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A novel geminal diol as a highly specific and stable in vivo inhibitor of insect juvenile hormone esterase
Author(s) -
Roe R. Michael,
Anspaugh Douglas D.,
Venkatesh Krishnappa,
Linderman Russell J.,
Graves David M.
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1997)36:3<165::aid-arch2>3.0.co;2-t
Subject(s) - juvenile hormone , esterase , sulfone , in vivo , biology , biochemistry , enzyme inhibitor , enzyme , stereochemistry , chemistry , hormone , organic chemistry , microbiology and biotechnology
Thio‐containing and acetylenic trifluoromethyl ketones were potent inhibitors of insect juvenile hormone (JH) esterase with greater inhibitory activity than aliphatic and α,β‐unsaturated homologs. Octylthio‐1,1,1‐trifluoropropan‐2‐one was the most potent inhibitor with the greatest equilibrium hydration constant in pure water. However, a keto/hydrate equilibrium was not necessary for JH esterase inhibition. The carbonyl tautomer of 1‐octyl [1‐(3,3,3‐trifluoropropan‐2,2‐ dihydroxy)] sulfone (OTPdOH‐sulfone) was not detectable, and yet OTPdOH‐sulfone was a potent in vitro inhibitor of JH esterase with an I 50 of 1.2 nM. The mechanism of JH esterase inhibition by these compounds is discussed. OTPdOH‐sulfone inhibited JH esterase with minimal activity toward insect 1‐naphthyl acetate esterase and electric eel acetylcholinesterase. The inhibitor was also active in vivo, selective for JH esterase, and persistent for over 32 h. OTPdOH‐sulfone when topically applied to larval and adult cabbage loopers, Trichoplusia ni , elicited juvenoid activity apparently because of the specific in vivo inhibition of JH metabolism. Arch. Insect Biochem. Physiol. 36:165–179, 1997. © 1997 Wiley‐Liss, Inc.