Information on EC 6.4.1.3 - propionyl-CoA carboxylase and Organism(s) Homo sapiens

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Homo sapiens


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.4.1.3
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RECOMMENDED NAME
GeneOntology No.
propionyl-CoA carboxylase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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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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anaerobic energy metabolism (invertebrates, mitochondrial)
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methylaspartate cycle
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mycolate biosynthesis
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propanoyl CoA degradation I
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CO2 fixation in Crenarchaeota
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Valine, leucine and isoleucine degradation
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Glyoxylate and dicarboxylate metabolism
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Propanoate metabolism
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Carbon fixation pathways in prokaryotes
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Metabolic pathways
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-94-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
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at a rate 1.5% that obtained for propionyl-CoA
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ATP + butanoyl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
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-
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ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
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
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
biotin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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stimulates, Km: 9.4 mM
Mg2+
required to form a complex with ATP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
ATP
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1.2
Butanoyl-CoA
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3
HCO3-
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0.28 - 0.59
propanoyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.54
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purified mutant enzyme E168K
9.93
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purified mutant enzyme R165W
9.95
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purified mutant enzyme R410W
23.35
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purified wild-type enzyme
27.7
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32.34
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purified mutant enzyme A497V
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 9.6
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7.2-8.8: maximal activity, 9.6: about 50% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
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x * 72000, alpha, + x * 56000, beta, SDS-PAGE under reducing conditions
60000
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x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
72000
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x * 72000, alpha, + x * 56000, beta, SDS-PAGE under reducing conditions
75000
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x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
540000
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gel filtration
800000
additional information
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contains the tripeptide Pro-Met-Pro, 26 residues towards the amino terminus from the biotin attachment site
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.4
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stable
1868
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-50 - 37
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stable
37
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30 min, wild-type enzyme is stable, mutant enzymes R165W, E168K and R410W lose 30% of their activity
47
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30 min, wild-type enzyme is stable, mutant enzyme A497V loses 40% of its activity mutant enzymes R165W, E168K and R410W lose 85% of their activity
58
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the wild-type enzyme undergoes a cooperative two-state transition between the native and denatured states with a Tm of 57.6°C
additional information
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thermal denaturation is irreversible
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
limited proteolysis with trypsin results in slow time-dependent deactivation of the enzyme with preferential cleavage of the smaller subunit
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant
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recombinant enzymes from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
correction of enzyme deficiency in pccA fibroblasts
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expressed in COS-7 cells at 27°C and 37°C
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expressed in Escherichia coli
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expressed using a two hybrid system in COS cells
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expression in Escherichia coli
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expression of alpha and beta subunit in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A487V
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no effect on activity
A513_R514insP
D178H
increased alpha/beta subunit ratio, very low activity
DELTA408
catalytically inactive
DELTA499
DELTA514
DELTA531
G246V
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activity of the mutant enzyme is 12% of the wild-type activity
M442T
catalytically inactive
P228L
increased alpha/beta subunit ratio, very low activity
R165Q
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beta subunit, no effect on subunit interactions and activity
R44P
catalytically inactive
R67S
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beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
W531X
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activity of the mutant enzyme is less than 1% of the wild-type activity
additional information
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intragenic complementation analysis to 15 naturally occuring mutations in the PCCB gene
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine