Information on EC 6.2.1.36 - 3-hydroxypropionyl-CoA synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.36
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RECOMMENDED NAME
GeneOntology No.
3-hydroxypropionyl-CoA synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
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3-hydroxypropanoate/4-hydroxybutanate cycle
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Carbon fixation pathways in prokaryotes
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glyoxylate assimilation
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Microbial metabolism in diverse environments
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propionyl-coA synthase
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CO2 fixation in Crenarchaeota
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxypropionate:CoA ligase (AMP-forming)
Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1,2].The enzymes from Metallosphaera sedula and Sulfolobus tokodaii can also use propionate, acrylate, acetate, and butanoate as substrates [2], and are thus different from EC 6.2.1.17 (propionate---CoA ligase), which does not accept acetate or butanoate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
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
3-chloropropionate + ATP + coenzyme A
3-chloropropionyl-CoA + AMP + diphosphate
show the reaction diagram
3-hydroxypropanoate + ATP + coenzyme A
3-hydroxypropanoyl-CoA + AMP + diphosphate
show the reaction diagram
3-hydroxypropanoate + CTP + coenzyme A
3-hydroxypropanoyl-CoA + CMP + diphosphate
show the reaction diagram
3-hydroxypropanoate + UTP + coenzyme A
3-hydroxypropanoyl-CoA + UMP + diphosphate
show the reaction diagram
32% of the activity with ATP
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-
?
3-mercaptopropionate + ATP + coenzyme A
3-mercaptopropionyl-CoA + AMP + diphosphate
show the reaction diagram
acetate + ATP + coenzyme A
acetyl-CoA + AMP + diphosphate
show the reaction diagram
acrylate + ATP + coenzyme A
acryloyl-CoA + AMP + diphosphate
show the reaction diagram
butyrate + ATP + coenzyme A
butyryl-CoA + AMP + diphosphate
show the reaction diagram
propionate + ATP + coenzyme A
propionyl-CoA + AMP + diphosphate
show the reaction diagram
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
3-hydroxypropanoate + ATP + coenzyme A
3-hydroxypropanoyl-CoA + AMP + diphosphate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
3-hydroxypropionate
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pH 8.5, 45C
1.42
Acrylate
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pH 8.5, 45C
0.045
ATP
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pH 8.5, 45C
0.12
propionate
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pH 8.5, 45C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.7
3-hydroxypropionate
Metallosphaera sedula
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pH 8.5, 45C
5.4
Acrylate
Metallosphaera sedula
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pH 8.5, 45C
5.6
propionate
Metallosphaera sedula
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pH 8.5, 45C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31.7
3-hydroxypropionate
Metallosphaera sedula
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pH 8.5, 45C
1632
3.8
Acrylate
Metallosphaera sedula
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pH 8.5, 45C
1915
46.7
propionate
Metallosphaera sedula
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pH 8.5, 45C
312
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
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pH 8,5, 45C, autotrophically grown cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
74000
2 * 74000, SDS-PAGE
78000
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4 * 78000, SDS-PAGE
140000
gel filtration
340000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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15 min, stable up to 80C
100
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15 min, 50% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli