PMID- 2634095
OWN - NLM
STAT- MEDLINE
DCOM- 19900530
LR  - 20191029
IS  - 0887-2082 (Print)
IS  - 0887-2082 (Linking)
VI  - 4
IP  - 4
DP  - 1989 Winter
TI  - Selective inhibition of cytosolic epoxide hydrolase activity in vitro by 
      compounds that inhibit catalase.
PG  - 241-9
AB  - The ability of a number of known inhibitors of catalase activity to affect 
      cytosolic and microsomal epoxide hydrolase activities in vitro, measured as 
      enzymatic trans-stilbene oxide hydrolysis and styrene oxide hydrolysis, 
      respectively, was investigated. Catalase and cytosolic epoxide hydrolase 
      activities are inhibited by hydroxylated metabolites of 
      2-amino-4,5-diphenylthiazole (DPT). The metabolite hydroxylated on the 4-phenyl 
      ring (4OH-DPT) and the metabolite hydroxylated on both phenyl rings 
      (4,5-DIOH-DPT) are potent inhibitors of both enzymes; the metabolite hydroxylated 
      on the 5-phenyl ring (5OH-DPT) is less potent. Unmetabolized DPT has no effect on 
      either enzyme. 4OH-DPT inhibits, but 5OH-DPT enhances, microsomal epoxide 
      hydrolase activity. 4,5-DIOH-DPT and DPT have no effect on this enzyme. Other 
      compounds that inhibit both catalase and cytosolic epoxide hydrolase activities, 
      but do not inhibit microsomal epoxide hydrolase activity, are 
      nordihydroguaiaretic acid and 2-aminothiazole. Microsomal epoxide hydrolase 
      activity is enhanced by 2-aminothiazole and levamisole in vitro. Thus these 
      inhibitors of catalase are selective epoxide hydrolase inhibitors in that they 
      inhibit cytosolic epoxide hydrolase activity in vitro, but have either no effect 
      on, or increase the activity of, microsomal epoxide hydrolase in vitro. 
      Conversely, the selective cytosolic epoxide hydrolase inhibitors 4-phenylchalcone 
      oxide and 4'-phenylchalcone oxide do not inhibit catalase activity, nor does 
      trichloropropene oxide, a selective microsomal epoxide hydrolase inhibitor.
FAU - Guenthner, T M
AU  - Guenthner TM
AD  - Department of Pharmacology, University of Illinois College of Medicine, Chicago 
      60612.
FAU - Hjelle, J T
AU  - Hjelle JT
FAU - Whalen, R
AU  - Whalen R
LA  - eng
GR  - AM 33003/AM/NIADDK NIH HHS/United States
GR  - CA 34455/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biochem Toxicol
JT  - Journal of biochemical toxicology
JID - 8700114
RN  - 0 (Thiazoles)
RN  - 6318-74-7 (Bax 439)
RN  - EC 1.11.1.6 (Catalase)
RN  - EC 3.3.2.- (Epoxide Hydrolases)
RN  - EC 3.3.2.- (stilbene oxide hydrolase)
RN  - EC 3.3.2.- (styrene oxide hydratase)
SB  - IM
MH  - Animals
MH  - Catalase/*antagonists & inhibitors
MH  - Cytosol/*enzymology
MH  - Epoxide Hydrolases/*antagonists & inhibitors
MH  - Liver/*enzymology
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Structure
MH  - Thiazoles/*pharmacology
EDAT- 1989/01/01 00:00
MHDA- 1989/01/01 00:01
CRDT- 1989/01/01 00:00
PHST- 1989/01/01 00:00 [pubmed]
PHST- 1989/01/01 00:01 [medline]
PHST- 1989/01/01 00:00 [entrez]
AID - 10.1002/jbt.2570040407 [doi]
PST - ppublish
SO  - J Biochem Toxicol. 1989 Winter;4(4):241-9. doi: 10.1002/jbt.2570040407.