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Pathway Description
Propionic Acidemia
Homo sapiens
Disease Pathway
Created: 2013-08-01
Last Updated: 2022-11-17
Propionic acidemia (Ketotic hyperglycinemia) is caused by mutation in the genes encoding propionyl-CoA carboxylase, PCCA or PCCB. The break down of Propionyl-CoA is catalyzed by Propionyl-CoA carboxylase (PCC). Propionyl-CoA plays an important role in amino acid metabolism. A mutation in this enzyme causes accumulation of ammonia and propionylcarnitine (C3) in the blood; carnitine , glutamine, glycine, and propionic acid in the plasma; 3-hydroxypropionic acid, 3-hydroxyvaleric acid, 5-oxoproline, acylcarnitin, glycine, methylcitric acid, propionylglycine and tiglylcine in the urine. Symptoms include cardio myopathy, growth retardation, hypothermia, ketosis, neutropenia, strokelike episodes, pyloric stenosis and spastic diplegia/quadriplegia.
References
Propionic Acidemia References
[OMIM: Entry 606054](http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606054)
[Uniprot: P05166](http://www.uniprot.org/uniprot/P05166)
Engelke, U., van der Graaf, M., Heerschap, A., Hoenderop, S., Moolenaar, S., Morava, E., Wevers, R. Handbook of 1H-NMR spectroscopy in inborn errors of metabolism: body fluid NMR spectroscopy and in vivo MR spectroscopy (2nd ed) (2007) p.84 Heilbronn: SPS Verlagsgesellschaft
Ando T, Rasmussen K, Nyhan WL, Donnell GN, Barnes ND: Propionic acidemia in patients with ketotic hyperglycinemia. J Pediatr. 1971 May;78(5):827-32.
Pubmed: 5581587
Desviat LR, Clavero S, Perez-Cerda C, Navarrete R, Ugarte M, Perez B: New splicing mutations in propionic acidemia. J Hum Genet. 2006;51(11):992-7. doi: 10.1007/s10038-006-0068-3. Epub 2006 Oct 19.
Pubmed: 17051315
Ohura T, Miyabayashi S, Narisawa K, Tada K: Genetic heterogeneity of propionic acidemia: analysis of 15 Japanese patients. Hum Genet. 1991 May;87(1):41-4.
Pubmed: 2037281
Wolf B, Willard HF, Rosenberg LE: Kinetic analysis of genetic complementation in heterokaryons of propionyl CoA carboxylase-deficient human fibroblasts. Am J Hum Genet. 1980 Jan;32(1):16-25.
Pubmed: 7361761
Shchelochkov OA, Carrillo N, Venditti C: Propionic Acidemia
Pubmed: 22593918
Valine, Leucine, and Isoleucine Degradation References
Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.
Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.
Wanders RJ, Duran M, Loupatty FJ: Enzymology of the branched-chain amino acid oxidation disorders: the valine pathway. J Inherit Metab Dis. 2012 Jan;35(1):5-12. doi: 10.1007/s10545-010-9236-x. Epub 2010 Nov 23.
Pubmed: 21104317
Wang YP, Qi ML, Li TT, Zhao YJ: Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic form of maple syrup urine disease (MSUD). Gene. 2012 Apr 25;498(1):112-5. doi: 10.1016/j.gene.2012.01.082. Epub 2012 Feb 3.
Pubmed: 22326532
Nobukuni Y, Mitsubuchi H, Endo F, Akaboshi I, Asaka J, Matsuda I: Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease. J Clin Invest. 1990 Jul;86(1):242-7. doi: 10.1172/JCI114690.
Pubmed: 2365818
Chuang JL, Cox RP, Chuang DT: Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences. Am J Hum Genet. 1996 Jun;58(6):1373-7.
Pubmed: 8651316
Park HD, Lee DH, Hong YH, Kang DH, Lee YK, Song J, Lee SY, Kim JW, Ki CS, Lee YW: Three Korean patients with maple syrup urine disease: four novel mutations in the BCKDHA gene. Ann Clin Lab Sci. 2011 Spring;41(2):167-73.
Pubmed: 21844576
McKean MC, Winkeler KA, Danner DJ: Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex. Biochim Biophys Acta. 1992 Nov 15;1171(1):109-12. doi: 10.1016/0167-4781(92)90149-t.
Pubmed: 1420356
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. doi: 10.1038/ng1285. Epub 2003 Dec 21.
Pubmed: 14702039
Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. doi: 10.1006/geno.1993.1335.
Pubmed: 8406489
Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8.
Pubmed: 3693355
Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. doi: 10.1073/pnas.85.5.1422.
Pubmed: 3278312
Wang SP, Robert MF, Gibson KM, Wanders RJ, Mitchell GA: 3-Hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene (HMGCL) cloning and detection of large gene deletions in two unrelated HL-deficient patients. Genomics. 1996 Apr 1;33(1):99-104. doi: 10.1006/geno.1996.0164.
Pubmed: 8617516
Mitchell GA, Robert MF, Hruz PW, Wang S, Fontaine G, Behnke CE, Mende-Mueller LM, Schappert K, Lee C, Gibson KM, Miziorko HM, et al.: 3-Hydroxy-3-methylglutaryl coenzyme A lyase (HL). Cloning of human and chicken liver HL cDNAs and characterization of a mutation causing human HL deficiency. J Biol Chem. 1993 Feb 25;268(6):4376-81.
Pubmed: 8440722
Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. doi: 10.1073/pnas.93.14.7143.
Pubmed: 8692959
Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. doi: 10.1186/1471-2164-8-399.
Pubmed: 17974005
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