Information on EC 6.4.1.3 - propionyl-CoA carboxylase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY
6.4.1.3
-
RECOMMENDED NAME
GeneOntology No.
propionyl-CoA carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
anaerobic energy metabolism (invertebrates, mitochondrial)
-
-
Biosynthesis of antibiotics
-
-
Carbon fixation pathways in prokaryotes
-
-
CO2 fixation in Crenarchaeota
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
methylaspartate cycle
-
-
Microbial metabolism in diverse environments
-
-
mycolate biosynthesis
-
-
Propanoate metabolism
-
-
propanoyl CoA degradation I
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Carboxylase, propional coenzyme A (adenosine triphosphate-hydrolyzing)
-
-
-
-
Pcase
-
-
-
-
PCC
-
-
-
-
PCCase
-
-
-
-
Propanoyl-CoA:carbon dioxide ligase
-
-
-
-
Propionyl coenzyme A carboxylase
-
-
-
-
Propionyl coenzyme A carboxylase (adenosine triphosphate-hydrolyzing)
-
-
-
-
Propionyl coenzyme A carboxylase (ATP-hydrolyzing)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-94-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
organism grows autotrophically
-
-
Manually annotated by BRENDA team
Q877I4: biotin carboxyl carrier protein of acetyl-CoA carboxylase, Q877I3: carboxyltransferase subunit of acetyl-CoA carboxylase, Q877I5: biotin carboxylase subunit of acetyl-CoA carboxylase
Q877I4 and Q877I3 and Q877I5
UniProt
Manually annotated by BRENDA team
strain So4a, DSM 3191
-
-
Manually annotated by BRENDA team
Acidianus infernus So4a
strain So4a, DSM 3191
-
-
Manually annotated by BRENDA team
Agrobacterium tumefaciens IAM13299
IAM13299
-
-
Manually annotated by BRENDA team
Azorhizobium caulinodans ORS571
ORS571
-
-
Manually annotated by BRENDA team
mid-lactation cow
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum USDA110
USDA110
-
-
Manually annotated by BRENDA team
strain OK-70-fl, DSM 636
-
-
Manually annotated by BRENDA team
strain OK70-fl, DSM 636
-
-
Manually annotated by BRENDA team
Chloroflexus aurantiacus OK-70-fl
strain OK-70-fl, DSM 636
-
-
Manually annotated by BRENDA team
Chloroflexus aurantiacus OK70-fl
strain OK70-fl, DSM 636
-
-
Manually annotated by BRENDA team
I3R7G3: biotin carboxylase subunit (PccA), I3R7F1: carboxyltransferase component (PccB), I3R7F2: essential small subunit PccX
I3R7G3 and I3R7F1 and I3R7F2
UniProt
Manually annotated by BRENDA team
cDNA encoding for the alpha subunit
-
-
Manually annotated by BRENDA team
cDNA encoding for the beta subunit
GenBank
Manually annotated by BRENDA team
Mesorhizobium huakuii CCBAU2609
CCBAU2609
-
-
Manually annotated by BRENDA team
strain TH2, DSM 348
-
-
Manually annotated by BRENDA team
strain TH2, DSM 5348
-
-
Manually annotated by BRENDA team
Metallosphaera sedula TH2
strain TH2, DSM 348
-
-
Manually annotated by BRENDA team
Metallosphaera sedula TH2
strain TH2, DSM 5348
-
-
Manually annotated by BRENDA team
cDNA of the beta subunit; studies on beta subunit
SwissProt
Manually annotated by BRENDA team
maximum activity after 40 h of development
-
-
Manually annotated by BRENDA team
wild type form. The dcm-1 mutant is deficient in propanoyl-CoA carboxylase
-
-
Manually annotated by BRENDA team
propionate- or valine-grown
-
-
Manually annotated by BRENDA team
; SpragueDawley rats
Uniprot
Manually annotated by BRENDA team
fed a biotin deficient and normal diet
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum bv. viciae MNF300
MNF300
-
-
Manually annotated by BRENDA team
Sinorhizobium fredii USDA205
USDA205
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti Rm1021
Rm1021
-
-
Manually annotated by BRENDA team
strains M145, MA4 and MTC21
-
-
Manually annotated by BRENDA team
Streptomyces hygroscopicus ATCC 29253
-
-
-
Manually annotated by BRENDA team
strain Kra23, DSM 6482
-
-
Manually annotated by BRENDA team
Sulfolobus metallicus Kra23
strain Kra23, DSM 6482
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
I3R7G3 and I3R7F1 and I3R7F2
gene knockout/complementation demonstrates that the enzyme consists of a fusion protein of a biotin carboxylase and a biotin-carboxyl carrier protein (PccA, HFX_2490), a carboxyltransferase component (PccB, HFX_2478), and an essential small subunit (PccX, HFX_2479). Knockout of pccBX leads to an inability to utilize propionate and a higher intracellular propionyl-CoA level, indicating that the enzyme is indispensable for propionyl-CoA utilization. the pccBX-deleted strain displays multiple phenotypic changes, including retarded cell growth, decreased glucose consumption, impaired PHBV biosynthesis, and wrinkled cells. Genome-wide microarray analysis shows that many genes for glycolysis, pyruvate oxidation, PHBV accumulation, electron transport, and stress responses are affected in the pccBX-deleted strain
metabolism
P14882
methylmalonyl-CoA mutase and PCC are key enzmyes in the catabolic pathway of propionate metabolism in the developing and adult rat central nervous system
metabolism
Q5LUF3
PCC is essential for the catabolism of the amino acids L-Thr, L-Val, L-Ile and L-Met, cholesterol and fatty acids with an odd number of carbon atoms
metabolism
I3R7G3 and I3R7F1 and I3R7F2
the enzyme is indispensability for propionyl-CoA assimilation und the global metabolism of Haloferax mediterranei
physiological function
-
the PCC pathway is the dominant route for the supply of methylmalonyl-CoA for rapamycin production in Streptomyces hygroscopicus UV2-2 strain
physiological function
Streptomyces hygroscopicus ATCC 29253
-
the PCC pathway is the dominant route for the supply of methylmalonyl-CoA for rapamycin production in Streptomyces hygroscopicus UV2-2 strain
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + CO2
?
show the reaction diagram
Q5LUF3
the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate
-
-
?
acetyl-CoA + CO2
?
show the reaction diagram
Q9X4K7
the wild type enzyme shows no activity with acetyl-CoA, but mutant enzyme D422I does
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
no other acetyl-CoA carboxylase detected in this organism
-
-
-
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
at 0.7% of the velocity compared to propanoyl-CoA
-
-
-
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
at a rate 1.5% that obtained for propionyl-CoA
-
-
-
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
EC 6.4.1.2 activity
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
-
EC 6.4.1.2 activity
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
Q5LUF3
the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK-70-fl, Metallosphaera sedula TH2
-
EC 6.4.1.2 activity
-
?
ATP + acetyl-CoA + HCO3-
?
show the reaction diagram
Q877I4 and Q877I3 and Q877I5
n-butyryl-CoA (0.5 mM) is carboxylated at 4.6% compared to carboxylation of acetyl-CoA or propionyl-CoA
-
-
?
ATP + butanoyl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
-
-
-
-
ATP + butanoyl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
at 5.7% of the velocity compared to propanoyl-CoA
-
-
-
ATP + butyryl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
-
-
?
ATP + crotonyl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
at 3% the velocity compared to propanoyl-CoA
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
show the reaction diagram
-
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
P05166
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Q99MN9
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
important for polyketide and fatty acid synthesis
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for long-chain fatty acids, polyketides and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Q99MN9
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
P05166
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Q5LUF3
the enzyme has a preference for propanoyl-CoA over acetyl-CoA as the substrate
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Q877I4 and Q877I3 and Q877I5
the bifunctional enzyme also catalyzes the carboxylation of acetyl-CoA. Vmax/Km for carboxylation of propanoyl-CoA is 1.6fold higher than Vmax/Km for carboxylation of acetyl-CoA. Quite specific for ATP. No activity with ADP, AMP, GTP, CTP, UTP, or dTTP (0.2 mM)
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Rhizobium leguminosarum bv. viciae MNF300, Agrobacterium tumefaciens IAM13299
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK-70-fl
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Azorhizobium caulinodans ORS571
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK70-fl
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Sinorhizobium fredii USDA205
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Metallosphaera sedula TH2
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Metallosphaera sedula TH2
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Acidianus infernus So4a
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Sinorhizobium meliloti Rm1021, Rhizobium etli 12-53
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Sulfolobus metallicus Krs23
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Sulfolobus metallicus Kra23
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK-70fl
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Mesorhizobium huakuii CCBAU2609
-
-
-
-
?
ATP + propanoyl-CoA + HCO3-
?
show the reaction diagram
-
key enzyme of the 3-hydroxypropanoate cycle
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (2S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + propionyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
preferred substrate
-
-
?
ATP + succinyl-CoA + HCO3-
ADP + phosphate + ?
show the reaction diagram
-
-
-
?
butyryl-CoA + CO2
?
show the reaction diagram
Q9X4K7
-
-
-
?
propionyl-CoA + CO2
(2S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + CO2
(2S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + CO2
(2S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + CO2
(2S)-methylmalonyl-CoA
show the reaction diagram
Streptomyces hygroscopicus ATCC 29253
-
-
-
-
?
propionyl-CoA + CO2
(S)-methylmalonyl-CoA
show the reaction diagram
Q9X4K7
-
-
-
?
propionyl-CoA + CO2
(S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + CO2
(S)-methylmalonyl-CoA
show the reaction diagram
Q5LUF3
the enzyme has a preference for propionyl-CoA over acetyl-CoA as the substrate
-
-
?
UTP + propanoyl-CoA + HCO3-
UDP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Metallosphaera sedula, Metallosphaera sedula TH2
-
40% of the activity with ATP
-
?
GTP + propanoyl-CoA + HCO3-
GDP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Metallosphaera sedula, Metallosphaera sedula TH2
-
10% of the activity with ATP
-
?
additional information
?
-
-
methylmalonyl-CoA, malonyl-CoA, isobutyryl-CoA, and isovaleryl-CoA are not metabolized
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
-
additional information
?
-
-
required for development of Myxococcus xanthus. The dcm-1 mutant, which is deficient in propanoyl-CoA carboxylase is unable to form fruiting bodies and spores
-
-
-
additional information
?
-
-
enzyme may play an important role in the biosynthesis of rifamycin as well as in the degradation of various amino acids
-
-
-
additional information
?
-
-
acetyl-CoA is not well converted to malonyl-CoA
-
-
-
additional information
?
-
Q9X4K7
the wild type enzyme shows no activity with acetyl-CoA
-
-
-
additional information
?
-
Q877I4 and Q877I3 and Q877I5
neither succinyl-CoA, palmitoyl-CoA, acetate (plus 0.5 mM CoASH), propionate (plus 0.5 mM CoASH), nor pyruvate is carboxylated by the enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
important for polyketide and fatty acid synthesis
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for long-chain fatty acids, polyketides and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Q99MN9
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
P05166
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
?
show the reaction diagram
-
key enzyme of the 3-hydroxypropanoate cycle
-
-
-
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK-70-fl
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Chloroflexus aurantiacus OK70-fl, Metallosphaera sedula TH2
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Metallosphaera sedula TH2
-
CO2 fixation during autotrophic growth, 3 -hydroxypropionate cycle
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
Acidianus infernus So4a, Sulfolobus metallicus Krs23, Sulfolobus metallicus Kra23, Chloroflexus aurantiacus OK-70fl
-
CO2 fixation during autotrophic growth, enzyme of the 3-hydroxypropionate cycle
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
-
additional information
?
-
-
required for development of Myxococcus xanthus. The dcm-1 mutant, which is deficient in propanoyl-CoA carboxylase is unable to form fruiting bodies and spores
-
-
-
additional information
?
-
-
enzyme may play an important role in the biosynthesis of rifamycin as well as in the degradation of various amino acids
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
Q5LUF3
-
biotin
-
biotin-containing enzyme
biotin
-
biotin-containing enzyme
biotin
-
6.2-6.3 mol of biotin per mol of enzyme; biotin-containing enzyme
biotin
-
4 mol of biotin bound per mol of enzyme; biotin-containing enzyme
biotin
-
3.8 mol of biotin per mol of enzyme; 4 mol of biotin bound per mol of enzyme; biotin-containing enzyme
biotin
-
biotin-containing enzyme
biotin
-
4 mol of biotin bound per mol of enzyme
biotin
-
bound to alpha-subunit of the enzyme
biotin
Q99MN9
bound to enzyme
biotin
-
bound to enzyme
biotin
-
bound to alpha subunit of the enzyme
biotin
-
bound to enzyme, very low activity when rats fed a biotin deficient diet for more than 2 weeks, in cell culture normal activity recovered 24 h after addition of biotin
biotin
-
bound to enzyme
biotin
-
dependent on
biotin
Q5LUF3
;
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
10% of the activity with Mg2+
Co2+
-
40% of the activity with Mg2+
Co2+
Q877I4 and Q877I3 and Q877I5
26% of the maximum activity is observed when Co2+(10 to 15 mM) is used as a divalent cation
Cs+
-
20 mM, activates, monovalent cation required
K+
-
stimulates, Km: 9.4 mM
K+
-
20 mM, activates, monovalent cation required
Mg2+
-
required for the formation of an Mg-ATP complex, highest activity between 1.5-2.0 mM (at 1.0-1.3 mM ATP)
Mg2+
-
required for the formation of Mg-ATP complex, optimum concentration 5 mM at 5 mM ATP
Mg2+
P05166
required to form a complex with ATP
Mg2+
Q877I4 and Q877I3 and Q877I5
maximum acetyl-CoA carboxylase activity is obtained at 4.0 mM
Mn2+
-
10% of the activity with Mg2+
Mn2+
Q877I4 and Q877I3 and Q877I5
1.0 mM Mn2+ gives 82% of the maximum activity obtained with the Mg2+ ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
weak inhibition
ATP
Q877I4 and Q877I3 and Q877I5
above 2.0 mM
citrate
Q877I4 and Q877I3 and Q877I5
3 mM, more than 50% inhibition
CoA
-
activity on propanoyl-CoA is more strongly inhibited than activity of acetyl-CoA
CoA
Q877I4 and Q877I3 and Q877I5
1 mM, 60% inhibition of propionyl-CoA carboxylase
DTT
Q877I4 and Q877I3 and Q877I5
5-10 mM, 12% inhibition
K+
Q877I4 and Q877I3 and Q877I5
-
L-alanine
-
-
L-phenylalanine
-
-
L-serine
-
-
L-tryptophan
-
strong inhibitor
L-tyrosine
-
-
L-valine
-
-
malonyl-CoA
-
activity on propanoyl-CoA is more strongly inhibited than activity of acetyl-CoA
malonyl-CoA
Q877I4 and Q877I3 and Q877I5
0.5 mM, 60% inhibition of propionyl-CoA carboxylase
methylmalonyl-CoA
Q877I4 and Q877I3 and Q877I5
0.5 mM, 60% inhibition of propionyl-CoA carboxylase
Mg2+
Q877I4 and Q877I3 and Q877I5
above 4.0 mM
Mn2+
Q877I4 and Q877I3 and Q877I5
above 2.0 mM
Na+
Q877I4 and Q877I3 and Q877I5
-
palmitoyl-CoA
-
-
succinyl-CoA
-
activity on propanoyl-CoA is more strongly inhibited than activity of acetyl-CoA
succinyl-CoA
Q877I4 and Q877I3 and Q877I5
0.5 mM, 57% inhibition of propionyl-CoA carboxylase
sulfate
Q877I4 and Q877I3 and Q877I5
25 mM, more than 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
Q877I4 and Q877I3 and Q877I5
biotin-dependent enzyme
NH4+
-
20 mM, activates, monovalent cation required
palmitoyl-CoA
Q877I4 and Q877I3 and Q877I5
slight stimulative effect on acetyl-CoA carboxylase (116%) and propionyl-CoA carboxylase (135%)
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
acetyl-CoA
-
-
0.06
acetyl-CoA
-
pH 7.5, 65C
0.25
acetyl-CoA
-
pH 7.2, 30C
0.31
acetyl-CoA
-
-
0.335
acetyl-CoA
Q9X4K7
mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30C
4.6
acetyl-CoA
-
pH 8, 30C, wild-type
4.8
acetyl-CoA
-
pH 8, 30C, mutant A431C
5
acetyl-CoA
-
pH 8, 30C, mutant A431I
0.036
ATP
-
pH 7.2, 30C
0.04
ATP
-
pH 7.5, 65C
0.08
ATP
-
-
1.2
Butanoyl-CoA
-
-
1.5
Butanoyl-CoA
-
-
0.036
Butyryl-CoA
Q9X4K7
mutant enzyme D422C, in 100 mM potassium phosphate, pH 7.6, at 30C
0.059
Butyryl-CoA
Q9X4K7
mutant enzyme D422A, in 100 mM potassium phosphate, pH 7.6, at 30C
0.104
Butyryl-CoA
Q9X4K7
wild type enzyme, in 100 mM potassium phosphate, pH 7.6, at 30C
0.144
Butyryl-CoA
-
-
0.22
Butyryl-CoA
-
pH 7.2, 30C
0.317
Butyryl-CoA
Q9X4K7
mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30C
0.383
Butyryl-CoA
Q9X4K7
mutant enzyme D422V, in 100 mM potassium phosphate, pH 7.6, at 30C
0.3
HCO3-
-
pH 7.5, 65C
1.13
HCO3-
-
pH 7.2, 30C
3
HCO3-
-
-
7
HCO3-
-
-
0.035
propanoyl-CoA
-
-
0.064
propanoyl-CoA
-
-
0.07
propanoyl-CoA
-
pH 7.5, 65C
0.1
propanoyl-CoA
-
-
0.1
propanoyl-CoA
Q877I4 and Q877I3 and Q877I5
pH 7.5, 70C
0.2
propanoyl-CoA
-
-
0.28
propanoyl-CoA
-
37C, pH 8.0, mutant enzyme E168K
0.29
propanoyl-CoA
-
-
0.32
propanoyl-CoA
-
crude extract
0.33
propanoyl-CoA
-
37C, pH 8.0, mutant enzyme R165W
0.41
propanoyl-CoA
-
37C, pH 8.0, wild-type enzyme
0.54
propanoyl-CoA
-
37C, pH 8.0, mutant enzyme R410W
0.59
propanoyl-CoA
-
37C, pH 8.0, mutant enzyme A497V
2.6
propanoyl-CoA
-
-
0.032
propionyl-CoA
-
pH 7.2, 30C
0.056
propionyl-CoA
Q9X4K7
mutant enzyme D422C, in 100 mM potassium phosphate, pH 7.6, at 30C
0.076
propionyl-CoA
Q9X4K7
wild type enzyme, in 100 mM potassium phosphate, pH 7.6, at 30C
0.077
propionyl-CoA
Q9X4K7
mutant enzyme D422V, in 100 mM potassium phosphate, pH 7.6, at 30C
0.1 - 1
propionyl-CoA
-
pH 8, 30C, wild-type
0.123
propionyl-CoA
Q9X4K7
mutant enzyme D422N, in 100 mM potassium phosphate, pH 7.6, at 30C
0.159
propionyl-CoA
Q9X4K7
mutant enzyme D422L, in 100 mM potassium phosphate, pH 7.6, at 30C
0.24
propionyl-CoA
-
pH 8, 30C, mutant A431C
0.262
propionyl-CoA
Q9X4K7
mutant enzyme D422A, in 100 mM potassium phosphate, pH 7.6, at 30C
0.315
propionyl-CoA
Q9X4K7
mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30C
1.3
propionyl-CoA
-
pH 8, 30C, mutant A431I
1.01
succinyl-CoA
-
pH 7.2, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.66
acetyl-CoA
-
pH 8, 30C, wild-type
1.4
acetyl-CoA
-
pH 8, 30C, mutant A431I
4
acetyl-CoA
-
pH 8, 30C, mutant A431C
2 - 8
propanoyl-CoA
-
pH 7.5, 65C
0.47
propionyl-CoA
-
pH 8, 30C, mutant A431I
1.46
propionyl-CoA
-
pH 8, 30C, mutant A431C
2.86
propionyl-CoA
-
pH 8, 30C, wild-type
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.144
acetyl-CoA
-
pH 8, 30C, wild-type
29
0.274
acetyl-CoA
-
pH 8, 30C, mutant A431I
29
0.826
acetyl-CoA
-
pH 8, 30C, mutant A431C
29
0.367
propionyl-CoA
-
pH 8, 30C, mutant A431I
350
6.09
propionyl-CoA
-
pH 8, 30C, mutant A431C
350
26
propionyl-CoA
-
pH 8, 30C, wild-type
350
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00186
-
cell culture
0.00199
-
cell culture
0.00442
-
cell culture
0.00483
-
cell culture
0.00535
-
cell culture
0.00673
-
cell culture
0.01177
-
cell culture
0.0248
-
cell culture
3.3
-
purified enzyme, pH 7.5, 65C
5.6
-
-
7.54
-
purified mutant enzyme E168K
9.93
-
purified mutant enzyme R165W
9.95
-
purified mutant enzyme R410W
11.9
Q877I4 and Q877I3 and Q877I5
pH 7.5, 70C, propionyl-CoA carboxylase activity
14.13
-
purified enzyme, pH 7.2, 30C
23.35
-
purified wild-type enzyme
27.7
-
-
32.34
-
purified mutant enzyme A497V
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 6.9
Q877I4 and Q877I3 and Q877I5
at 70C
7.2 - 8.8
-
-
7.5 - 8.3
-
-
7.5 - 8.5
-
-
7.5
Q877I4 and Q877I3 and Q877I5
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 9.6
-
7.2-8.8: maximal activity, 9.6: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
-
-
65
Q877I4 and Q877I3 and Q877I5
-
70
Q877I4 and Q877I3 and Q877I5
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 75
Q877I4 and Q877I3 and Q877I5
50C: about 60% of maximal activity, 75C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
P14882
in all regions of the adult rat brain
Manually annotated by BRENDA team
P14882
embryo, high level
Manually annotated by BRENDA team
P14882
adult, PCC together with methylmalonyl-CoA mutase and in whole rat embryonic central nervous system, both at E15.5 and E18.5, PCCalpha is present in all regions of the central nervous system. PCCalpha is present in the whole embryonic central nervous system, both at E15.5 and E18.5, predominantely in the periventricular zones of telencephalon, midbrain and rhombencephalon
Manually annotated by BRENDA team
P14882
adult, highest level, Purkinje and granular layers, pons, medulla and the Purkinje and granular layers
Manually annotated by BRENDA team
P14882
adult and embryo
Manually annotated by BRENDA team
P14882
in embryos (E15.5 and E18.5), PCCalpha shows a much higher expression level in the entire central nervous system than in the liver
Manually annotated by BRENDA team
P14882
adult, highest level
Manually annotated by BRENDA team
P14882
adult, highest level
Manually annotated by BRENDA team
P14882
in embryos (E15.5 and E18.5), PCCalpha shows a much higher expression level in the entire central nervous system than in the liver, low levels in the E15.5 embryonic liver
Manually annotated by BRENDA team
P14882
adult, highest level
Manually annotated by BRENDA team
P14882
adult, PCC together with methylmalonyl-CoA mutase, basal ganglia, both, methylmalonyl-CoA mutase and PCCalpha enzymes are co-expressed in neurons. PCCalpha is present in neurons of basal ganglia
Manually annotated by BRENDA team
-
developing
Manually annotated by BRENDA team
P14882
embryo, in the periventricular zones
Manually annotated by BRENDA team
P14882
adult, highest level
Manually annotated by BRENDA team
P14882
adult, highest level, such as the red nucleus and substantia nigra, as well as pons and medulla, and in embryo, red nucleus and substantia nigra
Manually annotated by BRENDA team
additional information
-
cell line 3152 and cell line 13042
Manually annotated by BRENDA team
additional information
P14882
in adult, absent from astrocytes, oligodendrocytes and microcapillary endothelial cells (blood-brain barrier). Present in rhombencephalon of embryos, PCCalpha is present in choroid plexus epithelium, is absent from astrocytes and oligodendrocytes and in microcapillary endothelial cells (blood brain barrier)
Manually annotated by BRENDA team
additional information
-
two-years-old girl with propionic acidemia
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63400
-
SDS-PAGE
728270
72000
P14882
SDS-PAGE, Western blot analysis; Western blot analysis, PCCalpha in the adult brain and liver
705936
450000
-
gel filtration
1878
500000
-
PAGE, gel filtration, sucrose density gradient ultracentrifugation
1869
540000
-
gel filtration
1868
540000
Q877I4 and Q877I3 and Q877I5
-
725234
560000
-
gel filtration
651169
605000 - 615000
-
gel filtration
649502
620000
-
gel filtration
662786
669000
-
alpha4beta4 quaternary structure
726557
690000
-
calculation from sedimentation and diffusion data
1873
730000
-
analytical ultracentrifugation
1866
750000
Q5LUF3
; gel filtration
716328
800000
P05166
-
651459
800000
-
gel filtration
653246, 662392
additional information
-
contains the tripeptide Pro-Met-Pro, 26 residues towards the amino terminus from the biotin attachment site
1863
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
?
-
x * 72000, alpha, + x * 56000, beta, SDS-PAGE under reducing conditions
?
-
x * 74000, biotin-containing, + x * 58000, SDS-PAGE
?
-
x * 57000 + x * 64000, SDS-PAGE of mercaptoethanol-treated enzyme
?
-
x * 64000 + x * 77000, SDS-PAGE under reducing conditions
?
-
x * 70000, propionyl-coA carboxylase alpha chain, mass spectrometry
dodecamer
-
a larger hexameric central subunit to which six biotinylated peripheral subunits are attached
dodecamer
-
6 * alpha + 6 * beta
dodecamer
Q99MN9
6 * alpha + 6 * beta
dodecamer
-
6 alpha and 6 beta subunits
dodecamer
-
alpha, beta, gamma, 4 * 57000 + 4 * 57000 + 4 * 18600, SDS-PAGE, biotin carboxylase (alpha subunit), carboxyl transferase (beta subunit) and biotin carrier protein (gamma subunit)
dodecamer
-
alpha6beta6
dodecamer
-
alpha6beta6, 6 * 74000 + 6 * 45000, SDS-PAGE
dodecamer
Q877I4 and Q877I3 and Q877I5
4 * 62000 + 4 * 59000 + 4 * 20000, SDS-PAGE
dodecamer
Metallosphaera sedula TH2
-
alpha, beta, gamma, 4 * 57000 + 4 * 57000 + 4 * 18600, SDS-PAGE, biotin carboxylase (alpha subunit), carboxyl transferase (beta subunit) and biotin carrier protein (gamma subunit)
-
dodecamer
Rhizobium etli 12-53
-
alpha6beta6, 6 * 74000 + 6 * 45000, SDS-PAGE
-
heterododecamer
Q5LUF3
alpha6beta6-heterododecamer, the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity, the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity
multimer
-
6 * 56000 + 6 * 53000, SDS-PAGE, composed of biotin carboxylase (alpha-subunit) and carboxyltransferase (beta-subunit)
multimer
-
alpha,beta, alpha subunit: 72000 Da
multimer
-
biotin carboxylase (alpha-subunit) and carboxyl transferase (beta-subunit)
heterododecamer
-
the alpha-subunit contains the biotin carboxylase and biotin carboxyl carrier protein domains, whereas the beta-subunit supplies the carboxyltransferase activity
additional information
-
propionyl-coA carboxylase alpha chain associates with neurofibromin
additional information
I3R7G3 and I3R7F1 and I3R7F2
the enzyme consists of a fusion protein of a biotin carboxylase and a biotin-carboxyl carrier protein (PccA, HFX_2490), a carboxyltransferase component (PccB, HFX_2478), and an essential small subunit (PccX, HFX_2479)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a PCC chimaera, containing the alpha-subunit of Ruegeria pomeroyi PCC and the beta-subunit of Roseobacter denitrificans PCC is crystallized by the microbatch method under paraffin oil, using 0.1 M HEPES (pH 8.0), 22% (w/v) PEG3350, 0.2 M NaCl and 16% (v/v) glycerol. Crystals of Ruegeria pomeroyi PCC are obtained at 20C by the microbatch method under paraffin oil, using 0.2 M succinic acid (pH 6.5), 22% (w/v) benzamidine and 22% (w/v) PEG3000; microbatch method under oil method
Q5LUF3
apo and substrate-bound crystal structure of PccB hexamers determined to 2.0-2.8 A. crystallization of PccB in sitting drops at room temperature by vapor diffusion. PccB is the core catalytic beta subunit of the propanoyl-CoA carboxylase multisubunit complex
-
sitting drop vapor diffusion method, mutant enzymes D422V and D422Lwith 0.1 M Tris pH 6.5, 2.0 M (NH4)SO4, mutant enzyme D422N with 0.1 M Bis-Tris pH 6.8, 10% (w/v) MPD, 0.2 M (NH4)OAc, mutant enzyme D422C with 0.1 M Na citrate pH 5.6, 0.2 M (NH4)SO4, and mutant enzyme D422A with 0.1 M Bis-Tris pH 6.2, 20% (w/v) PEG3350, 0.2 M (NH4)SO4
Q9X4K7
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.7
-
15 min, stable between 6-8, strong denaturation above pH 8.7, liver enzyme
1878
6.2 - 8.4
-
stable
1868
8 - 9.5
-
maximal stability, mammary gland enzyme
1878
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-50 - 37
-
stable
1868
0 - 40
-
maximal stability
1878
37
-
15 min, stable
1878
37
-
30 min, wild-type enzyme is stable, mutant enzymes R165W, E168K and R410W lose 30% of their activity
662392
47
-
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
662392
50
Q877I4 and Q877I3 and Q877I5
2 h, 40% loss of activity
725234
58
-
the wild-type enzyme undergoes a cooperative two-state transition between the native and denatured states with a Tm of 57.6C
662392
60
Q877I4 and Q877I3 and Q877I5
30 min, 50% loss of activity
725234
70
Q877I4 and Q877I3 and Q877I5
30 min, 90% loss of activity
725234
80
Q877I4 and Q877I3 and Q877I5
30 min, 95% loss of activity
725234
90
Q877I4 and Q877I3 and Q877I5
10 min, complete loss of activity
725234
additional information
-
thermal denaturation is irreversible
662392
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
-
crude enzyme is relatively unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 20 mM phosphate buffer, pH 7.0, 2-4 weeks, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q877I4 and Q877I3 and Q877I5
recombinant
-
recombinant enzymes from Escherichia coli
P05166
using Ni-NTA chromatography
-
nickel affinity column chromatography and gel filtration; nickel affinity column chromatography and gel filtration
Q5LUF3
nickel affinity column chromatography
Q9X4K7
Ni-NTA agarose CL-6B resin column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q877I4 and Q877I3 and Q877I5
expressed in Escherichia coli as a His-tagged fusion protein. Recombinant PCC, including the His tag are produced and are confirmed to react with clonorchiasis patient sera
-
correction of enzyme deficiency in pccA fibroblasts
-
expressed in COS-7 cells at 27C and 37C
-
expressed in Escherichia coli
-
expressed using a two hybrid system in COS cells
-
expression in Escherichia coli
-
expression of alpha and beta subunit in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli
Q5LUF3
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 lambda(DE3) cells
Q9X4K7
expressed in Saccharomyces cerevisiae
-
gene encoding the biotin-containing subunit
-
into plasmid pSET152 derivative containing an ermE* promoter, yielding pYJ269, expressed in Streptomyces clavuligerus CKD1119
-
subunits individually cloned and expressed in Escherichia coli DH5alpha
-
introduced into Streptomyces hygroscopicus UV2-2 strain by conjugation from Escherichia coli ET12567/pUZ8002
-
the PccB subunit is expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in rat embryos (E15.5 and E18.5), methylmalonyl-CoA mutase and PCC show a much higher expression level in the entire central nervous system than in the liver
P14882
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A487V
-
no effect on activity
A497V
-
beta subunit, no effect on subunit interactions and activity
A497V
P05166
significantly increased activity
A497V
-
polymorphism, 30% higher specific activity than wild-type enzyme
A513_R514insP
-
insertion between residues 513 and 514 of the beta subunit, leads to partial degradation of the subunit, strongly reduced activity
A513_R514insP
P05166
insertion, severe degradation of the subunit
D178H
P05166
increased alpha/beta subunit ratio, very low activity
DELTA408
P05166
catalytically inactive
DELTA499
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA499
P05166
severe degradation of the subunit
DELTA514
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA514
P05166
severe degradation of the subunit
DELTA531
-
very low activity
DELTA531
-
beta subunit, no effect
DELTA531
-
beta subunit, strongly affects subunit interactions, very low activity
E168K
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
E168K
P05166
increased alpha/beta subunit ratio, very low activity
E168K
-
mutant enzyme shows 32.3% of the specific activity of purified wild-type enzyme
G131R
P05166
catalytically inactive
G131R
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
G198D
P05166
catalytically inactive
G198D
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C) reduced activity at 37C
G246V
-
activity of the mutant enzyme is 12% of the wild-type activity
L519P
-
very low activity
L519P
-
beta subunit, leads to complete degradation of the subunit, no activity
L519P
-
beta subunit, strongly affects subunit interactions, very low activity
L519P
P05166
complete degradation of the subunit
L519P
-
activity of the mutant enzyme is less than 1% of the wild-type activity
N536D
-
beta subunit, leads to complete degradation of the subunit, no activity
N536D
-
beta subunit, strongly affects subunit interactions, very low activity
N536D
P05166
complete degradation of the subunit
P228L
P05166
increased alpha/beta subunit ratio, very low activity
R165Q
-
beta subunit, no effect on subunit interactions and activity
R165W
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
R165W
P05166
increased alpha/beta subunit ratio, very low activity
R165W
-
activity of the mutant enzyme is less than 1% of the wild-type activity
R165W
-
mutant enzyme shows 42.5% of the specific activity of purified wild-type enzyme
R410W
P05166
very low activity
R410W
-
activity of the mutant enzyme is 9% of the wild-type activity
R410W
-
mutant enzyme shows 42.61% of the specific activity of purified wild-type enzyme
R44P
P05166
catalytically inactive
R512C
-
very low activity
R512C
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
R512C
-
beta subunit, strongly affects subunit interactions, very low activity
R512C
P05166
severe degradation of the subunit
R512C
-
activity of the mutant enzyme is less than 1% of the wild-type activity
R67S
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
S106R
P05166
catalytically inactive
S106R
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
V205D
P05166
catalytically inactive
V205D
P05166
increased alpha/beta subunit ratio
V205D
-
activity of the mutant enzyme is less than 1% of the wild-type activity
W531X
-
activity of the mutant enzyme is less than 1% of the wild-type activity
A431C
-
kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type
A431D
-
mutant enzyme shows no activity
A431I
-
kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type
A431L
-
mutant enzyme shows no activity
D440I
Q5LUF3
the mutation does not change the substrate preference of the enzyme
G668R
Q5LUF3
the mutation in the biotin carboxyl carrier protein domain abolishes biotinylation
R165Q
Q5LUF3
the mutation disturbs the recognition of the adenine base of CoA
R165W
Q5LUF3
the mutation disturbs the recognition of the adenine base of CoA
R399Q
Q5LUF3
the mutation leads to a large loss in activity
D422A
Q9X4K7
mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate
D422C
Q9X4K7
mutant of the PccB subunit, shows strong preference for butyryl-CoA as substrate
D422I
Q9X4K7
mutant of the PccB subunit, accepts acetyl-CoA, propionyl-CoA, and butyrl-CoA as substrates, the latter two with lower Vmax/Km values as compared to the wild type enzyme
D422L
Q9X4K7
mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate
D422N
Q9X4K7
mutant of the PccB subunit, the mutants has narrowed down their substrate specificity, accepting only propionyl-CoA as its substrate
D422V
Q9X4K7
mutant of the PccB subunit, accepts both propionyl-CoA and butyrl-CoA as substrates but with lower Vmax/Km values as compared to the wild type enzyme
M442T
P05166
catalytically inactive
additional information
-
intragenic complementation analysis to 15 naturally occuring mutations in the PCCB gene
Y430H/A431I
-
mutant enzyme shows no activity
additional information
-
stringent model of propionyl CoA carboxylase subunit A deficiency, where homozygous knock-out mice are born, but die within 36 hours. Injection of vectors expressing propionyl CoA carboxylase subunit A significantly increases the lifespan for both unmodified and polyethylene glycol modified vectors, but the rescue is transient
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
propionyl-CoA carboxylase is a sensitive indicator of biotin status
medicine
-
living-donor liver transplantation is an effective treatment modality in patients with congenial metabolic liver disease, i. e., propionic acidemia caused by deficiency in propionyl-CoA carboxylase
medicine
-
stringent model of propionyl CoA carboxylase subunit A deficiency, where homozygous knock-out mice are born, but die within 36 hours. Injection of vectors expressing propionyl CoA carboxylase subunit A significantly increases the lifespan for both unmodified and polyethylene glycol modified vectors, but the rescue is transient