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Gene Review

PCCB  -  propionyl CoA carboxylase, beta polypeptide

Homo sapiens

Synonyms: PCCase subunit beta, Propanoyl-CoA:carbon dioxide ligase subunit beta, Propionyl-CoA carboxylase beta chain, mitochondrial
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Disease relevance of PCCB

  • Mutations in the PCCA (alpha subunit) or PCCB (beta subunit) gene can cause the inherited metabolic disease propionic acidemia (PA), which can be life threatening in the neonatal period [1].
  • Other PCCB mutants (R165W, E168K, D178H, P228L, and R410W) that are PCC deficient in patient-derived fibroblasts, were found to be capable of expressing wild-type level PCC activity when assembled in our chaperone-assisted E. coli expression system [2].
  • In all cases, the levels of mRNA were lower in colorectal cancers than in normal mucosae, the decrease being always more marked for PCCB than for PCCA [3].

High impact information on PCCB

  • PCC consists of two subunits, alpha and beta, encoded by the PCCA and PCCB genes, respectively [4].
  • Lack of data on the genomic structure of PCCB has been a significant impediment to full characterization of PCCB mutant chromosomes [1].
  • About two-thirds of fibroblast lines from patients with mutations in the PCCB (beta-subunit) gene show interallelic complementation in cell fusion experiments (the pccB and pccC subgroups of the pccBC major group defining beta-subunit mutations, where pccB x pccC fusions show complementation) [5].
  • Expression of the MCCB and PCCB chains that do not carry the biotin-binding motif did not change significantly; we speculate that expression of the biotin-binding chains of biotin-dependent carboxylases is more responsive to biotin status changes [6].
  • We have also analysed the effect of mutations c.653A>G and IVS10-11del6 in the PCCB gene present in heterozygous patients with mild phenotype [7].

Chemical compound and disease context of PCCB


Biological context of PCCB

  • By use of a panel of somatic mouse-human hybrids, the human gene encoding the alpha polypeptide (PCCA) was localized to chromosome 13, while the gene encoding the beta polypeptide (PCCB) was assigned to chromosome 3 [8].
  • We have proved the pathogenicity of R67S, R165Q and G112D mutation in PCCB gene, expressed for the first time in this work [9].
  • We present an initial characterization of 13 mutations located in exons 1, 3-7, and 12-14 of PCCB [2].
  • Cell fusion experiments have revealed two complementation groups, pccA and pccB, corresponding to defects of the PCCA (alpha-subunit) and PCCB (beta-subunit) genes, respectively [10].
  • A novel splicing mutation in propionic acidemia associated with a tetranucleotide direct repeat in the PCCB gene [11].

Anatomical context of PCCB

  • Functional analysis of PCCB mutations causing propionic acidemia based on expression studies in deficient human skin fibroblasts [9].
  • We have used a PCCB-deficient transformed fibroblast cell line to target the wild-type and mutant proteins to their physiological situation, analysing the effect of the mutations on PCC activity and protein stability [9].

Associations of PCCB with chemical compounds

  • Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes [8].
  • One of these is propionate, which is metabolized through carboxylation by propionyl-CoA carboxylase (PCC), an enzyme encoded by 2 genes, PCCA and PCCB [3].
  • Mutations in the PCCA or PCCB genes coding for alpha and beta subunits of propionyl CoA carboxylase can cause propionic acidemia [12].

Other interactions of PCCB

  • We demonstrate the reliability of this method for identification of the defective PCC gene in order to unequivocally approach the mutational analysis in the corresponding PCCA and PCCB genes [13].
  • SLC25A36, PCCB, and FNDC6 are of lesser interest because of moderate expression and changes in expression [14].

Analytical, diagnostic and therapeutic context of PCCB

  • Subjects were screened for defects affecting the PCCB gene by direct sequencing from genomic PCR products, restriction digests and mRNA analysis by RT-PCR [15].
  • The mRNA of PCCB gene in T428I and 1527del3 homozygotes were normal but in Western blot analysis, the betaPCC-subunit was only absent in 1527del3 homozygote patient suggesting different molecular pathology [16].


  1. Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Rodríguez-Pombo, P., Hoenicka, J., Muro, S., Pérez, B., Pérez-Cerdá, C., Richard, E., Desviat, L.R., Ugarte, M. Am. J. Hum. Genet. (1998) [Pubmed]
  2. Propionic acidemia: analysis of mutant propionyl-CoA carboxylase enzymes expressed in Escherichia coli. Chloupkova, M., Maclean, K.N., Alkhateeb, A., Kraus, J.P. Hum. Mutat. (2002) [Pubmed]
  3. Strong decrease in biotin content may correlate with metabolic alterations in colorectal adenocarcinoma. Cherbonnel-Lasserre, C.L., Linares-Cruz, G., Rigaut, J.P., Sabatier, L., Dutrillaux, B. Int. J. Cancer (1997) [Pubmed]
  4. High incidence of propionic acidemia in greenland is due to a prevalent mutation, 1540insCCC, in the gene for the beta-subunit of propionyl CoA carboxylase. Ravn, K., Chloupkova, M., Christensen, E., Brandt, N.J., Simonsen, H., Kraus, J.P., Nielsen, I.M., Skovby, F., Schwartz, M. Am. J. Hum. Genet. (2000) [Pubmed]
  5. Interallelic complementation of beta-subunit defects in fibroblasts of patients with propionyl-CoA carboxylase deficiency microinjected with mutant cDNA constructs. Loyer, M., Leclerc, D., Gravel, R.A. Hum. Mol. Genet. (1995) [Pubmed]
  6. Biotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood. Vlasova, T.I., Stratton, S.L., Wells, A.M., Mock, N.I., Mock, D.M. J. Nutr. (2005) [Pubmed]
  7. Qualitative and quantitative analysis of the effect of splicing mutations in propionic acidemia underlying non-severe phenotypes. Clavero, S., Pérez, B., Rincón, A., Ugarte, M., Desviat, L.R. Hum. Genet. (2004) [Pubmed]
  8. Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Lamhonwah, A.M., Barankiewicz, T.J., Willard, H.F., Mahuran, D.J., Quan, F., Gravel, R.A. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  9. Functional analysis of PCCB mutations causing propionic acidemia based on expression studies in deficient human skin fibroblasts. Pérez-Cerdá, C., Clavero, S., Pérez, B., Rodríguez-Pombo, P., Desviat, L.R., Ugarte, M. Biochim. Biophys. Acta (2003) [Pubmed]
  10. Mutations participating in interallelic complementation in propionic acidemia. Gravel, R.A., Akerman, B.R., Lamhonwah, A.M., Loyer, M., Léon-del-Rio, A., Italiano, I. Am. J. Hum. Genet. (1994) [Pubmed]
  11. A novel splicing mutation in propionic acidemia associated with a tetranucleotide direct repeat in the PCCB gene. Ohura, T., Narisawa, K., Tada, K., Iinuma, K. Hum. Genet. (1995) [Pubmed]
  12. Towards a model to explain the intragenic complementation in the heteromultimeric protein propionyl-CoA carboxylase. Rodríguez-Pombo, P., Pérez-Cerdá, C., Pérez, B., Desviat, L.R., Sánchez-Pulido, L., Ugarte, M. Biochim. Biophys. Acta (2005) [Pubmed]
  13. Transfection screening for defects in the PCCA and PCCB genes encoding propionyl-CoA carboxylase subunits. Rodriguez-Pombo, P., Pérez-Cerdá, C., Desviat, L.R., Pérez, B., Ugarte, M., Rodríguez-Pombo, P. Mol. Genet. Metab. (2002) [Pubmed]
  14. Differential Expression Profile Prioritization of Positional Candidate Glaucoma Genes: The GLC1C Locus. Rozsa, F.W., Scott, K.M., Pawar, H., Samples, J.R., Wirtz, M.K., Richards, J.E. Arch. Ophthalmol. (2007) [Pubmed]
  15. Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Muro, S., Rodríguez-Pombo, P., Pérez, B., Pérez-Cerdá, C., Desviat, L.R., Sperl, W., Skladal, D., Sass, J.O., Ugarte, M. Hum. Mutat. (1999) [Pubmed]
  16. Molecular analysis of PCCB gene in Korean patients with propionic acidemia. Kim, S.N., Ryu, K.H., Lee, E.H., Kim, J.S., Hahn, S.H. Mol. Genet. Metab. (2002) [Pubmed]
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