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cyp15 [2025/07/25 06:10] – external edit 127.0.0.1cyp15 [2025/09/12 06:07] (current) renefeyereisen
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 The CYP15 sequences do not form a monophyletic clade. The founder CYP15A1 from //Diploptera punctata// is the highly specific methyl farnesoate (MF) epoxidase that makes juvenile hormone III (methyl farnesoate 10//R//,11-epoxide) in the corpora allata of this cockroach (Helvig et al., 2004). It is part of a strongly supported clade (93/93.8/72) of CYP15A sequences, related to CYP15B1 of mosquitoes and to the CYP15C clade of Lepidoptera. CYP15C1 of //Bombyx mori// is the allatal farnesoic acid epoxidase (Daimon et al., 2012),  The CYP15 sequences do not form a monophyletic clade. The founder CYP15A1 from //Diploptera punctata// is the highly specific methyl farnesoate (MF) epoxidase that makes juvenile hormone III (methyl farnesoate 10//R//,11-epoxide) in the corpora allata of this cockroach (Helvig et al., 2004). It is part of a strongly supported clade (93/93.8/72) of CYP15A sequences, related to CYP15B1 of mosquitoes and to the CYP15C clade of Lepidoptera. CYP15C1 of //Bombyx mori// is the allatal farnesoic acid epoxidase (Daimon et al., 2012), 
  
-//Bombyx mori// CYP15B1 catalyses (homo and bishomo) farnesoic acid (i.e. JH, II, JH I and JH III -acid) epoxidation (T. Shinoda, pers. comm.) as expected from Lepidoptera where epoxidation takes place before esterification by JHAMT (juvenile hormone acid methyl transferase). The CYP15 enzymes have therefore evolved a lineage-specific substrate selectivity. Farnesoic acid is a better substrate for CYP15B1 than methyl farnesoate (Daimon et al., 2012), while CYP15A1 of //Tribolium castaneum// is a mixed farnesoic acid/MF epoxidase (Minakuchi et al., 2015).+//Bombyx mori// CYP15C1 catalyses (homo and bishomo) farnesoic acid (i.e. JH, II, JH I and JH III -acid) epoxidation (T. Shinoda, pers. comm.) as expected from Lepidoptera where epoxidation takes place before esterification by JHAMT (juvenile hormone acid methyl transferase). The CYP15 enzymes have therefore evolved a lineage-specific substrate selectivity. Farnesoic acid is a better substrate for CYP15C1 than methyl farnesoate (Daimon et al., 2012), while CYP15A1 of //Tribolium castaneum// is a mixed farnesoic acid/MF epoxidase (Minakuchi et al., 2015).
  
 The CYP15A/C clade therefore represents the bona fide enzymes producing the epoxide characteristic of juvenile hormones (JH). The CYP nomenclature places several CYP2 clan sequences in the CYP15 family, including two CYP15H from locusts, six from //Machilis hrabei//, three from //Calopterx splendens//, eight from //Catajapyx aquilonaris// and three from //Sinella curviseta//, but these do not form a single well supported clade and their function is unknown.  The CYP15A/C clade therefore represents the bona fide enzymes producing the epoxide characteristic of juvenile hormones (JH). The CYP nomenclature places several CYP2 clan sequences in the CYP15 family, including two CYP15H from locusts, six from //Machilis hrabei//, three from //Calopterx splendens//, eight from //Catajapyx aquilonaris// and three from //Sinella curviseta//, but these do not form a single well supported clade and their function is unknown. 
cyp15.txt · Last modified: by renefeyereisen