Key Amino Acids for Transferase Activity of GDSL Lipases
The Gly-Asp-Ser-Leu (GDSL) motif of esterase/lipase family proteins (GELPs) generally exhibit esterase activity, whereas transferase activity is markedly preferred in several GELPs, including the GDSL lipase TciGLIP, which is responsible for the biosynthesis of the natural insecticide, pyrethrin I....
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| Veröffentlicht in: | International journal of molecular sciences 2022-12, Vol.23 (23), p.15141 |
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| creator | Yamashiro, Takanori Shiraishi, Akira Nakayama, Koji Satake, Honoo |
| description | The Gly-Asp-Ser-Leu (GDSL) motif of esterase/lipase family proteins (GELPs) generally exhibit esterase activity, whereas transferase activity is markedly preferred in several GELPs, including the
GDSL lipase TciGLIP, which is responsible for the biosynthesis of the natural insecticide, pyrethrin I. This transferase activity is due to the substrate affinity regulated by the protein structure and these features are expected to be conserved in transferase activity-exhibiting GELPs (tr-GELPs). In this study, we identified two amino acid residues, [N/R]208 and D484, in GELP sequence alignments as candidate key residues for the transferase activity of tr-GELPs by two-entropy analysis. Molecular phylogenetic analysis demonstrated that each tr-GELP is located in the clusters for non-tr-GELPs, and most GELPs conserve at least one of the two residues. These results suggest that the two conserved residues are required for the acquisition of transferase activity in the GELP family. Furthermore, substrate docking analyses using ColabFold-generated structure models of both natives and each of the two amino acids-mutated TciGLIPs also revealed numerous docking models for the proper access of substrates to the active site, indicating crucial roles of these residues of TciGLIP in its transferase activity. This is the first report on essential residues in tr-GELPs for the transferase activity. |
| doi_str_mv | 10.3390/ijms232315141 |
| format | Article |
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GDSL lipase TciGLIP, which is responsible for the biosynthesis of the natural insecticide, pyrethrin I. This transferase activity is due to the substrate affinity regulated by the protein structure and these features are expected to be conserved in transferase activity-exhibiting GELPs (tr-GELPs). In this study, we identified two amino acid residues, [N/R]208 and D484, in GELP sequence alignments as candidate key residues for the transferase activity of tr-GELPs by two-entropy analysis. Molecular phylogenetic analysis demonstrated that each tr-GELP is located in the clusters for non-tr-GELPs, and most GELPs conserve at least one of the two residues. These results suggest that the two conserved residues are required for the acquisition of transferase activity in the GELP family. Furthermore, substrate docking analyses using ColabFold-generated structure models of both natives and each of the two amino acids-mutated TciGLIPs also revealed numerous docking models for the proper access of substrates to the active site, indicating crucial roles of these residues of TciGLIP in its transferase activity. This is the first report on essential residues in tr-GELPs for the transferase activity.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms232315141</identifier><identifier>PMID: 36499468</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acid sequence ; Amino Acids ; Biosynthesis ; Entropy ; Esterase ; Esterases - metabolism ; Lipase ; Lipase - metabolism ; Metabolism ; Metabolites ; Mutation ; Phylogenetics ; Phylogeny ; Protein structure ; Proteins ; Rape plants ; Residues ; Substrate preferences ; Transferases</subject><ispartof>International journal of molecular sciences, 2022-12, Vol.23 (23), p.15141</ispartof><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-b56f29e8f0c15e7c9f6548378301a700c55b881b5e86192bca11c9cec43d87c3</citedby><cites>FETCH-LOGICAL-c525t-b56f29e8f0c15e7c9f6548378301a700c55b881b5e86192bca11c9cec43d87c3</cites><orcidid>0000-0003-3456-3074 ; 0000-0003-1165-3624</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736205/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736205/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36499468$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamashiro, Takanori</creatorcontrib><creatorcontrib>Shiraishi, Akira</creatorcontrib><creatorcontrib>Nakayama, Koji</creatorcontrib><creatorcontrib>Satake, Honoo</creatorcontrib><title>Key Amino Acids for Transferase Activity of GDSL Lipases</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>The Gly-Asp-Ser-Leu (GDSL) motif of esterase/lipase family proteins (GELPs) generally exhibit esterase activity, whereas transferase activity is markedly preferred in several GELPs, including the
GDSL lipase TciGLIP, which is responsible for the biosynthesis of the natural insecticide, pyrethrin I. This transferase activity is due to the substrate affinity regulated by the protein structure and these features are expected to be conserved in transferase activity-exhibiting GELPs (tr-GELPs). In this study, we identified two amino acid residues, [N/R]208 and D484, in GELP sequence alignments as candidate key residues for the transferase activity of tr-GELPs by two-entropy analysis. Molecular phylogenetic analysis demonstrated that each tr-GELP is located in the clusters for non-tr-GELPs, and most GELPs conserve at least one of the two residues. These results suggest that the two conserved residues are required for the acquisition of transferase activity in the GELP family. Furthermore, substrate docking analyses using ColabFold-generated structure models of both natives and each of the two amino acids-mutated TciGLIPs also revealed numerous docking models for the proper access of substrates to the active site, indicating crucial roles of these residues of TciGLIP in its transferase activity. This is the first report on essential residues in tr-GELPs for the transferase activity.</description><subject>Amino acid sequence</subject><subject>Amino Acids</subject><subject>Biosynthesis</subject><subject>Entropy</subject><subject>Esterase</subject><subject>Esterases - metabolism</subject><subject>Lipase</subject><subject>Lipase - metabolism</subject><subject>Metabolism</subject><subject>Metabolites</subject><subject>Mutation</subject><subject>Phylogenetics</subject><subject>Phylogeny</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Rape plants</subject><subject>Residues</subject><subject>Substrate preferences</subject><subject>Transferases</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpdkc1LAzEQxYMotlaPXmXBi5fVfO4mF6FUreKCB3sP2TTRlO6mJruF_vdGWkv1NMObH495PAAuEbwlRMA7t2giJpgghig6AkNEMc4hLMrjg30AzmJcQJhAJk7BgBRUCFrwIeCvZpONG9f6bKzdPGbWh2wWVButCSqapHZu7bpN5m02fXivssqtkh7PwYlVy2gudnMEZk-Ps8lzXr1NXybjKtcMsy6vWWGxMNxCjZgptbAFo5yUnECkSgg1YzXnqGaGF0jgWiuEtNBGUzLnpSYjcL-1XfV1Y-batF1QS7kKrlFhI71y8u-ldZ_yw6-lKEmBIUsGNzuD4L96EzvZuKjNcqla4_socckIgYJAmtDrf-jC96FN6RJFOWMQcZGofEvp4GMMxu6fQVD-VCL_VJL4q8MEe_q3A_INp-CFwg</recordid><startdate>20221201</startdate><enddate>20221201</enddate><creator>Yamashiro, Takanori</creator><creator>Shiraishi, Akira</creator><creator>Nakayama, Koji</creator><creator>Satake, Honoo</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3456-3074</orcidid><orcidid>https://orcid.org/0000-0003-1165-3624</orcidid></search><sort><creationdate>20221201</creationdate><title>Key Amino Acids for Transferase Activity of GDSL Lipases</title><author>Yamashiro, Takanori ; 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| source | MDPI - Multidisciplinary Digital Publishing Institute; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino acid sequence Amino Acids Biosynthesis Entropy Esterase Esterases - metabolism Lipase Lipase - metabolism Metabolism Metabolites Mutation Phylogenetics Phylogeny Protein structure Proteins Rape plants Residues Substrate preferences Transferases |
| title | Key Amino Acids for Transferase Activity of GDSL Lipases |
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