Information on EC 1.1.1.31 - 3-hydroxyisobutyrate dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.31
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyisobutyrate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-valine degradation I
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Metabolic pathways
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valine metabolism
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Valine, leucine and isoleucine degradation
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-39-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; ATCC 14579; MmsB gene
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-
Manually annotated by BRENDA team
Bacillus cereus ATCC14579
MmsB gene
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Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Corynebacterium hydrocarbons
-
-
-
Manually annotated by BRENDA team
Endomyces reessii
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Nocardia lyena
-
-
-
Manually annotated by BRENDA team
Pseudomonas dacunhae
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Trichosporon aculeatum
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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3-hydroxyisobutyrate dehydrogenase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ acceptors
physiological function
additional information
-
enzyme activity of HIBADH in spermatozoa from patients with asthenozoospermia is reduced compared to controls
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methyl-D,L-serine + NAD+
?
show the reaction diagram
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
show the reaction diagram
3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
3-hydroxyisobutyric acid + NAD+
methylmalonic semialdehyde + NADH
show the reaction diagram
-
-
-
-
r
3-hydroxypropanoate + NAD(P)+
?
show the reaction diagram
3-hydroxypropanoate + NAD+
?
show the reaction diagram
3-hydroxypropanoate + NAD+
malonate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
show the reaction diagram
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-
-
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r
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
L-3-hydroxyisobutyrate + NAD+
3-oxoisobutyrate + NADH
show the reaction diagram
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
L-serine + NAD+
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
show the reaction diagram
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
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is more active with NADP+ than NAD+
additional information
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3-HIBADH is more active with NADP+ than NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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has no metal ion requirement, MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4 have no effect; no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-3-hydroxy-2-methylpropanoate
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competitive inhibitor of the S-isomer
iodoacetate
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NADH
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product inhibition
p-chloromercuribenzoate
Zn2+
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inhibits at 0.2 mM
ZnCl2
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0.2 mM, 60% inhibition; inhibits approximately 60% of 3-HIBADH activity at 0.2 mM but shows no effect at 0.005 mM
additional information
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is not inhibited by 1-propanol, lactate potassium, malate potassium, malonate potassium, acetaldehyde, ethanol, and glycerin
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ethylene glycol tetraacetic acid or EDTA (all at 0.005 and 0.2 mM) do not affect 3-HIBADH activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
83
2-methyl-D,L-serine
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0.12
3-hydroxyisobutyric acid
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16.8 - 18
3-hydroxypropionate
0.1 - 0.12
D,L-3-hydroxyisobutyrate
1.25
D-3-hydroxyisobutyrate
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0.056 - 0.37
L-3-hydroxyisobutyrate
44
L-serine
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0.022 - 2.4
NAD+
0.24 - 0.96
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.49
(R)-3-Hydroxyisobutyrate
Oryctolagus cuniculus
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7.1
(S)-3-hydroxyisobutyrate
Oryctolagus cuniculus
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0.21
3-hydroxypropionate
Bacillus cereus
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; pH 8.5, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125
3-hydroxypropionate
Bacillus cereus
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pH 8.5, 37C
1632
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0037
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index patient with 3-hydroxyisobutyric acidia
0.0042
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patient 2 with 3-hydroxyisobutyric acidia
0.0046
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patient 1 with 3-hydroxyisobutyric acidia
0.091
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homogenate
8.7
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purified enzyme
8.77
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pH 8.5, 37C; purified enzyme, pH 8.5, 37C
20.9
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
8.8 - 9
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; oxidation of 3-hydroxypropionate by 3-HIBADH
9 - 10.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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; oxidation of 3-hydroxypropionate by 3-HIBADH
7 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
37
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; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 45
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shows more than 90% of its optimized activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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astroglia-rich primary culture from neonatal rats
Manually annotated by BRENDA team
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astroglia-rich primary culture from neonatal rats
Manually annotated by BRENDA team
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elongating, elongated, and mature sperm
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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gel filtration
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
additional information
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hydroxybutyrate dehydrogenase and 3-hydroxyisobutyrate dehydrogenase activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
powdered ammonium sulfate is added to the enzyme solution until it becomes slightly turbid, after 4 days crystallization is complete
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.3
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286551
5.7 - 9.3
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286551
7 - 11.5
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286551
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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enzyme activity is not decreased during preincubation at 45C within 30 min, but preincubation at 55C in 3 min can significantly denaturate and deactivate the enzyme; stable at 45C for 30 min, about 40% activity after 3 min at 55C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM Tris-HCl buffer, pH 8.5, 2 mM EDTA, 2 mM DTT, 50% glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
96fold purified at 4C by ammonium sulfate fractionation and gel filtration; ammonium sulfate precipitation, hydrophobic interaction chromatography (Phenyl-Sepharose), anion exchange chromatography; native enzyme 100fold by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography
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affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21 (DE3); MmsB gene, overexpression in Escherichia coli strain BL21, subcloning in strain DH5alpha; pEB81 recombinant vector introduced into Escherichia coli BL21 to overexpress 3-HIBADH protein
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expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D33R
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higher affinity to cofactor NADP+ than to natural cofactor NAD+
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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