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Information on EC 6.4.1.3 - propionyl-CoA carboxylase and Organism(s) Homo sapiens and UniProt Accession P05165
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6.4.1.3 propionyl-CoA carboxylaseIUBMB Comments
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
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Word Map
- 6.4.1.3
- propionic
- acidemia
-
biotin-dependent
- carboxylases
- methylmalonyl-coa
- acidosis
-
methylmalonic
- 3-hydroxypropionate
-
methylcitrate
-
propionylation
-
hyperammonemia
- holocarboxylase
- 3-methylcrotonyl-coa
- acidurias
-
biotin-containing
- carboxyltransferase
-
biotin-deficient
- hyperglycinemia
- beta-methylcrotonyl-coa
-
biotin-binding
-
odd-chain
-
anaplerosis
- transcarboxylase
-
3-hydroxyisovaleric
- propionylcarnitine
- synthesis
- analysis
- medicine
- apocarboxylases
- biotinidase
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
propionyl-coa carboxylase, pccbc, propionyl-coenzyme a carboxylase, acetyl-coa/propionyl-coa carboxylase, pcca-1, pccb-1, pccase, propanoyl-coa:carbon-dioxide ligase (adp-forming), 
more
topSYNONYM 
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)
-
-
-
-
PCC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
CAS REGISTRY NUMBER
COMMENTARY
9023-94-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
at a rate 1.5% that obtained for propionyl-CoA
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
-
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
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
-
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
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
key enzyme in catabolic pathways for odd-chain fatty acids and branched chain amino acids
-
?
ATP + propanoyl-CoA + HCO3-
ADP + phosphate + (S)-methylmalonyl-CoA
-
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
-
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
key enzyme in catabolic pathways for odd-chain fatty acids, cholesterol and branched chain amino acids
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
?
additional information
?
-
-
inherited deficiency of the enzyme activity leads to propionicacidemia
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PCCB_HUMAN
539
0
58216
Swiss-Prot
Mitochondrion (Reliability: 1)
PCCA_HUMAN
728
0
80059
Swiss-Prot
Mitochondrion (Reliability: 2)
B2RDE0_HUMAN
703
0
77414
TrEMBL
Mitochondrion (Reliability: 3)
A0A1B0GU58_HUMAN
615
0
67344
TrEMBL
other Location (Reliability: 3)
H0Y4B9_HUMAN
134
0
14184
TrEMBL
other Location (Reliability: 2)
A0A1B0GWI4_HUMAN
461
0
50123
TrEMBL
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
-
x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
75000
-
x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
800000
additional information
-
contains the tripeptide Pro-Met-Pro, 26 residues towards the amino terminus from the biotin attachment site
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
?
-
x * 75000, biotin-containing subunit, + x * 60000, PAGE after reduction and alkylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A497V
A513_R514insP
DELTA499
DELTA514
DELTA531
E168K
G131R
G198D
L519P
N536D
R165W
R410W
R512C
R67S
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
S106R
V205D
additional information
-
intragenic complementation analysis to 15 naturally occuring mutations in the PCCB gene
A513_R514insP
-
insertion between residues 513 and 514 of the beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA499
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA514
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
DELTA531
-
beta subunit, strongly affects subunit interactions, very low activity
E168K
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
E168K
-
mutant enzyme shows 32.3% of the specific activity of purified wild-type enzyme
G131R
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
G198D
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C) reduced activity at 37°C
R165W
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
R165W
-
mutant enzyme shows 42.5% of the specific activity of purified wild-type enzyme
R410W
-
mutant enzyme shows 42.61% of the specific activity of purified wild-type enzyme
R512C
-
beta subunit, leads to partial degradation of the subunit, strongly reduced activity
S106R
-
beta subunit, no effect on subunit interactions only when expressed at low temperature (27°C), reduced activity at 37°C
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
58
-
the wild-type enzyme undergoes a cooperative two-state transition between the native and denatured states with a Tm of 57.6°C
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
method to analyze propionyl-CoA carboxylase activity in phytohemagglutinin stimulated lymphocytes using high performance liquid chromatography. Propionyl-CoA carboxylase activity is unaffected even when lymphocytes are isolated and phytohemagglutinin stimulated after a whole blood sample has been stored at 4°C for 5 days, and the method is useful for the confirmation of propionic acidemia in individuals, and prenatal diagnosis and genetic counseling for the affected families
medicine
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
treatment of propionic acidemia by import of a biologically active, fully assembled propionyl-CoA carboxylase dodecamer, posttranslationally chemically conjugated with the HIV TAT peptide. TAT-propionyl-CoA carboxylase is transferred into isolated mitochondria, as well as into mitochondria of patient fibroblasts . A single-dose intraperitoneal injection into propionyl-CoA carboxylase-deficient mice decreases the propionylcarnitine/acetylcarnitine (C3/C2) ratio toward the normal level
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lamhonwah, A.M.; Quan, F.; Gravel, R.A.
Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase
Arch. Biochem. Biophys.
254
631-636
1987
Homo sapiens
Gravel, R.A.; Lam, F.K.; Mahuran, D.; Kronis, A.
Purification of human liver propionyl-CoA carboxylase by carbon tetrachloride extraction and monomeric avidin affinity chromatography
Arch. Biochem. Biophys.
201
669-673
1980
Homo sapiens
Kalousek, F.; Darigo, M.D.; Rosenberg, L.E.
Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits
J. Biol. Chem.
255
60-65
1980
Homo sapiens
Lamhonwah, A.M.; Mahuran, D.; Gravel, R.A.
Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro-and mature alpha chains in the deduced primary sequence of a full-length cDNA
Nucleic Acids Res.
17
4396
1989
Homo sapiens
Stankovic, J.; Ledley, F.D.
Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts
Am. J. Hum. Genet.
52
144-151
1993
Homo sapiens
Kelson, T.L.; Ohura, T.; Kraus, J.P.
Chaperonin-mediated assembly of wild-type and mutant subunits of human propionyl-CoA carboxylase expressed in Escherichia coli
Hum. Mol. Genet.
5
331-337
1996
Homo sapiens
Schrick, J.J.; Lingrel, J.B.
cDNA cloning, mapping and expression of the mouse propionyl CoA carboxylase beta (pccb), the gene for human type II propionic acidaemia
Gene
264
147-152
2001
Homo sapiens, Mus musculus (Q99MN9)
Chloupkova, M.; Maclean, K.N.; Alkhateeb, A.; Kraus, J.P.
Propionic acidemia: analysis of mutant propionyl-CoA carboxylase enzymes expressed in Escherichia coli
Hum. Mutat.
19
629-640
2002
Homo sapiens, Homo sapiens (P05166)
Muro, S.; Perez, B.; Rodriguez-Pombo, P.; Desviat, L.R.; Perez-Cerda, C.; Ugarte, M.
Mutations affecting the beta-beta homomeric interaction in propionic acidaemia: An approach to the determination of the beta-propionyl-CoA carboxylase functional domains
J. Inherit. Metab. Dis.
23
300-304
2000
Homo sapiens
Chloupkova, M.; Ravn, K.; Schwartz, M.; Kraus, J.P.
Changes in the carboxyl terminus of the beta subunit of human propionyl-CoA carboxylase affect the oligomer assembly and catalysis: expression and characterization of seven patient-derived mutant forms of PCC in Escherichia coli
Mol. Genet. Metab.
71
623-632
2000
Homo sapiens
Muro, S.; Perez, B.; Desviat, L.R.; Rodriguez-Pombo, P.; Perez-Cerda, C.; Clavero, S.; Ugarte, M.
Effect of PCCB gene mutations on the heteromeric and homomeric assembly of propionyl-CoA carboxylase
Mol. Genet. Metab.
74
476-483
2001
Homo sapiens
Rodriguez-Pombo, P.; Perez-Cerda, C.; Perez, B.; Desviat, L.R.; Sanchez-Pulido, L.; Ugarte, M.
Towards a model to explain the intragenic complementation in the heteromultimeric protein propionyl-CoA carboxylase
Biochim. Biophys. Acta
1740
489-498
2005
Homo sapiens
Jiang, H.; Rao, K.S.; Yee, V.C.; Kraus, J.P.
Characterization of four variant forms of human propionyl-CoA carboxylase expressed in Escherichia coli
J. Biol. Chem.
280
27719-27727
2005
Homo sapiens
Stratton, S.L.; Bogusiewicz, A.; Mock, M.M.; Mock, N.I.; Wells, A.M.; Mock, D.M.
Lymphocyte propionyl-CoA carboxylase and its activation by biotin are sensitive indicators of marginal biotin deficiency in humans
Am. J. Clin. Nutr.
84
384-388
2006
Homo sapiens
Lee, T.M.; Addonizio, L.J.; Barshop, B.A.; Chung, W.K.
Unusual presentation of propionic acidaemia as isolated cardiomyopathy
J. Inherit. Metab. Dis.
23
S97-101
2009
Homo sapiens
Sato, S.; Kasahara, M.; Fukuda, A.; Mizuguchi, K.; Nakagawa, S.; Muguruma, T.; Saito, O.; Karaki, C.; Nakagawa, A.; Yoshii, K.; Horikawa, R.
Liver transplantation in a patient with propionic acidemia requiring extra corporeal membrane oxygenation during severe metabolic decompensation
Pediatr. Transplant.
13
790-793
2009
Homo sapiens
Liu, Y.N.; Liu, T.T.; Fan, Y.L.; Niu, D.M.; Chien, Y.H.; Chou, Y.Y.; Lee, N.C.; Hsiao, K.J.; Chiu, Y.H.
Measuring propionyl-CoA carboxylase activity in phytohemagglutinin stimulated lymphocytes using high performance liquid chromatography
Clin. Chim. Acta
453
13-20
2016
Homo sapiens
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