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 ACCESSION NO.
LITERATURE
ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
3-hydroxypropionate cycle
-
3-hydroxypropionate/4-hydroxybutyrate cycle
-
anaerobic energy metabolism (invertebrates, mitochondrial)
-
Carbon fixation pathways in prokaryotes
-
Glyoxylate and dicarboxylate metabolism
-
Metabolic pathways
-
methylaspartate cycle
-
Microbial metabolism in diverse environments
-
mycolate biosynthesis
-
Propanoate metabolism
-
propionyl CoA degradation
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
AccA3-PccB complex
-
the AccA3-PccB complex of Streptomyces toxytricini has a PCCase activity rather than ACCase activity
acetyl-CoA/propionyl-CoA carboxylase
-
enzyme acts equally well on both substrates
acetyl-CoA/propionyl-CoA carboxylase
Chloroflexus aurantiacus OK-70-fl
-
enzyme acts equally well on both substrates
-
acetyl-CoA/propionyl-CoA carboxylase
-
enzyme acts equally well on both substrates
acetyl-CoA/propionyl-CoA carboxylase
Metallosphaera sedula TH2
-
enzyme acts equally well on both substrates
-
acetyl-CoA/propionyl-CoA carboxylase
-
enzyme acts equally well on both substrates
Carboxylase, propional coenzyme A (adenosine triphosphate-hydrolyzing)
-
-
-
-
Pcase
-
-
-
-
PCC
-
-
-
-
PCC
Agrobacterium tumefaciens IAM13299
-
-
-
PCC
Azorhizobium caulinodans ORS571
-
-
-
PCC
Bradyrhizobium japonicum USDA110
-
-
-
PCC
Mesorhizobium huakuii CCBAU2609
-
-
-
PCC
Rhizobium leguminosarum bv. viciae MNF300
-
-
-
PCC
-, Q5LUF3
-
PCC
Sinorhizobium fredii USDA205
-
-
-
PCC
Sinorhizobium meliloti Rm1021
-
-
-
PCC
Streptomyces hygroscopicus ATCC 29253
-
-
-
PCCase
-
-
-
-
PccB
Q9X4K7
beta-subunit
PccB
-
beta subunit of PCCase
PccE
Q9X4K7
epsilon-subunit
PccE
-
epsilon subunit of PCCase
Propanoyl-CoA:carbon dioxide ligase
-
-
-
-
Propionyl coenzyme A carboxylase
-
-
-
-
Propionyl coenzyme A carboxylase (adenosine triphosphate-hydrolyzing)
-
-
-
-
Propionyl coenzyme A carboxylase (ATP-hydrolyzing)
-
-
-
-
Propionyl-CoA carboxylase
-
-
Propionyl-CoA carboxylase
-
-
Propionyl-CoA carboxylase
-
-
Propionyl-CoA carboxylase
Q9X4K7
-
Propionyl-CoA carboxylase
-
-
Propionyl-CoA carboxylase
Streptomyces hygroscopicus ATCC 29253
-
-
-
Propionyl-CoA carboxylase
-
-
propionyl-coenzyme A carboxylase
-, Q5LUF3
-
propionyl-coenzyme A carboxylase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-94-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
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
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 ACCESSION NO.
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
-
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 + (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 + 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
Streptomyces hygroscopicus, 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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
dependent on
biotin
Q5LUF3, -
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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-phenylalanine
-
-
L-tryptophan
-
strong inhibitor
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 ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
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
0.123
-
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
0.262
-
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
1.01
-
succinyl-CoA
-
pH 7.2, 30C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
8
propanoyl-CoA
-
pH 7.5, 65C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00186
-
-
cell culture
0.00199
-
-
cell culture
0.00442
-
-
cell culture
0.00459
-
-
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
-
-
-
7.27
-
-
-
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
20
-
-
-
23.35
-
-
purified wild-type enzyme
27.7
-
-
-
32.34
-
-
purified mutant enzyme A497V
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
9.6
-
7.2-8.8: maximal activity, 9.6: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
40
-
-
65
-
Q877I4 and Q877I3 and Q877I5
-
70
-
Q877I4 and Q877I3 and Q877I5
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72000
-
P14882
SDS-PAGE, Western blot analysis; Western blot analysis, PCCalpha in the adult brain and liver
450000
-
-
gel filtration
500000
-
-
PAGE, gel filtration, sucrose density gradient ultracentrifugation
540000
-
-
gel filtration
540000
-
Q877I4 and Q877I3 and Q877I5
-
560000
-
-
gel filtration
605000
615000
-
gel filtration
620000
-
-
gel filtration
690000
-
-
calculation from sedimentation and diffusion data
730000
-
-
analytical ultracentrifugation
750000
-
Q5LUF3, -
; gel filtration
800000
-
-, P05166
-
800000
-
-
gel filtration
additional information
-
-
contains the tripeptide Pro-Met-Pro, 26 residues towards the amino terminus from the biotin attachment site
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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 * 57000 + x * 64000, SDS-PAGE of mercaptoethanol-treated enzyme
?
-
x * 74000, biotin-containing, + x * 58000, SDS-PAGE
?
-
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
-
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
Q99MN9
6 * alpha + 6 * beta
dodecamer
-
6 * alpha + 6 * beta
dodecamer
-
6 alpha and 6 beta subunits
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
-
multimer
-
6 * 56000 + 6 * 53000, SDS-PAGE, composed of biotin carboxylase (alpha-subunit) and carboxyltransferase (beta-subunit)
multimer
-
biotin carboxylase (alpha-subunit) and carboxyl transferase (beta-subunit)
multimer
-
alpha,beta, alpha subunit: 72000 Da
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
additional information
-
propionyl-coA carboxylase alpha chain associates with neurofibromin
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.7
-
15 min, stable between 6-8, strong denaturation above pH 8.7, liver enzyme
6.2
8.4
-
stable
8
9.5
-
maximal stability, mammary gland enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-50
37
-
stable
0
40
-
maximal stability
37
-
-
15 min, stable
37
-
-
30 min, wild-type enzyme is stable, mutant enzymes R165W, E168K and R410W lose 30% of their activity
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
50
-
Q877I4 and Q877I3 and Q877I5
2 h, 40% loss of activity
58
-
-
the wild-type enzyme undergoes a cooperative two-state transition between the native and denatured states with a Tm of 57.6C
60
-
Q877I4 and Q877I3 and Q877I5
30 min, 50% loss of activity
70
-
Q877I4 and Q877I3 and Q877I5
30 min, 90% loss of activity
80
-
Q877I4 and Q877I3 and Q877I5
30 min, 95% loss of activity
90
-
Q877I4 and Q877I3 and Q877I5
10 min, complete loss of activity
additional information
-
-
thermal denaturation is irreversible
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
4C, 20 mM phosphate buffer, pH 7.0, 2-4 weeks, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Q877I4 and Q877I3 and Q877I5
recombinant
-
recombinant enzymes from Escherichia coli
-, P05166
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 ACCESSION NO.
LITERATURE
-
Q877I4 and Q877I3 and Q877I5
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
-
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
A487V
-
no effect on activity
A497V
-, P05166
significantly increased activity
A497V
-
beta subunit, no effect on subunit interactions and activity
A497V
-
polymorphism, 30% higher specific activity than wild-type enzyme
A513_R514insP
-, P05166
insertion, severe degradation of the subunit
A513_R514insP
-
insertion between residues 513 and 514 of the beta subunit, leads to partial degradation of the subunit, strongly reduced activity
D178H
-, P05166
increased alpha/beta subunit ratio, very low activity
DELTA408
-, P05166
catalytically inactive
DELTA499
-, P05166
severe degradation of the subunit
DELTA499
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA514
-, P05166
severe degradation of the subunit
DELTA514
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA531
-
very low activity
DELTA531
-
beta subunit, no effect
DELTA531
-
beta subunit, strongly affects subunit interactions, very low activity
E168K
-, P05166
increased alpha/beta subunit ratio, very low activity
E168K
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
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
-, P05166
complete degradation of the subunit
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
-
activity of the mutant enzyme is less than 1% of the wild-type activity
N536D
-, P05166
complete degradation of the subunit
N536D
-
beta subunit, leads to complete degradation of the subunit, no activity
N536D
-
beta subunit, strongly affects subunit interactions, very low activity
P228L
-, P05166
increased alpha/beta subunit ratio, very low activity
R165Q
-
beta subunit, no effect on subunit interactions and activity
R165W
-, P05166
increased alpha/beta subunit ratio, very low activity
R165W
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27C), reduced activity at 37C
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
-, P05166
severe degradation of the subunit
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
-
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; increased alpha/beta subunit ratio
V205D
-
activity of the mutant enzyme is less than 1% of the wild-type 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
W531X
-
activity of the mutant enzyme is less than 1% of the wild-type 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 ACCESSION NO.
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