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

FEBS Lett. 1999 Sep 10;458(1):17-22. doi: 10.1016/s0014-5793(99)01111-4.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Brain / enzymology*
  • Carboxylesterase
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / genetics*
  • Carboxylic Ester Hydrolases / metabolism*
  • Catalysis
  • Cell Line
  • Cloning, Molecular
  • Cricetinae
  • DNA, Complementary / metabolism*
  • Gene Expression Regulation, Enzymologic*
  • Gene Library
  • Humans
  • Isoenzymes / chemistry
  • Kinetics
  • Liver / metabolism
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Transfection

Substances

  • DNA, Complementary
  • Isoenzymes
  • Carboxylic Ester Hydrolases
  • Carboxylesterase

Associated data

  • GENBANK/AB025026
  • GENBANK/AB025028