C
100
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
110
-
acetoacetate
Q2PEN2, Q2PEN3
30C
110
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
120
-
acetoacetate
-
wild-type
125
-
acetoacetate
-
mutant T190S
150
-
acetoacetate
A8R3J3, Q2PEN2, Q2PEN3, -
-
6.1
-
D-3-hydroxybutyrate
-
mutant T190C
6.7
-
D-3-hydroxybutyrate
-
mutant H6-W257A
7.2
-
D-3-hydroxybutyrate
-
mutant H6-W187T
12
-
D-3-hydroxybutyrate
-
mutant H6-W257Y
21
-
D-3-hydroxybutyrate
-
mutant H6-H144A
22
-
D-3-hydroxybutyrate
-
mutant H6-Q196N; mutant T190A
29
-
D-3-hydroxybutyrate
-
mutant H6-W187A
70
-
D-3-hydroxybutyrate
-
mutant L215A
83
-
D-3-hydroxybutyrate
-
mutant H6-Q196E
88
-
D-3-hydroxybutyrate
-
mutant H6-W257F
99
-
D-3-hydroxybutyrate
-
mutant H6-Q196A
110
-
D-3-hydroxybutyrate
-
mutant H6-K152R
140
-
D-3-hydroxybutyrate
-
mutant H6-Q94A
180
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
180
-
D-3-hydroxybutyrate
-
mutant H6-W187Y
310
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
310
-
D-3-hydroxybutyrate
-
H6-HBDH; mutant H6-W187F
370
-
D-3-hydroxybutyrate
-
wild-type
435
-
D-3-hydroxybutyrate
-
mutant L215V
500
-
D-3-hydroxybutyrate
A8R3J3, Q2PEN2, Q2PEN3, -
-
705
-
D-3-hydroxybutyrate
-
mutant T190S
87
-
NAD+
Q2PEN2, Q2PEN3
30C
87
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
340
-
NAD+
Q2PEN2, Q2PEN3
30C
340
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
360
-
NAD+
A8R3J3, Q2PEN2, Q2PEN3, -
-
58
-
NADH
Q2PEN2, Q2PEN3
30C
58
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
280
-
NADH
Q2PEN2, Q2PEN3
30C
280
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
740
-
NADH
A8R3J3, Q2PEN2, Q2PEN3, -
-
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
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.02
-
-
cofactor 3-acetylpyridine adenine dinucleotide
0.038
-
-
brain 3-hydroxybutyrate dehydrogenase, mitochondrial extracts
0.07
-
-
heart 3-hydroxybutyrate dehydrogenase, mitochondrial extracts; kidney 3-hydroxybutyrate dehydrogenase, mitochondrial extracts
0.09
-
-
purified enzyme
0.17
-
-
solubilized apo-3-hydroxybutyrate dehydrogenase, reconstituted with phosphatidylcholine/phosphatidylethanolamine/diphosphatidylglycerol, 5/4/1
0.22
-
-
apo-3-hydroxybutyrate dehydrogenase, reconstituted with phosphatidylcholine/phosphatidylethanolamine/diphosphatidylglycerol, 5/4/1
0.36
-
-
liver 3-hydroxybutyrate dehydrogenase, mitochondrial extracts
0.5
-
-
enzyme expressed in SF9 cells, S24T mutatant
0.52
-
-
submitochondrial vesicles, membrane bound enzyme
0.54
-
-
submitochondrial vesicles
0.6
-
-
enzyme expressed in SF9 cells, M92V mutatant
0.63
-
-
enzyme expressed in SF9 cells, membrane bound
0.8
-
-
enzyme expressed in SF9 cells, C242S mutatant
1.15
-
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with microsomal membranes
1.26
-
-
brain 3-hydroxybutyrate dehydrogenase, mitochondrial extracts
1.275
-
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial inner membranes
2.7
-
-
submitochondrial vesicles
23.8
-
-
-
41
-
-
purified enzyme, reconstituted with mitochondrial phospholipids
72
-
Acidovorax sp.
Q767A0
purified native enzyme
85
-
Q2PEN2, Q2PEN3
-
86
-
-
purified enzyme, reconstituted with mitochondrial phospholipids
91
-
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial phospholipids
100
-
-
-
123
-
Zoogloea ramigera I-16-M
-
-
145
-
-
heart 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial phospholipids
180
-
Q2PEN2, Q2PEN3
-
300
-
Acidovorax sp.
Q767A0
purified recombinant enzyme
360
-
Q2PEN2, Q2PEN3
recombinant enzyme
450
-
Q2PEN2, Q2PEN3
recombinant enzyme
1200
-
A8R3J3, Q2PEN2, Q2PEN3, -
purified BDH3
additional information
-
-
0.0018 mM/min/g wet weight
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
5
Acidovorax sp.
Q767A0
reduction reaction
5
-
Q2PEN2, Q2PEN3
reduction
6
6.5
-
reduction of acetoacetate
6
-
-
reduction reaction
6.4
7
-
reduction of acetoacetate
6.5
-
Q2PEN2, Q2PEN3
reduction
6.8
-
-
acetoacetate reduction
7
-
-
reduction of acetoacetate
7
-
-
approximately, reduction reaction
7
-
-
reduction
7
-
-
assay at
7.4
-
-
assay at
7.5
-
Q2PEN2, Q2PEN3
oxidation
8
-
Zoogloea ramigera I-16-M
-
oxidation of beta-hydroxybutyrate
8
-
-
approximately, oxidation reaction
8
-
-
isoenzyme from heavy and light mitochondria
8.4
-
-
oxidation of beta-hydroxybutyrate
8.5
-
-
oxidation of beta-hydroxybutyrate
8.5
-
Acidovorax sp.
Q767A0
oxidation reaction
8.5
-
-
dehydrogenation
8.6
-
-
oxidation of (R)-3-hydroxybutanoate
9
-
Q2PEN2, Q2PEN3
oxidation
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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
high activity
Manually annotated by BRENDA team
-
gastric glandular mucosa
Manually annotated by BRENDA team
additional information
-
during the cold adaptation process, the prehibernating stage, the enzyme activity is decreased compared to euthermic state, in the hibernation state, the rate of acetoacetate reduction is increased in liver, while the oxidation of D-beta-hydroxybutyrate is increased in brain
Manually annotated by BRENDA team
additional information
-
the enzyme is localized in poly(3-hydroxybutyrate) granules, co-localization with acetoacetyl-CoA thiolase and PHB synthase, overview
Manually annotated by BRENDA team
additional information
-
the physiological states of the organism, i.e. euthermic, prehibernating, and hibernating, vary between in terms of ketone bodies, glucose and lipid levels, the enzyme might lead an important conformational change depending on the state, overview, enzyme expression is increased in hibernating state
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
located on the matrix face of the inner membrane
Manually annotated by BRENDA team
-
located on the matrix face of the inner membrane
Manually annotated by BRENDA team
-
located on the matrix face of the inner membrane
Manually annotated by BRENDA team
-
beta-hydroxybutyrate dehydrogenase from heavy and light mitochondria are isoforms
Manually annotated by BRENDA team
-
light and heavy mitochondria, enzyme expression and activity is increased in heavy mitochondria in hibernating state, overview
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
68000
-
-
nondenaturing PAGE
89000
-
-
gel filtration
106000
-
-
submitochondrial vesicles, radiation inactivation
110000
-
Acidovorax sp.
Q767A0
gel filtration
110000
-
Q2PEN2, Q2PEN3
gel filtration; gel filtration
112000
-
Zoogloea ramigera I-16-M
-
gel filtration
119000
-
-
reconstituted enzyme, radiation inactivation, irradiation leads to loss of activity and fragmentation
120000
-
-
gel filtration
132000
-
-
gel filtration
140000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 67000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
A8R3J3, Q2PEN2, Q2PEN3, -
x * 28000, SDS-PAGE, BDH3
tetramer
-
alpha4, 4 * 39000, SDS-PAGE
tetramer
-
alpha4, 4 * 33117, mature protein, calculated from deduced amino acid sequence; alpha4, 4 * 38000, preprotein, calculated from deduced amino acid sequence
tetramer
-
alpha4, 4 * 27000, sedimentation equilibrium; alpha4, 4 * 31000, SDS-PAGE
tetramer
-
alpha4, 4 * 32000, SDS-PAGE
tetramer
-
alpha4, 4 * 31500, SDS-PAGE
tetramer
-
alpha4, 4 * 23000, SDS-PAGE
tetramer
Zoogloea ramigera I-16-M
-
alpha4, 4 * 28000, SDS-PAGE
tetramer
Acidovorax sp.
Q767A0
4 * 27000, SDS-PAGE
tetramer
Q2PEN2, Q2PEN3
4 * 31000, SDS-PAGE; 4 * 31000, SDS-PAGE
tetramer
-
x-ray crystallography
tetramer
-
4 x 29000, SDS-PAGE
tetramer
Ralstonia pickettii T1
-
4 * 31000, SDS-PAGE; 4 * 31000, SDS-PAGE
-
?
Ralstonia pickettii T1
-
x * 28000, SDS-PAGE, BDH3
-
additional information
-
secondary and tertiary enzyme structure analysis, overview
additional information
-
three-dimensional structure modelling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallization of the enzyme in the apo form and in the holo form with acetate as a substrate analogue, method screening, mother liquor consists of 30% w/v PEG 4000, 0.2 M sodium acetate trihydrate and 100 mM Tris-HCl, pH 8.5, at 20C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular-replacement method
-
in the presence of the substrate D-3-hydroxybutyrate and the cofactor NAD+ at the optimum pH for the catalytic reaction. At 277 and 293 K using the hanging-drop vapour-diffusion method, to 2.3 A resolution. Structure is isomorphous to that of the complex with the substrate analogue acetate
-
sitting drop vapor diffusion method at 20C, structure determined at a resolution of 1.8 A in complex with NAD(H)
-
crystals of ternary complex of HBDH-NAD+-L-3-hydroxybutyrate and the binary complex of HBDH-NAD+. The former structure shows a closed-form conformation, which is considered an active form for catalysis, while the latter stays mostly in a open-form conformation. Crystals of mutants T190S and T190A
-
hanging-drop vapor-diffusion method, ligand-free enzyme and enzyme-NAD+ complex, 2.0 A resolution
-
hanging-drop vapour-diffusion method using PEG 3000 as a precipitating agent. The crystals belong to the orthorhombic group P2(1)2(1)2, with unit-cell parameters a = 64.3, b = 99.0, c = 110.2 A. The crystals are most likely to contain two tetrameric subunits in the asymmetric unit
Q5KST5
hanging drop vapour diffusion method with 17-20% polyethylene glycol 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2 and 10 mM acetoacetate; recombinant enzyme, hanging drop vapor diffusion method, 0.003 ml of HBDH, 10 mg/ml, is mixed with an equal volume of crystallization buffer containing 17-20% PEG 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2, and 10 mM acetoacetate, room temperature/22C, three different crystal forms, X-ray diffraction structure determination and analysis at resolutions between 1.9 and 2.1 A
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
37
-
stable at, 30% remaining activity after 40 min at 37C, oxidation reaction
0
40
Acidovorax sp.
Q767A0
-
0
45
-
stable at 0C and 25C for 90 min, 18% activity after 90 min at 45C, activity restored after 60 min at 37C, loss of activity at 60C
37
-
-
75% activity after 30 min in buffer containing 1 mM Ca2+, 46% with 1 mM MnCl2
37
-
-
loss of 70% activity after 15 min, 0.24 mg protein/ml, Ca2+ and Mn2+ stabilize enzyme
45
-
-
25% remaining activity after 20 min, oxidation reaction
60
-
-
28% remaining activity
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native by 3 chromatographic steps, recombinant from Escherichia coli in 2chromatographic steps
Acidovorax sp.
Q767A0
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant enzyme from Escherichia coli strain DH1 by anion exchange chromatography, hydrophobic interaction chromatography using a gradient of 1-20% ammonium sulfate, and ultrafiltration
-
ammonium sulfate precipitation, DEAE-Sephadex, Sephadex G-200
-
ammonium sulfate, acid precipitation, DEAE-Sepharose, glass beads
-
phospholipase A2 treatment, controlled-pore glass beads
-
about 1000fold, to homogeneity from liver mitochondrial membranes by solubilization with Triton X-100, DEAE-ion-exchange chromatography and phenyl-resin chromatography
-
ammonium sulfate precipitation, DEAE-cellulose
-
DEAE-cellulose, Matrex gel blue A, Sephadex G-200, chromatofocusing
-
native enzyme by ammonium sulfate fractionation and affinity chromatography
-
recombinant
-
wild-type and mutants purified by metal chelating affinity chromatography followed by ion-exchange chromatography
-
charge-controlled hydrophobic chromatography and Sephadex G-100 gel filtration
-
;
Q2PEN2, Q2PEN3
BDH3 partially purified from bdh2 mutant by three steps of column chromatography. Gene product of bdh3 expressed in Escherichia coli purified with 100% yield by two steps of column chromatography
A8R3J3, Q2PEN2, Q2PEN3, -
phospholipase A2 treatment, controlled-pore glass beads
-
affinity chromatography on two triazine dyes
-
protamine sulfate precipitation, Sephacryl S-400, S200, DEAE-Sepharose
-
ammonium sulfate, DEAE-Sepharose, 60C, 10 min, hydroxylapatite, octyl-Sepharose, Sephadex G-200, DEAE-Sepharose
Zoogloea ramigera I-16-M
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
Acidovorax sp.
Q767A0
enzyme expression in Escherichia coli strain DH1
-
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
functional co-expression with acetoacetyl-CoA thiolase and PHB synthase in Escherichia coli, recombinant production of poly(3-hydroxybutanoate) granules, overview
-
His-tagged 3-hydroxybutyrate dehydrogenase, expressed in Escherichia coli
-
mature form, expressed in Spodoptera frugiperda, SF9 cells
-
DNA and amino acid sequence determination and analysis
-
efficiently expressed in Escherichia coli cells harboring pHBDH11
-
wild-type and mutants expressed in Escherichia coli XL1Blue harbouring pHBDH11. Wild-type HBDH and mutants containing an N-terminal His-tag expressed in Escherichia coli XL1Blue using pQE30 as a vector
-
enzyme expression in Escherichia coli strain XL-1 Blue; expressed in Escherichia coli XL1-Blue cells
-
expression in Escherichia coli
-
BDH3 expressed in Escherichia coli BLR (DE3)/pLysS harboring pETT13
A8R3J3, Q2PEN2, Q2PEN3, -
expression in Escherichia coli; expression in Escherichia coli
Q2PEN2, Q2PEN3
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H144L/W187F
-
site-directed mutagenesis, the mutant shows activity with levulinnic acid, in contrast to the wild-type enzyme, and is engineered for production of 4-hydroxyvaleric acid, molecular docking simulation, overview
C242S
-
PCR derived cDNA clone
M92V
-
PCR derived cDNA clone
S24T
-
PCR derived cDNA clone
H144A
-
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
K152A
-
no activity
K152E
-
very low activity
K152Q
-
very low activity
K152R
-
retains a significant level of activity
L215A
-
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
L215V
-
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Q196A
-
kcat/Km value is 0.6% that of the wild-type
Q196E
-
substantially reduced activity
Q196N
-
substantially reduced activity
Q94A
-
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
T190A
-
activity decreases to 0.1% that of the wild-type enzyme
T190C
-
decreased activity
T190S
-
retains 37% of the activity
W187A
-
very low activity
W187F
-
shows significant activity levels, 65% that of the wild-type enzyme
W187T
-
shows faint activity
W187Y
-
shows significant activity levels, 41% that of the wild-type enzyme
W257A
-
no activity
W257F
-
shows low activity levels, 2% that of the wild-type enzyme
W257Y
-
shows low activity levels, 1% that of the wild-type enzyme
Y155F
-
no activity
H141A
-
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 12.9fold lower than wild-type enzyme
H141A
-
strongly decreased activity
K149A
-
inactive mutant enzyme
K149R
-
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
L149A
-
inactive
Q133A
-
decreased activity
Q193A
-
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
Q91A
-
kcat/KM for (R)-3-hydroxybutanoate is 83.7fold lower than wild-type value, kcat/Km for NAD+ is 2.8fold lower than wild-type enzyme
Q91A
-
decreased activity
additional information
A8R3J3, Q2PEN2, Q2PEN3, -
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
Ralstonia pickettii T1
-
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
-
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