|
|
||||||||
Papers In Press, published online ahead of print July 1, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Department of Laboratory Medicine, Karolinska Institutet, Stockholm SE 141 86
Corresponding Author: mary.hunt{at}labmed.ki.se
Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branched chain), bile acid-CoAs, CoA esters of prostaglandins etc, to the corresponding free acid and coenzyme A. There is however significant confusion regarding the nomenclature of these genes. In agreement with the HUGO Gene Nomenclature Committee (HGNC) and the Mouse Genomic Nomenclature Committee (MGNC), a revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases has been suggested for the 12 member family. The family root symbol is ACOT, with human genes named ACOT1-12, and rat and mouse named Acot1-12. Several of the ACOT genes are the result of splicing events and these splice variants are catalogued.
Revised on June 20, 2005
Accepted on July 1, 2005
A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
S. Wiese, T. Gronemeyer, R. Ofman, M. Kunze, C. P. Grou, J. A. Almeida, M. Eisenacher, C. Stephan, H. Hayen, L. Schollenberger, et al. Proteomics Characterization of Mouse Kidney Peroxisomes by Tandem Mass Spectrometry and Protein Correlation Profiling Mol. Cell. Proteomics, December 1, 2007; 6(12): 2045 - 2057. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Kanno, M. K. Wu, D. S. Agate, B. J. Fanelli, N. Wagle, E. F. Scapa, C. Ukomadu, and D. E. Cohen Interacting Proteins Dictate Function of the Minimal START Domain Phosphatidylcholine Transfer Protein/StarD2 J. Biol. Chem., October 19, 2007; 282(42): 30728 - 30736. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. Dongol, Y. Shah, I. Kim, F. J. Gonzalez, and M. C. Hunt The acyl-CoA thioesterase I is regulated by PPAR{alpha} and HNF4{alpha} via a distal response element in the promoter J. Lipid Res., August 1, 2007; 48(8): 1781 - 1791. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. K. Forwood, A. S. Thakur, G. Guncar, M. Marfori, D. Mouradov, W. Meng, J. Robinson, T. Huber, S. Kellie, J. L. Martin, et al. Structural basis for recruitment of tandem hotdog domains in acyl-CoA thioesterase 7 and its role in inflammation PNAS, June 19, 2007; 104(25): 10382 - 10387. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. T. Eppig, J. A. Blake, C. J. Bult, J. A. Kadin, J. E. Richardson, and the Mouse Genome Database Group The mouse genome database (MGD): new features facilitating a model system Nucleic Acids Res., January 12, 2007; 35(suppl_1): D630 - D637. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. C. Hunt, A. Rautanen, M. A. K. Westin, L. T. Svensson, and S. E. H. Alexson Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs FASEB J, September 1, 2006; 20(11): 1855 - 1864. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. A. Blake, J. T. Eppig, C. J. Bult, J. A. Kadin, J. E. Richardson, and Mouse Genome Database Group The Mouse Genome Database (MGD): updates and enhancements Nucleic Acids Res., January 1, 2006; 34(suppl_1): D562 - D567. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. A. K. Westin, M. C. Hunt, and S. E. H. Alexson The Identification of a Succinyl-CoA Thioesterase Suggests a Novel Pathway for Succinate Production in Peroxisomes J. Biol. Chem., November 18, 2005; 280(46): 38125 - 38132. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| All ASBMB Journals | Journal of Biological Chemistry |
| Molecular and Cellular Proteomics | ASBMB Today |