CROT (gene)

From Wikipedia, the free encyclopedia

Carnitine O-octanoyltransferase

Identifiers

External IDs

OMIM: 606090 MGI: 1921364 HomoloGene: 10899

Gene ontology
Molecular Function:	• acyltransferase activity • carnitine O-octanoyltransferase activity • transferase activity
Cellular Component:	• peroxisome
Biological Process:	• generation of precursor metabolites and energy • lipid metabolic process • fatty acid metabolic process • transport • fatty acid transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_021151 (mRNA)
NP_066974 (protein)

NM_023733 (mRNA)
NP_076222 (protein)

Location

Chr 7: 86.81 - 86.87 Mb

Chr 5: 8.97 - 9 Mb

Pubmed search

[1]

[2]

Carnitine O-octanoyltransferase, also known as CROT, is a human gene.^[1]

Carnitine octanoyltransferase (EC 2.3.1.137) is a carnitine acyltransferase that catalyzes the reversible transfer of fatty acyl groups between CoA and carnitine. This provides a crucial step in the transport of medium- and long-chain acyl-CoA out of the mammalian peroxisome to the cytosol and mitochondria. See also CRAT (MIM 600184). Van der Leij et al. (2000) reviewed the function, structural features, and phylogenetics of human carnitine acyltransferase genes, including CROT.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: CROT carnitine O-octanoyltransferase.

[edit] Further reading

van der Leij FR, Huijkman NC, Boomsma C, et al. (2000). "Genomics of the human carnitine acyltransferase genes.". Mol. Genet. Metab. 71 (1-2): 139-53. doi:10.1006/mgme.2000.3055. PMID 11001805.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767-72. doi:10.1126/science.1083423. PMID 12690205.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Morillas M, Gómez-Puertas P, Rubí B, et al. (2002). "Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain.". J. Biol. Chem. 277 (13): 11473-80. doi:10.1074/jbc.M111628200. PMID 11790793.
Ferdinandusse S, Mulders J, IJlst L, et al. (1999). "Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids.". Biochem. Biophys. Res. Commun. 263 (1): 213-8. doi:10.1006/bbrc.1999.1340. PMID 10486279.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107-13. doi:10.1006/abio.1996.0138. PMID 8619474.