Juvenile hormone (JH) esterase: Why are you so JH specific?

Shizuo G. Kamita, Andrew C. Hintona, Craig E. Wheelock, Mark D. Wogulis, David K. Wilson, Nicola M. Wolf, Jeanette E. Stok, Bertold Hock, Bruce D. Hammock

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

Juvenile hormone esterases (JHEs) from six insects belonging to three orders (Lepidoptera, Coleoptera, and Diptera) were compared in terms of their deduced amino acid sequence and biochemical properties. The four lepidopteran JHEs showed from 52% to 59% identity to each other and about 30% identity to the coleopteran and dipteran JHEs. The JHE of Manduca sexta was remarkably resistant to the addition of organic co-solvents and detergent; in some cases, it demonstrated significant activation of activity. Triflouromethylketone (TFK) inhibitors with chain lengths of 8, 10 or 12 carbons were highly effective against both lepidopteran and coleopteran JHEs. The coleopteran JHE remained sensitive to TFK inhibitors with a chain length of 6 carbons, whereas the lepidopteran JHEs were significantly less sensitive. When the chain was altered to a phenethyl moiety, the coleopteran JHE remained moderately sensitive, while the lepidopteran JHEs were much less sensitive. The lepidopteran and coleopteran JHEs did not show dramatic differences in specificity to α-naphthyl and p-nitrophenyl substrates. However, as the chain length of the α-naphthyl substrates increased from propionate to caprylate, there was a trend towards reduced activity. The JHE of M. sexta was crystallized and the properties of the crystal suggest a high-resolution structure will follow.

Original languageEnglish (US)
Pages (from-to)1261-1273
Number of pages13
JournalInsect Biochemistry and Molecular Biology
Volume33
Issue number12
DOIs
StatePublished - Dec 2003

Fingerprint

juvenile hormone esterase
Juvenile Hormones
juvenile hormones
Lepidoptera
Chain length
Manduca
Manduca sexta
Carbon
Caprylates
carbon
Beetles
Propionates
Substrates
propionates
Diptera
detergents
Detergents
Insects
crystals
Amino Acid Sequence

Keywords

  • Baculovirus
  • Comparative sequence analysis
  • JH
  • JH metabolism
  • Juvenile hormone esterase
  • Trifluoromethylketone inhibitor

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry

Cite this

Kamita, S. G., Hintona, A. C., Wheelock, C. E., Wogulis, M. D., Wilson, D. K., Wolf, N. M., ... Hammock, B. D. (2003). Juvenile hormone (JH) esterase: Why are you so JH specific? Insect Biochemistry and Molecular Biology, 33(12), 1261-1273. https://doi.org/10.1016/j.ibmb.2003.08.004

Juvenile hormone (JH) esterase : Why are you so JH specific? / Kamita, Shizuo G.; Hintona, Andrew C.; Wheelock, Craig E.; Wogulis, Mark D.; Wilson, David K.; Wolf, Nicola M.; Stok, Jeanette E.; Hock, Bertold; Hammock, Bruce D.

In: Insect Biochemistry and Molecular Biology, Vol. 33, No. 12, 12.2003, p. 1261-1273.

Research output: Contribution to journalArticle

Kamita, SG, Hintona, AC, Wheelock, CE, Wogulis, MD, Wilson, DK, Wolf, NM, Stok, JE, Hock, B & Hammock, BD 2003, 'Juvenile hormone (JH) esterase: Why are you so JH specific?', Insect Biochemistry and Molecular Biology, vol. 33, no. 12, pp. 1261-1273. https://doi.org/10.1016/j.ibmb.2003.08.004
Kamita SG, Hintona AC, Wheelock CE, Wogulis MD, Wilson DK, Wolf NM et al. Juvenile hormone (JH) esterase: Why are you so JH specific? Insect Biochemistry and Molecular Biology. 2003 Dec;33(12):1261-1273. https://doi.org/10.1016/j.ibmb.2003.08.004
Kamita, Shizuo G. ; Hintona, Andrew C. ; Wheelock, Craig E. ; Wogulis, Mark D. ; Wilson, David K. ; Wolf, Nicola M. ; Stok, Jeanette E. ; Hock, Bertold ; Hammock, Bruce D. / Juvenile hormone (JH) esterase : Why are you so JH specific?. In: Insect Biochemistry and Molecular Biology. 2003 ; Vol. 33, No. 12. pp. 1261-1273.
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abstract = "Juvenile hormone esterases (JHEs) from six insects belonging to three orders (Lepidoptera, Coleoptera, and Diptera) were compared in terms of their deduced amino acid sequence and biochemical properties. The four lepidopteran JHEs showed from 52{\%} to 59{\%} identity to each other and about 30{\%} identity to the coleopteran and dipteran JHEs. The JHE of Manduca sexta was remarkably resistant to the addition of organic co-solvents and detergent; in some cases, it demonstrated significant activation of activity. Triflouromethylketone (TFK) inhibitors with chain lengths of 8, 10 or 12 carbons were highly effective against both lepidopteran and coleopteran JHEs. The coleopteran JHE remained sensitive to TFK inhibitors with a chain length of 6 carbons, whereas the lepidopteran JHEs were significantly less sensitive. When the chain was altered to a phenethyl moiety, the coleopteran JHE remained moderately sensitive, while the lepidopteran JHEs were much less sensitive. The lepidopteran and coleopteran JHEs did not show dramatic differences in specificity to α-naphthyl and p-nitrophenyl substrates. However, as the chain length of the α-naphthyl substrates increased from propionate to caprylate, there was a trend towards reduced activity. The JHE of M. sexta was crystallized and the properties of the crystal suggest a high-resolution structure will follow.",
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