- CRAT (gene)
Carnitine acetyltransferase, also known as CRAT, is a human
gene .cite web | title = Entrez Gene: CRAT carnitine acetyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1384| accessdate = ]PBB_Summary
section_title =
summary_text = Carnitine acetyltransferase (CRAT) is a key enzyme in the metabolic pathway in mitochondria, peroxisomes and endoplasmic reticulum. CRAT catalyzes the reversible transfer of acyl groups from an acyl-CoA thioester to carnitine and regulates the ratio of acylCoA/CoA in the subcellular compartments. Different subcellular localizations of the CRAT mRNAs are thought to result from alternative splicing of the CRAT gene suggested by the divergent sequences in the 5' region of peroxisomal and mitochondrial CRAT cDNAs and the location of an intron where the sequences diverge. The alternatively splicing of this gene results in three distinct isoforms, one of which contains an N-terminial mitochondrial transit peptide, and has been shown to be located in mitochondria.cite web | title = Entrez Gene: CRAT carnitine acetyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1384| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=van der Leij FR, Huijkman NC, Boomsma C, "et al." |title=Genomics of the human carnitine acyltransferase genes. |journal=Mol. Genet. Metab. |volume=71 |issue= 1-2 |pages= 139–53 |year= 2000 |pmid= 11001805 |doi= 10.1006/mgme.2000.3055
*cite journal | author=Kalaria RN, Harik SI |title=Carnitine acetyltransferase activity in the human brain and its microvessels is decreased in Alzheimer's disease. |journal=Ann. Neurol. |volume=32 |issue= 4 |pages= 583–6 |year= 1992 |pmid= 1456745 |doi= 10.1002/ana.410320417
*cite journal | author=Corti O, Finocchiaro G, Rossi E, "et al." |title=Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. |journal=Genomics |volume=23 |issue= 1 |pages= 94–9 |year= 1995 |pmid= 7829107 |doi= 10.1006/geno.1994.1463
*cite journal | author=Corti O, DiDonato S, Finocchiaro G |title=Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. |journal=Biochem. J. |volume=303 ( Pt 1) |issue= |pages= 37–41 |year= 1994 |pmid= 7945262 |doi=
*cite journal | author=Lian W, Govindasamy L, Gu Y, "et al." |title=Crystallization and preliminary X-ray crystallographic studies on recombinant human carnitine acetyltransferase. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=58 |issue= Pt 7 |pages= 1193–4 |year= 2003 |pmid= 12077440 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Jogl G, Tong L |title=Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. |journal=Cell |volume=112 |issue= 1 |pages= 113–22 |year= 2003 |pmid= 12526798 |doi=
*cite journal | author=Wu D, Govindasamy L, Lian W, "et al." |title=Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13159–65 |year= 2003 |pmid= 12562770 |doi= 10.1074/jbc.M212356200
*cite journal | author=Govindasamy L, Kukar T, Lian W, "et al." |title=Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase. |journal=J. Struct. Biol. |volume=146 |issue= 3 |pages= 416–24 |year= 2005 |pmid= 15099582 |doi= 10.1016/j.jsb.2004.01.011
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504PBB_Controls
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