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Structural characterization and functional analysis of juvenile hormone acid methyltransferase JHAMT3 from the silkworm, Bombyx mori.
Zhang, Li; Xu, Haiyang; Zhang, Yunshi; Zhang, Huan; Wang, Zhan; Guo, Pengchao; Zhao, Ping.
Afiliación
  • Zhang L; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China.
  • Xu H; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China.
  • Zhang Y; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China.
  • Zhang H; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China.
  • Wang Z; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China.
  • Guo P; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China; Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City & Southwest University,
  • Zhao P; State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, China; Biological Science Research Center, Southwest University, Chongqing, 400716, China; Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City & Southwest University,
Insect Biochem Mol Biol ; 151: 103863, 2022 12.
Article en En | MEDLINE | ID: mdl-36341863
Juvenile hormone acid methyltransferase (JHAMT) is a rate-limiting enzyme of juvenile hormone (JH) biosynthesis in insects. It transfers the methyl group of S-adenosyl methionine to either the carboxyl group of JH acids or farnesoic acid to produce JH. Six JHAMT paralogues have been identified in the silkworm (Bombyx mori); among them, JHAMT1 and JHAMT2 display a methyltransferase activity. Here, the three-dimensional crystal structure of inactive JHAMT3 and the binary complex of JHAMT3 with its cofactor S-adenosyl-l-homocysteine were determined through X-ray crystallization. Comparative structural analysis revealed that JHAMT3 adopted a similar structural pattern to that of functional JHAMT2, which comprised one core Rossmann fold domain and one substrate-binding domain. Similar to JHAMT2, JHAMT3 underwent a conformational change at the Rossmann fold domain because of cofactor binding, which promoted ligand accommodation. However, it exhibited a relatively rigid substrate-binding pocket compared with that of JHAMT2. JHAMT3 was also highly expressed in the silk gland of fourth- and fifth-instar B. mori larvae. The results of expression profiling combined with activity analysis suggested that JHAMT3 might function as a binding protein of JH acids for the regulation of JH acid titers. These findings provide a structural basis for enhancing the understanding of the physiological function of JHAMT3 and a rational framework for the development of potent and specific inhibitors of JHAMT family members.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bombyx / Hormonas Juveniles Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Insect Biochem Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bombyx / Hormonas Juveniles Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Insect Biochem Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido