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Functional analysis of novel sulfotransferases in the silkworm Bombyx mori.
- Source :
-
Archives of insect biochemistry and physiology [Arch Insect Biochem Physiol] 2020 Jul; Vol. 104 (3), pp. e21671. Date of Electronic Publication: 2020 Mar 29. - Publication Year :
- 2020
-
Abstract
- Sulfoconjugation plays a vital role in the detoxification of xenobiotics and in the metabolism of endogenous compounds. In this study, we aimed to identify new members of the sulfotransferase (SULT) superfamily in the silkworm Bombyx mori. Based on amino acid sequence and phylogenetic analyses, two new enzymes, swSULT ST1 and swSULT ST2, were identified that appear to belong to a distinct group of SULTs including several other insect SULTs. We expressed, purified, and characterized recombinant SULTs. While swSULT ST1 sulfated xanthurenic acid and pentachlorophenol, swSULT ST2 exclusively utilized xanthurenic acid as a substrate. Based on these results, and those concerning the tissue distribution and substrate specificity toward pentachlorophenol analyses, we hypothesize that swSULT ST1 plays a role in the detoxification of xenobiotics, including insecticides, in the silkworm midgut and in the induction of gametogenesis in silkworm ovary and testis. Collectively, the data obtained herein contribute to a better understanding of SULT enzymatic functions in insects.<br /> (© 2020 Wiley Periodicals, Inc.)
- Subjects :
- Amino Acid Sequence
Animals
Bombyx growth & development
Bombyx metabolism
Female
Gametogenesis
Gastrointestinal Tract enzymology
Insect Proteins
Larva enzymology
Male
Ovary
Pentachlorophenol metabolism
Phylogeny
Sulfotransferases metabolism
Testis
Xanthurenates metabolism
Bombyx enzymology
Inactivation, Metabolic
Sulfotransferases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-6327
- Volume :
- 104
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Archives of insect biochemistry and physiology
- Publication Type :
- Academic Journal
- Accession number :
- 32227386
- Full Text :
- https://doi.org/10.1002/arch.21671