Information on EC 3.1.1.22 - hydroxybutyrate-dimer hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.22
-
RECOMMENDED NAME
GeneOntology No.
hydroxybutyrate-dimer hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O = 2 (R)-3-hydroxybutanoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Butanoate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
37278-37-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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-
-
Manually annotated by BRENDA team
strain a
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-3-((R)-3-hydroxybutanoloxy)butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)11butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)2butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)3butanoate
?
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)3butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)4butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)7butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((S)-3-hydroxybutanoyloxy)butanoate + H2O
(R)-3-hydroxybutanoate + (S)-3-hydroxybutanoate
show the reaction diagram
(S)-3-((R)-3-hydroxybutanoyloxy)butanoate + H2O
(R)-3-hydroxybutanoate + (S)-3-hydroxybutanoate
show the reaction diagram
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i.e. L-(+)-3-[D-(-)-hydroxybutuyryloxy]butyric acid
-
?
3-(3-hydroxybutanoyloxy)butanoate + H2O
3-hydroxybutanoate
show the reaction diagram
3-(3-hydroxypentanoyloxy)pentanoate + H2O
3-hydroxypentanoate
show the reaction diagram
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
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75% of the activity with 4-nitrophenyl butyrate
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butanoate
show the reaction diagram
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
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best 4-nitrophenyl ester substrate
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?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
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43% of the activity with 4-nitrophenyl butyrate
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?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
show the reaction diagram
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
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81% of the activity with 4-nitrophenyl butyrate
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?
D-(-)-3-butyryloxybutyrate + H2O
?
show the reaction diagram
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-
-
-
?
D-(-)3-(3-O-methyloxybutyryl)hydroxybutyrate + H2O
?
show the reaction diagram
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
show the reaction diagram
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-
-
?
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
(R)-3-((R)-3-hydroxybutanoloxy)butanoate + H2O
(R)-3-hydroxybutanoate
show the reaction diagram
(R)-3-((R)-3-hydroxybutanoyloxy)3butanoate
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropylfluorophosphate
EDTA
-
inhibition after prolonged incubation
iodoacetamide
N-ethylmaleimide
74.8% residual activity at 1 mM
NEM
-
13% inhibition at 1 mM
phenylmethylsulfonyl fluoride
27.4% residual activity at 1 mM
Phenylmethylsulfonylfluoride
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10 mM, 50% enzyme activity inhibited
PMSF
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92% inhibition at 1 mM
SDS
61.1% residual activity at 0.05% (w/v)
Triton X-100
67.3% residual activity at 0.05% (v/v)
additional information
-
not inhibited by 1,4-dimercapto-2,3-butanediol; not inhibited by (p-tert-octylphenoxy)polyethoxyethanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 0.7
(R)-3-((R)-3-hydroxybutanoloxy)butanoate
1.3
(R)-3-((R)-3-hydroxybutanoyloxy)11butanoate
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0.17 - 5.2
(R)-3-((R)-3-hydroxybutanoyloxy)2butanoate
0.36 - 11.1
(R)-3-((R)-3-hydroxybutanoyloxy)3butanoate
0.12 - 4
(R)-3-((R)-3-hydroxybutanoyloxy)4butanoate
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1.5
(R)-3-((R)-3-hydroxybutanoyloxy)7butanoate
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0.18 - 32.8
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate
0.2
(R)-3-((S)-3-hydroxybutanoyloxy)butanoate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80
(R)-3-((R)-3-hydroxybutanoyloxy)2butanoate
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22
(R)-3-((R)-3-hydroxybutanoyloxy)3butanoate
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1500
(R)-3-((R)-3-hydroxybutanoyloxy)butanoate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.48
with 3-(3-hydroxypentanoyloxy)pentanoate as substrate, at pH 8.0 and 30C
0.67
with 3-(3-hydroxybutanoyloxy)butanoate as substrate, at pH 8.0 and 30C
14.1
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purified enzyme
additional information
-
substrate specificity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
more than 50% activity between pH 5.0 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
more than 50% activity between 20-60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
up to the mid-exponential growth phase, used for purification purpose
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7200
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1 * 7200, SDS-PAGE
28000 - 30000
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gel filtration, SDS-PAGE
32000
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estimated by SDS-PAGE, deduced from sequence of cDNA
68000 - 74000
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gel filtration, SDS-PAGE
70000
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1 * 70000, SDS-PAGE
72880
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calculation from sequence of cDNA
78000
x * 78000, invitro transcribed and translated enzyme, SDS-PAGE
120000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 78000, invitro transcribed and translated enzyme, SDS-PAGE
homotetramer
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
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unstable at
30 - 45
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15 min, 80% activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, at least 6 months
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-20C, NaCl 0.4 M, 6 months
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-20C, pH 7.5, 1 year
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-20C, pH 8.0, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2350fold, to homogeneity
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ammonium sulfate precipitation, Ni-NTA column chromatography, and TSK gel G3000SW gel filtration
hydrophobic column chromatography
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native from strain SA1 and recombinant from Escherichia coli
recombinant from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, functional expression in Escherichia coli as His-tagged enzyme, in vitro transcription and translation
expressed in Escherichia coli JM109 cells
expression in Escherichia coli
gene i3HBOH, DNA sequence determination and analysis, expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S102A
site-directed mutagenesis, inactive mutant
S191A
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
S218A
site-directed mutagenesis, slightly decreased activity compared to the wild-type enzyme
S306A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
S356A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
S359A
site-directed mutagenesis, inactive mutant
S630A
site-directed mutagenesis, increased activity compared to the wild-type enzyme
Show AA Sequence (290 entries)
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