Investigation of the Substrate‐Binding Site of a Prostaglandin E Synthase in Bombyx mori
Prostaglandin E synthase (PGES) catalyzes the conversion of prostaglandin H 2 to prostaglandin E 2 in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm Bombyx mori (bmPGES) and d...
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| Veröffentlicht in: | The Protein Journal 2021-02, Vol.40 (1), p.63-67 |
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| creator | Yamamoto, Kohji Hirowatari, Aiko |
| description | Prostaglandin E synthase (PGES) catalyzes the conversion of prostaglandin H
2
to prostaglandin E
2
in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm
Bombyx mori
(bmPGES) and determined its crystal structure complexed with GSH. In the current study, we investigated the substrate-binding site of bmPGES by site-directed mutagenesis and X-ray crystallography. We found that the residues Tyr107, Val155, Met159, and Glu203 are located in the catalytic pockets of bmPGES, and mutagenesis of each residue reduced the bmPGES activity. Our results suggest that these four residues contribute to the catalytic activity of bmPGES. Overall, this structure-function study holds implications in controlling pests by designing rational and efficient pesticides. |
| doi_str_mv | 10.1007/s10930-020-09956-3 |
| format | Article |
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2
to prostaglandin E
2
in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm
Bombyx mori
(bmPGES) and determined its crystal structure complexed with GSH. In the current study, we investigated the substrate-binding site of bmPGES by site-directed mutagenesis and X-ray crystallography. We found that the residues Tyr107, Val155, Met159, and Glu203 are located in the catalytic pockets of bmPGES, and mutagenesis of each residue reduced the bmPGES activity. Our results suggest that these four residues contribute to the catalytic activity of bmPGES. Overall, this structure-function study holds implications in controlling pests by designing rational and efficient pesticides.</description><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>EISSN: 1875-8355</identifier><identifier>DOI: 10.1007/s10930-020-09956-3</identifier><identifier>PMID: 33403608</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Animal Anatomy ; Binding sites ; Biochemistry ; Bioorganic Chemistry ; Bombyx mori ; Catalytic activity ; Chemistry ; Chemistry and Materials Science ; Crystal structure ; Crystallography ; Crystals ; Enzymes ; Glutathione ; Histology ; Insects ; Morphology ; Mutagenesis ; Organic Chemistry ; Pest control ; Pesticides ; Pests ; Prostaglandin E ; Prostaglandin E2 ; Prostaglandin H2 ; Residues ; Silkworms ; Site-directed mutagenesis ; Structure ; Structure-function relationships ; Substrates ; Synthetic prostaglandins E ; X-ray crystallography</subject><ispartof>The Protein Journal, 2021-02, Vol.40 (1), p.63-67</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature 2021</rights><rights>COPYRIGHT 2021 Springer</rights><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c393t-bba453b376ebac03f9bd57c2beb166b4dff4883963ddb5f4ff364a99329e107e3</cites><orcidid>0000-0002-5859-912X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10930-020-09956-3$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10930-020-09956-3$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33403608$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamamoto, Kohji</creatorcontrib><creatorcontrib>Hirowatari, Aiko</creatorcontrib><title>Investigation of the Substrate‐Binding Site of a Prostaglandin E Synthase in Bombyx mori</title><title>The Protein Journal</title><addtitle>Protein J</addtitle><addtitle>Protein J</addtitle><description>Prostaglandin E synthase (PGES) catalyzes the conversion of prostaglandin H
2
to prostaglandin E
2
in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm
Bombyx mori
(bmPGES) and determined its crystal structure complexed with GSH. In the current study, we investigated the substrate-binding site of bmPGES by site-directed mutagenesis and X-ray crystallography. We found that the residues Tyr107, Val155, Met159, and Glu203 are located in the catalytic pockets of bmPGES, and mutagenesis of each residue reduced the bmPGES activity. Our results suggest that these four residues contribute to the catalytic activity of bmPGES. Overall, this structure-function study holds implications in controlling pests by designing rational and efficient pesticides.</description><subject>Animal Anatomy</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Bioorganic Chemistry</subject><subject>Bombyx mori</subject><subject>Catalytic activity</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Crystal structure</subject><subject>Crystallography</subject><subject>Crystals</subject><subject>Enzymes</subject><subject>Glutathione</subject><subject>Histology</subject><subject>Insects</subject><subject>Morphology</subject><subject>Mutagenesis</subject><subject>Organic Chemistry</subject><subject>Pest control</subject><subject>Pesticides</subject><subject>Pests</subject><subject>Prostaglandin E</subject><subject>Prostaglandin E2</subject><subject>Prostaglandin H2</subject><subject>Residues</subject><subject>Silkworms</subject><subject>Site-directed mutagenesis</subject><subject>Structure</subject><subject>Structure-function relationships</subject><subject>Substrates</subject><subject>Synthetic prostaglandins E</subject><subject>X-ray 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2
to prostaglandin E
2
in the presence of glutathione (GSH) in mammals. Amid the limited knowledge on prostaglandin and its related enzymes in insects, we recently identified PGES from the silkworm
Bombyx mori
(bmPGES) and determined its crystal structure complexed with GSH. In the current study, we investigated the substrate-binding site of bmPGES by site-directed mutagenesis and X-ray crystallography. We found that the residues Tyr107, Val155, Met159, and Glu203 are located in the catalytic pockets of bmPGES, and mutagenesis of each residue reduced the bmPGES activity. Our results suggest that these four residues contribute to the catalytic activity of bmPGES. Overall, this structure-function study holds implications in controlling pests by designing rational and efficient pesticides.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>33403608</pmid><doi>10.1007/s10930-020-09956-3</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-5859-912X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1572-3887 |
| ispartof | The Protein Journal, 2021-02, Vol.40 (1), p.63-67 |
| issn | 1572-3887 1573-4943 1875-8355 |
| language | eng |
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| source | SpringerLink Journals |
| subjects | Animal Anatomy Binding sites Biochemistry Bioorganic Chemistry Bombyx mori Catalytic activity Chemistry Chemistry and Materials Science Crystal structure Crystallography Crystals Enzymes Glutathione Histology Insects Morphology Mutagenesis Organic Chemistry Pest control Pesticides Pests Prostaglandin E Prostaglandin E2 Prostaglandin H2 Residues Silkworms Site-directed mutagenesis Structure Structure-function relationships Substrates Synthetic prostaglandins E X-ray crystallography |
| title | Investigation of the Substrate‐Binding Site of a Prostaglandin E Synthase in Bombyx mori |
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