TE contents of millipede and centipede.
<div><p>Hydrogen cyanide (HCN) is a highly toxic biogenic compound. Unlike most natural defensive chemicals, which are typically lineage-specific, the biosynthesis and liberation of HCN, called “cyanogenesis”, occur sporadically among arthropod and plant lineages. This suggests that cyan...
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2025
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| _version_ | 1849927642359267328 |
|---|---|
| author | Takuya Yamaguchi (4543105) |
| author2 | Yasuhisa Asano (727606) |
| author2_role | author |
| author_facet | Takuya Yamaguchi (4543105) Yasuhisa Asano (727606) |
| author_role | author |
| dc.creator.none.fl_str_mv | Takuya Yamaguchi (4543105) Yasuhisa Asano (727606) |
| dc.date.none.fl_str_mv | 2025-11-24T18:30:14Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pgen.1011955.s027 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/dataset/TE_contents_of_millipede_and_centipede_/30697230 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |
| dc.title.none.fl_str_mv | TE contents of millipede and centipede. |
| dc.type.none.fl_str_mv | Dataset info:eu-repo/semantics/publishedVersion dataset |
| description | <div><p>Hydrogen cyanide (HCN) is a highly toxic biogenic compound. Unlike most natural defensive chemicals, which are typically lineage-specific, the biosynthesis and liberation of HCN, called “cyanogenesis”, occur sporadically among arthropod and plant lineages. This suggests that cyanogenesis has evolved independently numerous times in the animal and plant kingdoms. Although cyanogenesis was identified in millipedes 140 years ago, the cyanogenesis-related enzymes in these arthropods have not yet been fully identified. Here, we report a complete set of cyanogenesis-related enzymes in the millipede <i>Chamberlinius hualienensis</i> based on an analysis combining genome sequencing and biological characterisation. The gene encoding hydroxynitrile lyase, which catalyses the liberation of HCN from (<i>R</i>)-mandelonitrile, and its paralogous genes were clustered, indicating sequential duplication of their coding genes, giving rise to hydroxynitrile lyase in millipedes. We discovered that (<i>R</i>)-mandelonitrile cyanohydrin biosynthesis in <i>C. hualienensis</i> utilises a flavin-dependent monooxygenase (ChuaMOxS) for the initial aldoxime synthesis step, similar to the process in ferns, instead of cytochrome P450 (CYP) as in higher plants and insects. Although a single CYP is responsible for subsequently converting aldoxime into cyanohydrin in plants and insects, the reaction involves two enzymes in millipedes. We found two millipede CYPs (CYP4GL4 and CYP30008A2) that catalyse aldoxime dehydration to produce nitrile, in addition to CYP3201B1, which then catalyses the formation of (<i>R</i>)-mandelonitrile from nitrile. The discovery of cyanogenesis-related enzymes in millipedes demonstrates that cyanogenic millipedes evolved these enzymes independently from plants and insects, providing a deeper understanding of the mechanisms underlying the evolution of metabolic pathways.</p></div> |
| eu_rights_str_mv | openAccess |
| id | Manara_efde1296e45243990c36f4c4b2152709 |
| identifier_str_mv | 10.1371/journal.pgen.1011955.s027 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30697230 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | TE contents of millipede and centipede.Takuya Yamaguchi (4543105)Yasuhisa Asano (727606)BiochemistryEvolutionary BiologyEcologyPlant BiologyVirologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedsubsequently converting aldoximenatural defensive chemicalsindicating sequential duplicationcatalyse aldoxime dehydrationdiv >< pcyanogenic millipedes evolvedchamberlinius hualienensis </hualienensis </r </typically lineagerelated enzymesplant lineagesplant kingdomsparalogous genesmillipedes demonstratesmechanisms underlyinghydroxynitrile lyasehydrogen cyanidegiving riseenzymes independentlydependent monooxygenasedeeper understandingcytochrome p450complete setcoding genesbiological characterisation>)- mandelonitrile<div><p>Hydrogen cyanide (HCN) is a highly toxic biogenic compound. Unlike most natural defensive chemicals, which are typically lineage-specific, the biosynthesis and liberation of HCN, called “cyanogenesis”, occur sporadically among arthropod and plant lineages. This suggests that cyanogenesis has evolved independently numerous times in the animal and plant kingdoms. Although cyanogenesis was identified in millipedes 140 years ago, the cyanogenesis-related enzymes in these arthropods have not yet been fully identified. Here, we report a complete set of cyanogenesis-related enzymes in the millipede <i>Chamberlinius hualienensis</i> based on an analysis combining genome sequencing and biological characterisation. The gene encoding hydroxynitrile lyase, which catalyses the liberation of HCN from (<i>R</i>)-mandelonitrile, and its paralogous genes were clustered, indicating sequential duplication of their coding genes, giving rise to hydroxynitrile lyase in millipedes. We discovered that (<i>R</i>)-mandelonitrile cyanohydrin biosynthesis in <i>C. hualienensis</i> utilises a flavin-dependent monooxygenase (ChuaMOxS) for the initial aldoxime synthesis step, similar to the process in ferns, instead of cytochrome P450 (CYP) as in higher plants and insects. Although a single CYP is responsible for subsequently converting aldoxime into cyanohydrin in plants and insects, the reaction involves two enzymes in millipedes. We found two millipede CYPs (CYP4GL4 and CYP30008A2) that catalyse aldoxime dehydration to produce nitrile, in addition to CYP3201B1, which then catalyses the formation of (<i>R</i>)-mandelonitrile from nitrile. The discovery of cyanogenesis-related enzymes in millipedes demonstrates that cyanogenic millipedes evolved these enzymes independently from plants and insects, providing a deeper understanding of the mechanisms underlying the evolution of metabolic pathways.</p></div>2025-11-24T18:30:14ZDatasetinfo:eu-repo/semantics/publishedVersiondataset10.1371/journal.pgen.1011955.s027https://figshare.com/articles/dataset/TE_contents_of_millipede_and_centipede_/30697230CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/306972302025-11-24T18:30:14Z |
| spellingShingle | TE contents of millipede and centipede. Takuya Yamaguchi (4543105) Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |
| status_str | publishedVersion |
| title | TE contents of millipede and centipede. |
| title_full | TE contents of millipede and centipede. |
| title_fullStr | TE contents of millipede and centipede. |
| title_full_unstemmed | TE contents of millipede and centipede. |
| title_short | TE contents of millipede and centipede. |
| title_sort | TE contents of millipede and centipede. |
| topic | Biochemistry Evolutionary Biology Ecology Plant Biology Virology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified subsequently converting aldoxime natural defensive chemicals indicating sequential duplication catalyse aldoxime dehydration div >< p cyanogenic millipedes evolved chamberlinius hualienensis </ hualienensis </ r </ typically lineage related enzymes plant lineages plant kingdoms paralogous genes millipedes demonstrates mechanisms underlying hydroxynitrile lyase hydrogen cyanide giving rise enzymes independently dependent monooxygenase deeper understanding cytochrome p450 complete set coding genes biological characterisation >)- mandelonitrile |