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Publication : cDNA cloning, characterization and stable expression of novel human brain carboxylesterase.

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.
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