# TOXICOLOGIC IMPLICATIONS OF MULTIPLE EPOXIDE HYDROLASES

> **NIH NIH R01** · UNIVERSITY OF ILLINOIS AT CHICAGO · 1987 · $69,697

## Abstract

Epoxide hydrolases are cellular enzymes that catalyze the conversion of
epoxides to dihydrodiols.  Because epoxides are highly reactive
electrophiles, they are common ultimate toxins, mutagens, and carcinogens.
The capability of epoxide hydrolases to convert these reactive
intermediates to less reactive products places them among the most
important endogenous means of protection against chemical toxins and
carcinogens.  The purpose of these studies is to examine several epoxide
hydrolases, to compare and contrast their structural and catalytic
properties, and to investigate their participation in the metabolism of
toxic compounds.  Understanding the nature of these multiple epoxide
hydrolases and their participation in the deactivation of epoxide
intermediates is essential to our ultimate understanding of mechanisms of
chemical toxicity and carcinogenesis.

The emphasis of these studies is on the examination of different epoxide
hydrolases derived from different organs, species, and individuals.  Of
specific interest is the possible polymorphism of epoxide hydrolases in
man.  The existence of multiple enzyme forms in man may represent a
significant genetically regulated determinant of different individual
responses to chemical toxins and carcinogens.

## Key facts

- **NIH application ID:** 3172147
- **Project number:** 5R01CA034455-05
- **Recipient organization:** UNIVERSITY OF ILLINOIS AT CHICAGO
- **SAM.gov UEI:** W8XEAJDKMXH3
- **Principal Investigator:** THOMAS M GUENTHNER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $69,697
- **Award type:** 5
- **Project period:** 1983-05-01 → 1990-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3172147

## Citation

> US National Institutes of Health, RePORTER application 3172147, TOXICOLOGIC IMPLICATIONS OF MULTIPLE EPOXIDE HYDROLASES (5R01CA034455-05). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3172147. Licensed CC0.

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