Information on EC 3.1.2.4 - 3-hydroxyisobutyryl-CoA hydrolase

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: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.2.4
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyisobutyryl-CoA hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
formation of an anhydride reaction intermediate, catalytic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of thioester
-
-
-
-
hydrolysis of thioester
-
-
hydrolysis of thioester
-
-
hydrolysis of thioester
-
-
PATHWAY
KEGG Link
MetaCyc Link
beta-alanine biosynthesis II
-
beta-Alanine metabolism
-
Metabolic pathways
-
Propanoate metabolism
-
valine degradation I
-
Valine, leucine and isoleucine degradation
-
SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methylpropanoyl-CoA hydrolase
Also hydrolyses 3-hydroxypropanoyl-CoA.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hydroxy-isobutyryl CoA hydrolase
-
-
-
-
3-hydroxyisobutyryl-CoA hydrolase
Q81DR3
-
3-hydroxyisobutyryl-CoA hydrolase
-
-
BCH
Q81DR3
-
beta-hydroxyisobutyryl-CoA hydrolase
-
-
beta-hydroxyisobutyryl-coenzyme A hydrolase
-
-
HIB CoA hydrolase
-
-
HIB CoA hydrolase
Pseudomonas fluorescens UK-1
-
-
-
HIB-CoA hydrolase
-
-
HIBYL-CoA hydrolase
-
-
HIBYL-CoA hydrolase
-
-
hydrolase, 3-hydroxyisobutyryl coenzyme A
-
-
-
-
additional information
-
the enzyme belongs to the crotonase superfamily
CAS REGISTRY NUMBER
COMMENTARY
9025-88-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain ATCC 14579
UniProt
Manually annotated by BRENDA team
mitochondrial precursor
Uniprot
Manually annotated by BRENDA team
strain UK-1
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens UK-1
strain UK-1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the chy1-10 mutation disrupts a peroxisomal HIBYL-CoA hydrolase, causing reduced cold-induction of CBF3 promoter (CBF3-LUC) in chy1-10. Transcription factors (CBFs) also reduced in the chy1 mutant. Chy1-10 mutant plants are more sensitive to freezing treatment than wild-type after cold acclimation. Both the wild-type and chy1 mutant plants are sensitive to darkness-induced starvation at warm temperatures, although chy1 plants are slightly more sensitive. Chy1-10 is allelic to chy1-1 and chy1-3, all of the examined alleles disrupt HIBYL-CoA hydrolase activity similarly. CBF3 overexpression in chy1-10 partially rescues the mutant defects in cold and dark responses. Disruption of the HIBYL-CoA hydrolase causes accumulation of reactive oxygen species
malfunction
-, Q9LKJ1
mutations in the Chy1 gene lead to a deficiency of benzoic acid-containing glucosinolates in the seeds
physiological function
-
a role for peroxisomal metabolism in cold stress signaling, and plant tolerance to cold stress and darkness-induced starvation. Is needed for fatty acid beta-oxidation and valine catabolism
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + (S)-3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
?
(S)-methylmalonyl-CoA + H2O
CoA + methylmalonate
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylbutyryl-CoA + H2O
CoA + 3-hydroxy-2-methylbutyrate
show the reaction diagram
-
low activity
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-, Q6NVY1
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
ir
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-, Q81DR3
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-, Q81DR3
-
(S)-3-hydroxyacids and their esters, such as (S)-3-hydroxybutyric acid, can be used as chiral building blocks for the chemical synthesis of optically active fine chemicals such as antibiotics, vitamins, perfumes, and pheromones
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
key enzyme in valine metabolism regulating the toxic concentration of methacrylyl-coenzyme A, human liver disease decreases the enzyme activity in vivo
-
ir
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
Pseudomonas fluorescens UK-1
-
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-, Q6NVY1
the enzyme is responsible for the specific hydrolysis of 3-hydroxy-2-methylpropanoyl-CoA, a saline catabolite
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-
enzyme is involved in Val catabolism. The enzyme protects cells against toxic effects of methacrylyl-CoA, an intermediate in the Val pathway occuring upstream of 3-hydroxy-2-methylpropanoyl-CoA
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
3-hydroxy-2-methylpropanoate + CoA
show the reaction diagram
-
substrate is an intermediate in the pathway of valine catabolism, which is unique in that it produces a radily diffusible monocarboxylic acid
-
?
3-hydroxy-3-phenylpropionyl-CoA + H2O
3-hydroxy-3-phenylpropionate + CoA
show the reaction diagram
-, Q9LKJ1
-
-
-
?
3-hydroxyisobutyryl-CoA + H2O
CoA + 3-hydroxyisobutyrate
show the reaction diagram
-
formation of an anhydride reaction intermediate, Glu164 is involved
-
?
3-hydroxypropionyl-CoA + H2O
CoA + 3-hydroxypropanoate
show the reaction diagram
-, Q6NVY1
-
-
-
?
3-hydroxypropionyl-CoA + H2O
CoA + 3-hydroxypropanoate
show the reaction diagram
-
-
-
?
3-hydroxypropionyl-CoA + H2O
CoA + 3-hydroxypropanoate
show the reaction diagram
-
-
-
-
?
3-hydroxypropionyl-CoA + H2O
CoA + 3-hydroxypropanoate
show the reaction diagram
-, Q6NVY1
hydrolysis of beta-hydroxypropionyl-CoA, an intermediate in a minor pathway of propionate metabolism
-
-
-
cinnamoyl-CoA + H2O
cinnamic acid + CoA
show the reaction diagram
-, Q9LKJ1
-
-
-
?
DL-3-hydroxybutyryl-CoA + H2O
CoA + DL-3-hydroxybutyrate
show the reaction diagram
-
low activity
-
?
p-coumaroyl-CoA + H2O
p-coumaric acid + CoA
show the reaction diagram
-, Q9LKJ1
-
-
-
?
L-3-hydroxybutyryl-CoA + H2O
CoA + L-3-hydroxybutyrate
show the reaction diagram
-
low activity
-
?
additional information
?
-
-
substrate specificity, overview, acetoacetyl-CoA, DL-methylmalonyl-CoA, isobutyryl-CoA, malonyl-CoA, acetyl-CoA, propionyl-CoA, and n-valeryl-CoA are poor substrates
-
?
additional information
?
-
-
enzyme production is induced in presence of Val, 2-oxoisovalerate, isobutyrate and 3-hydroxyisobutyrate. Intermediates of the Krebs cycle repress the formation of 3-hydroxyisobutyryl CoA when isobutyrate is present as the inducer. Activity is maximal at the end of the exponential phase
-
-
-
additional information
?
-
Q6NVY1
mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results in progressive infantile neurodegeneration
-
-
-
additional information
?
-
-, Q9LKJ1
has no hydrolase activity with benzoyl-CoA
-
-
-
additional information
?
-
Pseudomonas fluorescens UK-1
-
enzyme production is induced in presence of Val, 2-oxoisovalerate, isobutyrate and 3-hydroxyisobutyrate. Intermediates of the Krebs cycle repress the formation of 3-hydroxyisobutyryl CoA when isobutyrate is present as the inducer. Activity is maximal at the end of the exponential phase
-
-
-
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-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-, Q81DR3
-
-
-
?
3-hydroxy-2-methylpropanoyl-CoA + H2O
CoA + 3-hydroxy-2-methylpropanoate
show the reaction diagram
-
key enzyme in valine metabolism regulating the toxic concentration of methacrylyl-coenzyme A, human liver disease decreases the enzyme activity in vivo
-
ir
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-
-
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-, Q6NVY1
the enzyme is responsible for the specific hydrolysis of 3-hydroxy-2-methylpropanoyl-CoA, a saline catabolite
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
?
show the reaction diagram
-
enzyme is involved in Val catabolism. The enzyme protects cells against toxic effects of methacrylyl-CoA, an intermediate in the Val pathway occuring upstream of 3-hydroxy-2-methylpropanoyl-CoA
-
-
-
3-hydroxy-2-methylpropanoyl-CoA + H2O
3-hydroxy-2-methylpropanoate + CoA
show the reaction diagram
-
substrate is an intermediate in the pathway of valine catabolism, which is unique in that it produces a radily diffusible monocarboxylic acid
-
?
3-hydroxypropionyl-CoA + H2O
CoA + 3-hydroxypropanoate
show the reaction diagram
-, Q6NVY1
hydrolysis of beta-hydroxypropionyl-CoA, an intermediate in a minor pathway of propionate metabolism
-
-
-
additional information
?
-
-
enzyme production is induced in presence of Val, 2-oxoisovalerate, isobutyrate and 3-hydroxyisobutyrate. Intermediates of the Krebs cycle repress the formation of 3-hydroxyisobutyryl CoA when isobutyrate is present as the inducer. Activity is maximal at the end of the exponential phase
-
-
-
additional information
?
-
Q6NVY1
mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results in progressive infantile neurodegeneration
-
-
-
additional information
?
-
Pseudomonas fluorescens UK-1
-
enzyme production is induced in presence of Val, 2-oxoisovalerate, isobutyrate and 3-hydroxyisobutyrate. Intermediates of the Krebs cycle repress the formation of 3-hydroxyisobutyryl CoA when isobutyrate is present as the inducer. Activity is maximal at the end of the exponential phase
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-, Q9LKJ1
Mg2+, Fe2+, Cu2+, Zn2+, and Mn2+ at concentrations of 1 mM have no effect on the hydrolase activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetoacetyl-CoA
-
competitive inhibition
acetoacetyl-CoA
-
competitive
acetyl-CoA
-
competitive inhibition
acetyl-CoA
-
competitive
Cu2+
-, Q9LKJ1
at 1 mM causes more than 90% inhibition of activity
DL-3-hydroxybutyryl-CoA
-
competitive inhibition
DL-3-hydroxybutyryl-CoA
-
competitive
DL-methylmalonyl-CoA
-
competitive inhibition
DL-methylmalonyl-CoA
-
competitive
isobutyryl-CoA
-
competitive inhibition
isobutyryl-CoA
-
competitive
malonyl-CoA
-
competitive inhibition
malonyl-CoA
-
competitive
n-Valeryl-CoA
-
competitive inhibition
n-Valeryl-CoA
-
competitive
propionyl-CoA
-
competitive inhibition
propionyl-CoA
-
competitive
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.006
-
(S)-3-hydroxy-2-methylpropanoyl-CoA
-
recombinant enzyme, pH 8.0, 30C
0.006
-
3-hydroxy-2-methylpropanoyl-CoA
-
-
0.025
-
3-hydroxypropionyl-CoA
-
recombinant enzyme, pH 8.0, 30C
0.025
-
3-hydroxypropionyl-CoA
-
-
0.0029
-
cinnamoyl-CoA
-, Q9LKJ1
at 30C, in 50 mM Tris/HCl buffer, pH 7.0
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
150
-
3-hydroxy-2-methylpropanoyl-CoA
-
-
266
-
3-hydroxy-2-methylpropanoyl-CoA
-
-
1
-
3-hydroxyisobutyryl-CoA
-
mutant D151N
89
-
3-hydroxyisobutyryl-CoA
-
wild-type enzyme, a deuterium isotope of the substrate is used
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
acetoacetyl-CoA
-
recombinant enzyme, pH 8.0, 30C
2.61
-
acetyl-CoA
-
recombinant enzyme, pH 8.0, 30C
0.14
-
DL-3-hydroxybutyryl-CoA
-
recombinant enzyme, pH 8.0, 30C
2.26
-
DL-methylmalonyl-CoA
-
recombinant enzyme, pH 8.0, 30C
1.19
-
isobutyryl-CoA
-
recombinant enzyme, pH 8.0, 30C
1.6
-
malonyl-CoA
-
recombinant enzyme, pH 8.0, 30C
0.72
-
n-Valeryl-CoA
-
recombinant enzyme, pH 8.0, 30C
0.83
-
propionyl-CoA
-
recombinant enzyme, pH 8.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.073
-
-, Q81DR3
recombinant BCH in Escherichia coli strain BL21(DE3) crude extract
244
-
-
purified recombinant enzyme, substrate 3-hydroxypropionyl-CoA
427
-
-
purified enzyme
430
-
-
purified recombinant enzyme, substrate (S)-3-hydroxy-2-methylpropanoyl-CoA
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
hydrolysis of (S)-methylmalonyl-CoA
7
-
-, Q81DR3
assay at
7
-
-, Q9LKJ1
in 50 mm Tris-buffer
8
-
-
assay at
8
-
-
hydrolysis of 3-hydroxy-2-methylpropanoyl-CoA
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10.5
-
pH 5.0: about 40% of maximal activity, pH 10.5: about 80% of maximal activity, hydrolysis of 3-hydroxy-2-methylpropanoyl-CoA
5
7
-
pH 5.0, about 30% of maximal activity, pH 7.0: 65% of maximal activity, hydrolysis of (S)-methylmalonyl-CoA
5.1
10.3
-
at least
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-, Q81DR3
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Shewanella oneidensis (strain MR-1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37000, SDS-PAGE
?
-, Q6NVY1
x * 36000, SDS-PAGE; x * 39398, calculation from nucleotide sequence
monomer
-
1 * 39398, amino acid sequence calculation, 1 * 38000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by Ni chromatography
-, Q9LKJ1
native enzyme from mitochondrial membranes of HL-60 cells by two-step heparin affinity chromatography method using divalent cations, e.g. Mg2+, as eluents
-
recombinant enzyme from Escherichia coli, removal of His-tag with thrombin
-
from rat liver, 7200fold, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
CHY1 cDNA cloned behind the 35S promoter in a binary vector, introduced into homozygous chy1-10 mutant plants by Agrobacterium tumefaciens strain GV3101 transformation
-
open-reading frame of the Chy1 gene amplified, cDNA ligated into the vector pEX5-CT/TOPO TA to create a fusion of the open-reading frame with a His tag-coding extension at the C-terminus. Plasmid transferred into Escherichia coli BL21 (DE3) cells for expression
-, Q9LKJ1
subcloning in Escherichia coli strain XL1-Blue, and expression in Escherichia coli strain BL21 (DE3) under control of the T7 promoter, co-expression with the beta-ketothiolase gene from Ralstonia eutropha strain H16 and the (S)-3-hydroxybutyryl-CoA dehydrogenase gene from Ralstonia eutropha strain H16, or Clostridium acetobutylicum strain ATCC824 leads to biosynthesis of enantiomerically pure (S)-3-hydroxybutyric acid in the engineered Escherichia coli cells, extracellular product, method optimization, overview
-, Q81DR3
DNA and amino acid sequence determination and analysis, expression in Escherichia coli BL21(DE3) as His-tagged enzyme
-
expression in Escherichia coli
-, Q6NVY1
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D151N
-
reduced activity
E143A
-
no detectable activity
E143D
-
no detectable activity
E143Q
-
no detectable activity