First Author | Mori M | Year | 1999 |
Journal | FEBS Lett | Volume | 458 |
Issue | 1 | Pages | 17-22 |
PubMed ID | 10518925 | Mgi Jnum | J:113779 |
Mgi Id | MGI:3687660 | Doi | 10.1016/s0014-5793(99)01111-4 |
Citation | Mori M, et al. (1999) cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. FEBS Lett 458(1):17-22 |
abstractText | 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. |