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Information on EC 1.1.1.31 - 3-hydroxyisobutyrate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.31
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.31 3-hydroxyisobutyrate dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
3-hydroxyisobutyrate dehydrogenase, hibadh, hibdh, 3hibdh-iv, beta-hydroxyisobutyrate dehydrogenase, athdh1, 3-hydroxyisobutyric acid dehydrogenase, 3-hibadh, 3hibdhi, at4g20930, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-HIBADH
3-hydroxyisobutyrate dehydrogenase
3-hydroxyisobutyrate dehydrogenase-I
3-hydroxyisobutyric acid dehydrogenase
3HIBDH-IV
3HIBDHI
beta-hydroxyisobutyrate dehydrogenase
-
-
-
-
HIBADH
3-hydroxyisobutyrate dehydrogenase
-
cf. EC1.1.1.59, wide substrate specificity (hydroxyacid derivatives)
3-hydroxyisobutyrate dehydrogenase
-
cf. EC1.1.1.59, wide substrate specificity (hydroxyacid derivatives)
-
HIBADH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-2-methylpropanoate + NAD+ = 2-methyl-3-oxopropanoate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-valine degradation I
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-39-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
Substrates: 100% activity
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-beta-hydroxyisobutyrate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-methyl-3-hydroxy-2-methylpropionate + NAD+
?
Substrates: 1.2% activity compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxyisobutyric acid + NAD+
methylmalonic semialdehyde + NADH
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NAD+
malonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NADP+
malonate semialdehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropionate + NAD+
3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxypropionate + NAD+
malonate semialdehyde + NADH + H+
Substrates: 13% activity compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D-3-hydroxyisobutyrate + NAD+
(S)-methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
DL-3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
(S)-methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
methylmalonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
methyl (2S)-3-hydroxy-2-methylpropanoate + NAD+
methyl (2S)-2-methyl-3-oxopropanoate + NADH + H+
(R)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: 2% activity compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(R)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(R)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: the enzyme is very specific to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate and prefers NAD+ as cofactor
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate and prefers NAD+ as cofactor
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: the enzyme is very specific to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
Substrates: the enzyme is very specific to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropanoate + NAD(P)+
?
-
Substrates: is more active with NADP+ than NAD+
Products: -
Products: -
?
3-hydroxypropanoate + NAD(P)+
?
-
Substrates: is more active with NADP+ than NAD+
Products: -
Products: -
?
3-hydroxypropanoic acid + NAD+
3-oxopropanoate + NADH + H+
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
3-hydroxypropanoic acid + NAD+
3-oxopropanoate + NADH + H+
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
3-hydroxypropionic acid + NAD+
malonate semialdehyde + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxypropionic acid + NAD+
malonate semialdehyde + NADH + H+
Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
Substrates: -
Products: -
Products: -
r
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
-
Substrates: strain IFO 0750
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: strain IFO 1542
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Nocardia lyena
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Pseudomonas dacunhae
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
3-oxoisobutyrate + NADH
Substrates: high stereospecificity
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
3-oxoisobutyrate + NADH
Substrates: high stereospecificity
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Corynebacterium hydrocarbons
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-serine + NAD+
3-oxo-L-alanine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-serine + NAD+
3-oxo-L-alanine + NADH + H+
Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
Substrates: -
Products: -
Products: -
r
L-serine + NAD+
?
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
L-serine + NAD+
?
Substrates: substrate with much less efficiency compared to (S)-3-hydroxyisobutyrate
Products: -
Products: -
?
methyl (2S)-3-hydroxy-2-methylpropanoate + NAD+
methyl (2S)-2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
methyl (2S)-3-hydroxy-2-methylpropanoate + NAD+
methyl (2S)-2-methyl-3-oxopropanoate + NADH + H+
Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
Substrates: -
Products: -
Products: -
r
methyl DL-serine + NAD+
methyl 3-oxo-DL-alanine + NADH + H+
-
Substrates: -
Products: -
Products: -
r
methyl DL-serine + NAD+
methyl 3-oxo-DL-alanine + NADH + H+
Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: no activity with (R)-methyl-3-hydroxy-2-methylpropionate, glycerate, serine, beta-hydroxypyruvate, threonine, 2-hydroxybutyrate, malate, glycolate, beta-hydroxybutyrate, lactate, and 6-phosphogluconate. NADP+ is not a suitable cofactor. Also, FAD, oxidized cytochrome c, as well as the artificial electron acceptors phenazine methosulfate and dichlorophenol indophenol cannot be reduced by the enzyme
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with (R)-methyl-3-hydroxy-2-methylpropionate, glycerate, serine, beta-hydroxypyruvate, threonine, 2-hydroxybutyrate, malate, glycolate, beta-hydroxybutyrate, lactate, and 6-phosphogluconate. NADP+ is not a suitable cofactor. Also, FAD, oxidized cytochrome c, as well as the artificial electron acceptors phenazine methosulfate and dichlorophenol indophenol cannot be reduced by the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59
Products: -
Products: -
?
additional information
?
-
-
Substrates: wide substrate specificity of the 3-HIBADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with NADP+, DL-glycerate, (R)-3-hydroxyisobutyrate, L-threonine, D-threonine, and D-serine
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with D-serine, (S)-3-hydroxyisobutyrate methyl ester, (R)-3-hydroxyisobutyrate methyl ester, L-threonine and D-threonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-serine, (S)-3-hydroxyisobutyrate methyl ester, (R)-3-hydroxyisobutyrate methyl ester, L-threonine and D-threonine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with (R)-3-hydroxyisobutyrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D,L-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: -
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate and prefers NAD+ as cofactor
Products: -
Products: -
?
(S)-3-hydroxyisobutyrate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: the enzyme is specific to (S)-3-hydroxyisobutyrate and prefers NAD+ as cofactor
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NAD+
2-methyl-3-oxopropanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
3-hydroxy-2-methylpropanoate + NADP+
2-methyl-3-oxopropanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
D-2-methyl-3-oxopropionate + NADH
-
Substrates: strain IFO 0750
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: strain IFO 1542
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Nocardia lyena
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
D,L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Pseudomonas dacunhae
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
Corynebacterium hydrocarbons
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
r
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
L-3-hydroxyisobutyrate + NAD+
L-2-methyl-3-oxopropionate + NADH
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: MmsB from Bacillus cereus exhibits 3-hydroxyisobutyrate dehydrogenase as well as 3-hydroxypropionate dehydrogenase activity, EC 1.1.1.59
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the enzyme prefers NAD+ over NADP+ as a cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
additional information
-
has no metal ion requirement, MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4 have no effect
additional information
-
not influenced by Na+, K+, NH3+, and Li+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-3-hydroxy-2-methylpropanoate
-
competitive inhibitor of the S-isomer
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
additional information
-
is not inhibited by 1-propanol, lactate potassium, malate potassium, malonate potassium, acetaldehyde, ethanol, and glycerin
-
NADH
competitive inhibition in the presence of NADH when NAD+ is varied, noncompetitive inhibition with NADH when (S)-3-hydroxyisobutyrate is varied
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
3-hydroxyisobutyrate dehydrogenase deficiency
3-Hydroxyisobutyrate dehydrogenase (HIBADH) deficiency-A novel disorder of valine metabolism.
Gastroesophageal Reflux
Duodenal lipid-induced symptom generation in gastroesophageal reflux disease: role of apolipoprotein A-IV and cholecystokinin.
Paralysis
[Mutants of bacterium Azospirillum brasilense Sp245 with Omegon insertion in mmsB or fabG genes of lipid metabolism are defective in motility and flagellation].
Tuberculosis
Role of a cysteine residue in substrate entry and catalysis in MtHIBADH: Analysis by chemical modifications and site-directed mutagenesis.
Tuberculosis
Structure, interactions and action of Mycobacterium tuberculosis 3-hydroxyisobutyric acid dehydrogenase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.652
(S)-3-hydroxyisobutyrate
-
at pH 10.0, temperature not specified in the publication
16.8
3-hydroxypropionate
-
pH 8.5, 37°C, KM-value for 3-hydroxyisobutyrate is approximately 20fold lower
10.48
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 37°C and pH 9.0
25.14
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 30°C and pH 9.0
0.164
NAD+
-
with 3-hydroxypropionic acid as cosubstrate, at 30°C and pH 9.0
0.563
NAD+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
0.24
NADP+
-
mutant enzyme D33R, pH and temperature not specified in the publication
0.582
NADP+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
0.96
NADP+
-
wild type enzyme, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
NADP+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
24.1
(S)-3-hydroxyisobutyrate
-
at pH 10.0, temperature not specified in the publication
35.76
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 30°C and pH 9.0
41.35
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 37°C and pH 9.0
1.182
NAD+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
6.717
NAD+
-
with 3-hydroxypropionic acid as cosubstrate, at 30°C and pH 9.0
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.498
NADP+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
37.1
(S)-3-hydroxyisobutyrate
-
at pH 10.0, temperature not specified in the publication
1.433
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 30°C and pH 9.0
4.04
methyl (2S)-3-hydroxy-2-methylpropanoate
-
at 37°C and pH 9.0
2.1
NAD+
with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C
42.44
NAD+
-
with 3-hydroxypropionic acid as cosubstrate, at 30°C and pH 9.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58.67
-
after 36.22fold purification, at 37°C and pH 9.0
8.77
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
8.5
8.8 - 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
7.5 - 9.5
pH 7.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity
8 - 10
8 - 10
-
more than 60% activity between pH 8.0 and 10.0
8 - 10
-
approximately 40% of the activity is retained at pH 11.0. At pH 7.0, the activity is reduced to 30% of the activity observed at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
40
the optimum activity is at about 40°C. Above 50°C, the enzyme activity declines
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
20°C: about 90% of maximal activity, 50°C: about 60% of maximal activity
30 - 45
-
more than 50% activity between 30 and 40°C. Approximately 80% of the activity is lost at 45°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme expressed in Escherichia coli
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis, quantitative RT-PCR expression analysis, overview
brenda
additional information
-
cell type-specific enzyme expression analysis, immunofluorescence labeling, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
the enzyme is located at the mid-piece (a specialized development from the mitochondria) of elongating, elongated, and mature sperm
-
brenda
additional information
-
subcellular enzyme expression analysis, overview
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
At4g20930 knockdown plants show increased root growth inhibition of the mutants if cultivated in the presence of Val or Ile but not in the presence of leucine
metabolism
the enzyme is involved in both, valine and isoleucine degradation in Arabidopsis thaliana
physiological function
additional information
-
enzyme activity of HIBADH in spermatozoa from patients with asthenozoospermia is reduced compared to controls
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
-
the enzyme plays a role in the assembly of motile polar flagellum and in biofilm biomass accumulation
physiological function
-
the enzyme plays a role in the assembly of motile polar flagellum and in biofilm biomass accumulation
-
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
-
Show AA Sequence and Transmembrane Helices (10513 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
74000
80000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
tetramer
additional information
-
hydroxybutyrate dehydrogenase and 3-hydroxyisobutyrate dehydrogenase activity
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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
-
native enzyme, the holoenzyme, binary complexes with NAD+, (S)-3-hydroxyisobutyrate, (R)-3-hydroxyisobutyrate, L-serine and 3-hydroxypropanoic acid and ternary complexes involving the substrates and NAD+, microbatch-under-oil method, using 0.02 M MgCl2, 0.1 M HEPES (pH 7.5), 22% (w/v) polyacrylic acid sodium salt 5100
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D244A
the mutant shows strong reduction in the activity compared to the wild type enzyme
D275A
the mutant shows a marginal loss of activity compared to the wild type enzyme
F236A
the mutant shows reduction in the activity compared to the wild type enzyme
N172A
the mutant shows dramatic reduction in the activity compared to the wild type enzyme
T207A
the mutant shows reduction in the activity compared to the wild type enzyme
W211A
the mutant shows dramatic reduction in the activity compared to the wild type enzyme
D275A
-
the mutant shows a marginal loss of activity compared to the wild type enzyme
-
N172A
-
the mutant shows dramatic reduction in the activity compared to the wild type enzyme
-
W211A
-
the mutant shows dramatic reduction in the activity compared to the wild type enzyme
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
45
-
enzyme activity is not decreased during preincubation at 45°C within 30 min, but preincubation at 55°C in 3 min can significantly denaturate and deactivate the enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
96fold purified at 4°C 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
-
Ni-NTA column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography, Mono Q column chromatography, and Superdex 200 gel filtration
-
Ni-NTA resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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 BL21(DE3) cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HIBADH is downregulated in low-motility sperm, and is enriched expressed during human spermiogenesis
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
3-HIBADH may play a role in biosynthesis of 3-hydroxypropionate as a biological source
additional information
-
3-HIBADH may play a role in biosynthesis of 3-hydroxypropionate as a biological source
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Worral, E.B.; Gassain, S.; Cox, D.J.; Sugden, M.C.; Palmer, T.N.
3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase
Biochem. J.
241
297-300
1987
Cereibacter sphaeroides
brenda
Rougraff, P.M.; Paxton, R.; Kuntz, M.J.; Crabb, D.W.; Harris, R.A
Purification and characterization of 3-hydroxyisobutyrate dehydrogenase from rat liver
J. Biol. Chem.
263
327-331
1988
Oryctolagus cuniculus
brenda
Hasegawa, J
Distribution in organisms and stereospecificity of beta-hydroxyisobutyrate dehydrogenase
Agric. Biol. Chem.
45
2899-2901
1981
Aciculoconidium aculeatum, Bos taurus, Candida parapsilosis, Corynebacterium hydrocarbons, Diutina rugosa, Geotrichum reessii, Micrococcus flavus, Micrococcus luteus, Nocardia lyena, Oryctolagus cuniculus, Pseudomonas aeruginosa, Pseudomonas dacunhae, Rhodotorula mucilaginosa, Sus scrofa, Tsukamurella paurometabola
-
brenda
Hasegawa, J
Purification, crystallization and some properties of beta-hydroxyisobutyrate dehydrogenase from candida rugosa IFO 0750
Agric. Biol. Chem.
45
2805-2814
1981
Diutina rugosa
-
brenda
De Paul Marshall, V.; Sokatch, J.R.
Regulation of valine catabolism in Pseudomonas putida
J. Bacteriol.
110
1073-1081
1972
Pseudomonas putida
brenda
Robinson, W.G.; Coon, M.J.
The purification and properties of beta-hydroxyisobutyrate dehydrogenase
J. Biol. Chem.
225
511-521
1956
Sus scrofa
brenda
Hawes, J.W.; Crabb, D.W.; Chan, R.J.; Rougraff, P.M.; Paxton, R.; Harris, R.A.
Mammalien 3-hydroxyisobutyrate dehydrogenase
Methods Enzymol.
324
218-228
2000
Homo sapiens, Oryctolagus cuniculus, Rattus norvegicus
brenda
Chowdhury, E.K.; Nagata, S.; Misono, H.
3-Hydroxyisobutyrate dehydrogenase from Pseudomonas putida E23: purification and characterization
Biosci. Biotechnol. Biochem.
60
2043-2047
1996
Diutina rugosa, Oryctolagus cuniculus, Pseudomonas putida, Pseudomonas putida E23
brenda
Hawes, J.W.; Harper, E.T.; Crabb, D.W.; Harris, R.A.
Structural and mechanistic aspects of a new family of dehydrogenases, the beta-hydroxyacid dehydrogenases
Adv. Exp. Med. Biol.
414
395-402
1996
Rattus norvegicus
brenda
Chowdhury, E.K.; Akaishi, Y.; Nagata, S.; Misono, H.
Cloning and overexpression of the 3-hydroxyisobutyrate dehydrogenase gene from Pseudomonas putida E23
Biosci. Biotechnol. Biochem.
67
438-441
2003
Pseudomonas putida (Q76KL5), Pseudomonas putida E23 (Q76KL5), Pseudomonas putida E23
brenda
Loupatty, F.J.; van der Steen, A.; Ijlst, L.; Ruiter, J.P.; Ofman, R.; Baumgartner, M.R.; Ballhausen, D.; Yamaguchi, S.; Duran, M.; Wanders, R.J.
Clinical, biochemical, and molecular findings in three patients with 3-hydroxyisobutyric aciduria
Mol. Genet. Metab.
87
243-248
2006
Homo sapiens
brenda
Murin, R.; Schaer, A.; Kowtharapu, B.S.; Verleysdonk, S.; Hamprecht, B.
Expression of 3-hydroxyisobutyrate dehydrogenase in cultured neural cells
J. Neurochem.
105
1176-1186
2008
Rattus norvegicus
brenda
Yao, T.; Xu, L.; Ying, H.; Huang, H.; Yan, M.
The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate
Appl. Biochem. Biotechnol.
160
694-703
2009
Bacillus cereus, Bacillus cereus ATCC 14579
brenda
Tasi, Y.C.; Chao, H.C.; Chung, C.L.; Liu, X.Y.; Lin, Y.M.; Liao, P.C.; Pan, H.A.; Chiang, H.S.; Kuo, P.L.; Lin, Y.H.
Characterization of 3-hydroxyisobutyrate dehydrogenase, HIBADH, as a sperm-motility marker
J. Assist. Reprod. Genet.
30
505-512
2013
Homo sapiens
brenda
Park, S.C.; Kim, P.H.; Lee, G.S.; Kang, S.G.; Ko, H.J.; Yoon, S.I.
Structural and biochemical characterization of the Bacillus cereus 3-hydroxyisobutyrate dehydrogenase
Biochem. Biophys. Res. Commun.
474
522-527
2016
Bacillus cereus
brenda
Lee, P.; Raj, S.; Zhou, S.; Ashok, S.; Edwardraja, S.; Park, S.
3-Hydroxyisobutyrate dehydrogenase-I from Pseudomonas denitrificans ATCC 13867 degrades 3-hydroxypropionic acid
Biotechnol. Bioprocess Eng.
19
1-7
2014
Pseudomonas denitrificans (nom. rej.), Pseudomonas denitrificans (nom. rej.) ATCC 13867
-
brenda
Zhou, S.; Mohan Raj, S.; Ashok, S.; Edwardraja, S.; Lee, S.G.; Park, S.
Cloning, expression and characterization of 3-hydroxyisobutyrate dehydrogenase from Pseudomonas denitrificans ATCC 13867
PLoS ONE
8
e62666
2013
Pseudomonas denitrificans (nom. rej.), Pseudomonas denitrificans (nom. rej.) ATCC 13867
brenda
Srikalaivani, R.; Singh, A.; Vijayan, M.; Surolia, A.
Structure, interactions and action of Mycobacterium tuberculosis 3-hydroxyisobutyric acid dehydrogenase
Biochem. J.
475
2457-2471
2018
Mycobacterium tuberculosis (P9WNY5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNY5)
brenda
Sheludko, A.V.; Filipecheva, Y.A.; Telesheva, E.M.; Yevstigneyeva, S.S.; Petrova, L.P.; Katsy, E.I.
Restoration of polar-flagellum motility and biofilm-forming capacity in the mmsB1 mutant of the alphaproteobacterium Azospirillum brasilense Sp245 points to a new role for a homologue of 3-hydroxyisobutyrate dehydrogenase
Can. J. Microbiol.
65
144-154
2019
Azospirillum brasilense, Azospirillum brasilense SP245
brenda
Schertl, P.; Danne, L.; Braun, H.P.
3-Hydroxyisobutyrate dehydrogenase is involved in both, valine and isoleucine degradation in Arabidopsis thaliana
Plant Physiol.
175
51-61
2017
Arabidopsis thaliana, Arabidopsis thaliana (Q9SUC0)
brenda
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