Skip to content
2000
Volume 13, Issue 9
  • ISSN: 0929-8673
  • E-ISSN: 1875-533X

Abstract

Carboxylesterases (CE) are ubiquitous enzymes responsible for the detoxification of xenobiotics. Many therapeutically useful drugs are metabolized by these proteins which impacts upon the efficiency of drug treatment. In some instances, CEs convert inactive prodrugs to active metabolites, a process that is essential for biological activity. Such compounds include the anticancer agents CPT-11 (3) and capecitabine (4), the antibiotics Ceftin (9) and Vantin, as well as the illicit street drug heroin (6). However, more commonly, CEs hydrolyze many esterified drugs to inactive products that are then excreted. Agents such as flestolol (11), meperidine (5), lidocaine (8) and cocaine (7), are all hydrolyzed and inactivated by these enzymes. Therefore the efficacy of esterified drugs will be dependent upon the distribution and catalytic activity of different CEs. In this review, we examine the structural aspects of CEs and their roles in drug detoxification and propose that modulation of CE activity may allow for improvements in, and potentiation of, drug efficacy.

Loading

Article metrics loading...

/content/journals/cmc/10.2174/092986706776360969
2006-04-01
2025-05-04
Loading full text...

Full text loading...

/content/journals/cmc/10.2174/092986706776360969
Loading

  • Article Type:
    Research Article
Keyword(s): Carboxylesterase; drug metabolism; enzyme structure; inhibitor
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test