Information on EC 6.2.1.40 - 4-hydroxybutyrate-CoA ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.40
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RECOMMENDED NAME
GeneOntology No.
4-hydroxybutyrate-CoA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 4-hydroxybutanoate + CoA = AMP + diphosphate + 4-hydroxybutanoyl-CoA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate/4-hydroxybutanate cycle
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Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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CO2 fixation in Crenarchaeota
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxybutyrate:CoA ligase (AMP formimg)
Isolated from the archaeon Metallosphaera sedula. Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-hydroxybutyrate + CoA
AMP + diphosphate + 3-hydroxybutyryl-CoA
show the reaction diagram
ATP + 3-hydroxypropionate + CoA
AMP + diphosphate + 3-hydroxypropionyl-CoA
show the reaction diagram
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9% of the activity compared to 4-hydroxybutanoate
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-
?
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
show the reaction diagram
ATP + acetate + CoA
AMP + diphosphate + acetyl-CoA
show the reaction diagram
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
show the reaction diagram
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
ATP + 4-hydroxybutanoate + CoA
AMP + diphosphate + 4-hydroxybutanoyl-CoA
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 2
4-hydroxybutanoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24 - 2.5
4-hydroxybutanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 2.18
4-hydroxybutanoate
4210
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.22
substrate: 4-hydroxybutanoate, pH 7.9, 75°C
1.6
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pH 7.8, 85°C
1.7
substrate: 4-hydroxybutanoate, pH 7.9, 75°C
2.3
substrate: 4-hydroxybutanoate, pH 7.9, 75°C, mutant enzyme W424G
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
7.9
assay at; assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
assay at; assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
x * 62000, calculated from sequence
64000
x * 64000, SDS-PAGE
71356
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x * 71356, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli. The recombinant enzyme is modified by acetylation at Lys594 and is partly inactive
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expression in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
recombinantly expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
approximately 10fold downregulated in presence of acetate, 4-hydroxybutyrate, succinate or pyruvate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE