Title : cDNA cloning, characterization and stable expression of novel human brain carboxylesterase - Mori_1999_FEBS.Lett_458_17 |
Author(s) : Mori M , Hosokawa M , Ogasawara Y , Tsukada E , Chiba K |
Ref : FEBS Letters , 458 :17 , 1999 |
Abstract :
The DNA sequence encoding a novel human brain carboxylesterase (CES) has been determined. The protein is predicted to have 567 amino acids, including conserved motifs, such as GESAGG, GXXXXEFG, and GDHGD which comprise a catalytic triad, and the endoplasmic reticulum retention motif (HXEL-COOH) observed in CES families. Their gene products exhibited hydrolase activity towards temocapril, p-nitrophenyl-acetate and long-chain acyl-CoA. Since the molecular masses of these gene products are similar to those that exist in capillary endothelial cells of the human brain [Yamamda et al. (1994) Brain Res. 658, 163-167], these CES isozymes may function as a blood-brain barrier to protect the central nervous system from ester or amide compounds. |
PubMedSearch : Mori_1999_FEBS.Lett_458_17 |
PubMedID: 10518925 |
Gene_locus related to this paper: human-CES1 , mouse-Ces1d |
Gene_locus | human-CES1 mouse-Ces1d |
Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K (1999)
cDNA cloning, characterization and stable expression of novel human brain carboxylesterase
FEBS Letters
458 :17
Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K (1999)
FEBS Letters
458 :17