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
1.1.1.31
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyisobutyrate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
valine degradation I
-
Valine, leucine and isoleucine degradation
-
SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-HIBADH
-
-
3-HIBADH
Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
-
-
3-hydroxyisobutyrate dehydrogenase
-
cf. EC1.1.1.59, wide substrate specificity (hydroxyacid derivatives)
3-hydroxyisobutyrate dehydrogenase
Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
cf. EC1.1.1.59, wide substrate specificity (hydroxyacid derivatives)
-
beta-hydroxyisobutyrate dehydrogenase
-
-
-
-
HIBADH
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-39-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; ATCC 14579; MmsB gene
-
-
Manually annotated by BRENDA team
Bacillus cereus ATCC14579
MmsB gene
-
-
Manually annotated by BRENDA team
IFO 0750
-
-
Manually annotated by BRENDA team
IFO 0750; IFO 1542
-
-
Manually annotated by BRENDA team
Corynebacterium hydrocarbons
-
-
-
Manually annotated by BRENDA team
Endomyces reessii
-
-
-
Manually annotated by BRENDA team
Nocardia lyena
-
-
-
Manually annotated by BRENDA team
Pseudomonas dacunhae
-
-
-
Manually annotated by BRENDA team
strain E23, recombinant enzyme expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
Pseudomonas putida E23
E23
-
-
Manually annotated by BRENDA team
Pseudomonas putida E23
strain E23, recombinant enzyme expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
Wistar rats
-
-
Manually annotated by BRENDA team
Trichosporon aculeatum
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
3-hydroxyisobutyrate dehydrogenase is a key enzyme for the metabolism of valine and some keto-bodies. It can catalyze reversible conversion of 3-hydroxyisobutyrate to methylmalonate semialdehyde
physiological function
-
3-hydroxyisobutyrate dehydrogenase is one of the critical enzymes generating glucose by metabolizing amino acids in the gluconeogenesis pathway. It participates in valine, leucine, and isoleucine degradation and is a central metabolic enzyme in the valine catabolic pathway. The enzyme plays an important role in regulating sperm motility and may serve as a novel sperm-motility marker
physiological function
Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
3-hydroxyisobutyrate dehydrogenase is a key enzyme for the metabolism of valine and some keto-bodies. It can catalyze reversible conversion of 3-hydroxyisobutyrate to methylmalonate semialdehyde
-
evolution
-
3-hydroxyisobutyrate dehydrogenase belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donors with NAD+ or NADP+ acceptors
additional information
-
enzyme activity of HIBADH in spermatozoa from patients with asthenozoospermia is reduced compared to controls
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-methyl-D,L-serine + NAD+
?
show the reaction diagram
Pseudomonas putida, Pseudomonas putida E23
-
-
-
-
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
-
-
-
r
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
-
-
-
r
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-hydroxypropionate + NAD(P)+
?
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
is more active with NADP+ than NAD+
-
-
?
3-hydroxypropionate + NAD+
?
show the reaction diagram
-
-
-
-
?
3-hydroxypropionate + NAD+
?
show the reaction diagram
Pseudomonas putida, Pseudomonas putida E23
-
-
-
-
?
3-hydroxypropionate + NAD+
malonate semialdehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
3-hydroxypropionate + NADP+
malonate semialdehyde + NADPH + H+
show the reaction diagram
-
-
-
-
r
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
Pseudomonas aeruginosa, Pseudomonas dacunhae, Endomyces reessii, Nocardia lyena
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
strain IFO 1542
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
strain IFO 0750
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
-
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
-
-
-
-
-
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
r
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
Micrococcus luteus, Rhodotorula mucilaginosa, Micrococcus flavus, Corynebacterium hydrocarbons, Tsukamurella paurometabola, Trichosporon aculeatum
-
-
-
-
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
Pseudomonas putida E23
-
-
-
-
?
L-3-hydroxyisobutyrate + NAD+
3-oxoisobutyrate + NADH
show the reaction diagram
Pseudomonas putida, Pseudomonas putida E23
Q59477
high stereospecificity
-
-
r
L-serine + NAD+
?
show the reaction diagram
Pseudomonas putida, Pseudomonas putida E23
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in the irreversible degradative pathway for the carbon skeleton of valine and the other branched-chain amino acids
-
-
-
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59, wide substrate specificity of the 3-HIBADH
-
-
-
additional information
?
-
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59, wide substrate specificity of the 3-HIBADH
-
-
-
additional information
?
-
Bacillus cereus ATCC14579
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59, wide substrate specificity of the 3-HIBADH
-
-
-
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
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
-
-
-
r
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
-
-
-
r
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
Pseudomonas aeruginosa, Pseudomonas dacunhae, Endomyces reessii, Nocardia lyena
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
strain IFO 1542
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
strain IFO 0750
-
-
?
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
r
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
Micrococcus luteus, Rhodotorula mucilaginosa, Micrococcus flavus, Corynebacterium hydrocarbons, Tsukamurella paurometabola, Trichosporon aculeatum
-
-
-
-
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
show the reaction diagram
Pseudomonas putida E23
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in the irreversible degradative pathway for the carbon skeleton of valine and the other branched-chain amino acids
-
-
-
additional information
?
-
Bacillus cereus, Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD(P)+
-
is more active with NADP+ than NAD+
additional information
-
3-HIBADH is more active with NADP+ than NAD+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
has no metal ion requirement, MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4 have no effect; no metal ion requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(R)-3-hydroxy-2-methylpropanoate
-
competitive inhibitor of the S-isomer
NADH
-
product inhibition
p-chloromercuribenzoate
-
-
Zn2+
-
inhibits at 0.2 mM
ZnCl2
-
0.2 mM, 60% inhibition; inhibits approximately 60% of 3-HIBADH activity at 0.2 mM but shows no effect at 0.005 mM
iodoacetate
-
-
additional information
-
is not inhibited by 1-propanol, lactate potassium, malate potassium, malonate potassium, acetaldehyde, ethanol, and glycerin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
ethylene glycol tetraacetic acid or EDTA (all at 0.005 and 0.2 mM) do not affect 3-HIBADH activity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
83
-
2-methyl-D,L-serine
-
-
0.12
-
3-hydroxyisobutyric acid
-
-
16.8
-
3-hydroxypropionate
-
; pH 8.5, 37C, KM-value for 3-hydroxyisobutyrate is approximately 20fold lower
18
-
3-hydroxypropionate
-
-
0.1
-
D,L-3-hydroxyisobutyrate
-
-
0.12
-
D,L-3-hydroxyisobutyrate
-
-
1.25
-
D-3-hydroxyisobutyrate
-
-
0.056
-
L-3-hydroxyisobutyrate
-
wild type, NAD as cofactor
0.061
-
L-3-hydroxyisobutyrate
-
-
0.104
-
L-3-hydroxyisobutyrate
-
wild type, NADP as cofactor
0.11
-
L-3-hydroxyisobutyrate
-
mutant D33R, NADP as cofactor
0.112
-
L-3-hydroxyisobutyrate
-
mutant D33R, NAD as cofactor
0.12
-
L-3-hydroxyisobutyrate
-
-
0.37
-
L-3-hydroxyisobutyrate
-
-
44
-
L-serine
-
-
0.022
-
NAD+
-
wild type
0.054
-
NAD+
-
-
0.5
-
NAD+
-
-
1.24
-
NAD+
-
mutant D33R
2.4
-
NAD+
-
; pH 8.5, 37C
0.24
-
NADP+
-
mutant D33R
0.25
-
NADP+
-
; pH 8.5, 37C
0.96
-
NADP+
-
wild type
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.49
-
(R)-3-Hydroxyisobutyrate
-
-
7.1
-
(S)-3-hydroxyisobutyrate
-
-
0.21
-
3-hydroxypropionate
-
; pH 8.5, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0125
-
3-hydroxypropionate
-
pH 8.5, 37C
34987
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0037
-
-
index patient with 3-hydroxyisobutyric acidia
0.0042
-
-
patient 2 with 3-hydroxyisobutyric acidia
0.0046
-
-
patient 1 with 3-hydroxyisobutyric acidia
0.091
-
-
homogenate
8.7
-
-
purified enzyme
8.77
-
-
pH 8.5, 37C; purified enzyme, pH 8.5, 37C
20.9
-
-
-
36.1
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
assay at
8.8
9
-
; oxidation of 3-hydroxypropionate by 3-HIBADH
9
10.5
-
-
9
-
-
-
10
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10
-
; oxidation of 3-hydroxypropionate by 3-HIBADH
7
11
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
37
-
-
; assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
45
-
shows more than 90% of its optimized activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
astroglia-rich primary culture from neonatal rats
Manually annotated by BRENDA team
-
astroglia-rich primary culture from neonatal rats
Manually annotated by BRENDA team
-
elongating, elongated, and mature sperm
Manually annotated by BRENDA team
additional information
-
cell type-specific enzyme expression analysis, immunofluorescence labeling, overview
Manually annotated by BRENDA team
additional information
-
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis, quantitative RT-PCR expression analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular enzyme expression analysis, overview
-
Manually annotated by BRENDA team
additional information
-
the enzyme is located at the mid-piece (a specialized development from the mitochondria) of elongating, elongated, and mature sperm
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
gel filtration
74000
-
-
gel filtration
80000
-
-
gel filtration
80000
-
-
-
120000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q59477
x * 30280, deduced from gene sequence, x * 30300, SDS-PAGE
?
-
x * 32000, SDS-PAGE
?
Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
x * 32000, SDS-PAGE
-
?
Pseudomonas putida E23
-
x * 30280, deduced from gene sequence, x * 30300, SDS-PAGE
-
homodimer
-
alpha2, 2 * 34000, SDS-PAGE
homodimer
-
alpha2, 2 * 40000, SDS-PAGE
tetramer
-
alpha4, 4 * 30000, SDS-PAGE
tetramer
Pseudomonas putida E23
-
alpha4, 4 * 30000, SDS-PAGE
-
additional information
-
hydroxybutyrate dehydrogenase and 3-hydroxyisobutyrate dehydrogenase activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
powdered ammonium sulfate is added to the enzyme solution until it becomes slightly turbid, after 4 days crystallization is complete
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
7.3
-
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
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 ACCESSION NO.
LITERATURE
-20C, 50 mM Tris-HCl buffer, pH 8.5, 2 mM EDTA, 2 mM DTT, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D33R
-
higher affinity to cofactor NADP+ than to natural cofactor NAD+
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
3-HIBADH may play a role in biosynthesis of 3-hydroxypropionate as a biological source
additional information
Bacillus cereus ATCC 14579, Bacillus cereus ATCC14579
-
3-HIBADH may play a role in biosynthesis of 3-hydroxypropionate as a biological source
-