A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases

被引:68
作者
Hunt, MC [1 ]
Yamada, J
Maltais, LJ
Wright, MW
Podesta, EJ
Alexson, SEH
机构
[1] Karolinska Univ, Huddinge Hosp, Dept Lab Med, Div Clin Chem C174,Karolinska Inst, Stockholm, Sweden
[2] Tokyo Univ Pharm & Life Sci, Dept Clin Biochem, Tokyo, Japan
[3] Jackson Lab, Mouse Genome Informat, Mouse Genom Nomenclature Committee, Bar Harbor, ME 04609 USA
[4] UCL, London, England
[5] Univ Buenos Aires, Sch Med, Dept Biochem, Buenos Aires, DF, Argentina
关键词
fatty acid metabolism; coenzyme A; peroxisomes;
D O I
10.1194/jlr.E500003-JLR200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branchedchain), bile acid-CoAs, CoA esters of prostaglandins, etc., to the corresponding free acid and CoA. However, there is significant confusion regarding the nomenclature of these genes. In agreement with the HUGO Gene Nomenclature Committee and the Mouse Genomic Nomenclature Committee, 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-ACOT12, and rat and mouse genes named Acot1-Acot12. Several of the ACOT genes are the result of splicing events, and these splice variants are cataloged.
引用
收藏
页码:2029 / 2032
页数:4
相关论文
共 25 条
[1]  
Adams SH, 2001, BIOCHEM J, V360, P135, DOI 10.1042/bj3600135
[2]   An adrenocorticotropin-regulated phosphoprotein intermediary in steroid synthesis is similar to an acyl-CoA thioesterase enzyme [J].
Finkielstein, C ;
Maloberti, P ;
Mendez, CF ;
Paz, C ;
Maciel, FC ;
Cymeryng, C ;
Neuman, I ;
Dada, L ;
Mele, PG ;
Solano, A ;
Podestá, EJ .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 256 (01) :60-66
[3]   A CONSERVED TRIPEPTIDE SORTS PROTEINS TO PEROXISOMES [J].
GOULD, SJ ;
KELLER, GA ;
HOSKEN, N ;
WILKINSON, J ;
SUBRAMANI, S .
JOURNAL OF CELL BIOLOGY, 1989, 108 (05) :1657-1664
[4]   The peroxisome proliferator-induced cytosolic type I Acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid α/β hydrolase [J].
Huhtinen, K ;
O'Byrne, J ;
Lindquist, PJG ;
Contreras, JA ;
Alexson, SEH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (05) :3424-3432
[5]   The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism [J].
Hunt, MC ;
Alexson, SEH .
PROGRESS IN LIPID RESEARCH, 2002, 41 (02) :99-130
[6]   Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism [J].
Hunt, MC ;
Solaas, K ;
Kase, BF ;
Alexson, SEH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (02) :1128-1138
[7]   Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism [J].
Hunt, MC ;
Nousiainen, SEB ;
Huttunen, MK ;
Orii, KE ;
Svensson, LT ;
Alexson, SEH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (48) :34317-34326
[8]   Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase [J].
Jones, JM ;
Gould, SJ .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 275 (01) :233-240
[9]   Identification of peroxisomal acyl-CoA thioesterases in yeast and humans [J].
Jones, JM ;
Nau, K ;
Geraghty, MT ;
Erdmann, R ;
Gould, SJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (14) :9216-9223
[10]   Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic acyl-CoA thioesterase from mouse and rat liver -: Recombinant expression in Escherichia coli, tissue expression, and nutritional regulation [J].
Lindquist, PJG ;
Svensson, LT ;
Alexson, SEH .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 251 (03) :631-640