Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Carnosinuria, Carnosinemia
Rattus norvegicus
Category:
Metabolite Pathway
Sub-Category:
Disease
Created: 2018-09-10
Last Updated: 2019-09-15
Carnosinemia, also known as carnosinemia, is a rare inborn error of metabolism (IEM) and recessive autosomal disorder caused by a defective CNDP1 gene which encodes for carnosinase. Carnosinase is a dipeptidase enzyme that catalyzes the breakdown of Carnosine into alanine and histidine. This disorder is characterized by secretion of large amounts of carnosine and anserine in the urine but low levels of methylhistidine. Patients also have unusually high concentrations of homocarnosine in the cerebrospinal fluid. Other symptoms include progressive neurologic disorders characterized by severe mental defect and myoclonic seizures. There is no known cure for Carnosinemia therefore treatment involves management of symptoms. There have been about 30 cases of Carnosinemia reported worldwide.
References
Carnosinuria, Carnosinemia References
Perry TL, Hansen S, Tischler B, Bunting R, Berry K: Carnosinemia. A new metabolic disorder associated with neurologic disease and mental defect. N Engl J Med. 1967 Dec 7;277(23):1219-27. doi: 10.1056/NEJM196712072772302.
Pubmed: 6058610
beta-Alanine Metabolism References
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. doi: 10.1101/gr.2596504.
Pubmed: 15489334
Teufel M, Saudek V, Ledig JP, Bernhardt A, Boularand S, Carreau A, Cairns NJ, Carter C, Cowley DJ, Duverger D, Ganzhorn AJ, Guenet C, Heintzelmann B, Laucher V, Sauvage C, Smirnova T: Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. J Biol Chem. 2003 Feb 21;278(8):6521-31. doi: 10.1074/jbc.M209764200. Epub 2002 Dec 6.
Pubmed: 12473676
Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA: Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci U S A. 2006 May 2;103(18):7159-64. doi: 10.1073/pnas.0600895103. Epub 2006 Apr 25.
Pubmed: 16641100
Wyborski RJ, Bond RW, Gottlieb DI: Characterization of a cDNA coding for rat glutamic acid decarboxylase. Brain Res Mol Brain Res. 1990 Aug;8(3):193-8. doi: 10.1016/0169-328x(90)90016-7.
Pubmed: 2170798
Julien JF, Samama P, Mallet J: Rat brain glutamic acid decarboxylase sequence deduced from a cloned cDNA. J Neurochem. 1990 Feb;54(2):703-5. doi: 10.1111/j.1471-4159.1990.tb01928.x.
Pubmed: 2299361
Michelsen BK, Petersen JS, Boel E, Moldrup A, Dyrberg T, Madsen OD: Cloning, characterization, and autoimmune recognition of rat islet glutamic acid decarboxylase in insulin-dependent diabetes mellitus. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8754-8. doi: 10.1073/pnas.88.19.8754.
Pubmed: 1924335
Kvalnes-Krick KL, Traut TW: Cloning, sequencing, and expression of a cDNA encoding beta-alanine synthase from rat liver. J Biol Chem. 1993 Mar 15;268(8):5686-93.
Pubmed: 8449931
Matthews MM, Liao W, Kvalnes-Krick KL, Traut TW: beta-Alanine synthase: purification and allosteric properties. Arch Biochem Biophys. 1992 Mar;293(2):254-63. doi: 10.1016/0003-9861(92)90393-b.
Pubmed: 1536562
Matsuda K, Sakata S, Kaneko M, Hamajima N, Nonaka M, Sasaki M, Tamaki N: Molecular cloning and sequencing of a cDNA encoding dihydropyrimidinase from the rat liver. Biochim Biophys Acta. 1996 Jun 7;1307(2):140-4. doi: 10.1016/0167-4781(96)00056-5.
Pubmed: 8679696
Kimura M, Sakata SF, Matoba Y, Matsuda K, Kontani Y, Kaneko M, Tamaki N: Cloning of rat dihydropyrimidine dehydrogenase and correlation of its mRNA increase in the rat liver with age. J Nutr Sci Vitaminol (Tokyo). 1998 Aug;44(4):537-46.
Pubmed: 9819714
Medina-Kauwe LK, Tillakaratne NJ, Wu JY, Tobin AJ: A rat brain cDNA encodes enzymatically active GABA transaminase and provides a molecular probe for GABA-catabolizing cells. J Neurochem. 1994 Apr;62(4):1267-75. doi: 10.1046/j.1471-4159.1994.62041267.x.
Pubmed: 8133261
Kontani Y, Sakata SF, Matsuda K, Ohyama T, Sano K, Tamaki N: The mature size of rat 4-aminobutyrate aminotransferase is different in liver and brain. Eur J Biochem. 1999 Aug;264(1):218-22. doi: 10.1046/j.1432-1327.1999.00612.x.
Pubmed: 10447691
Tamaki N, Sakata SF, Matsuda K: Purification, properties, and sequencing of aminoisobutyrate aminotransferases from rat liver. Methods Enzymol. 2000;324:376-89. doi: 10.1016/s0076-6879(00)24247-x.
Pubmed: 10989446
Kedishvili NY, Popov KM, Rougraff PM, Zhao Y, Crabb DW, Harris RA: CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution. J Biol Chem. 1992 Sep 25;267(27):19724-9.
Pubmed: 1527093
Goodwin GW, Rougraff PM, Davis EJ, Harris RA: Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase. J Biol Chem. 1989 Sep 5;264(25):14965-71.
Pubmed: 2768248
Kedishvili NY, Popov KM, Harris RA: The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase. Arch Biochem Biophys. 1991 Oct;290(1):21-6. doi: 10.1016/0003-9861(91)90586-8.
Pubmed: 1898092
Farres J, Guan KL, Weiner H: Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences. Eur J Biochem. 1989 Mar 1;180(1):67-74. doi: 10.1111/j.1432-1033.1989.tb14616.x.
Pubmed: 2540003
Farres J, Guan KL, Weiner H: Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase. Biochem Biophys Res Commun. 1988 Feb 15;150(3):1083-7. doi: 10.1016/0006-291x(88)90740-1.
Pubmed: 3342060
Ochiai Y, Itoh K, Sakurai E, Tanaka Y: Molecular cloning and characterization of rat semicarbazide-sensitive amine oxidase. Biol Pharm Bull. 2005 Mar;28(3):413-8. doi: 10.1248/bpb.28.413.
Pubmed: 15744061
Morris NJ, Ducret A, Aebersold R, Ross SA, Keller SR, Lienhard GE: Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane. J Biol Chem. 1997 Apr 4;272(14):9388-92. doi: 10.1074/jbc.272.14.9388.
Pubmed: 9083076
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000493
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Downloads
Settings