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{{Short description|Class of enzymes}}
{{Infobox enzyme
{{Infobox enzyme
| Name = 1,8-Cineole 2-exo-monooxygenase
| Name = 1,8-Cineole 2-exo-monooxygenase
| EC_number = 1.14.13.157
| EC_number = 1.14.13.157
| CAS_number =
| CAS_number =
| GO_code =
| IUBMB_EC_number = 1/14/13/157
| GO_code =
| image =
| image =
| width =
| width =
| caption =
| caption =
}}
}}
'''1,8-Cineole 2-exo-monooxygenase''' ({{EC number|1.14.13.157}}, ''[[CYP3A4]]'') is an [[enzyme]] with system name ''1,8-cineole,NADPH:oxygen oxidoreductase (2-exo-hydroxylating)''.<ref>{{cite journal | title = Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from ''Eucalyptus polybractea'', by cytochrome P450 3A enzymes in rat and human liver microsomes |author = Miyazawa, M., Shindo, M. and Shimada, T. |journal = Drug Metab. Dispos. |year = 2001 |volume = 29 |pages = 200–205 |pmid = 11159812 |issue=2}}</ref><ref>{{cite journal | title = Biotransformation of 1,8-cineole by human liver microsomes |author = Miyazawa, M. and Shindo, M. |journal = Nat. Prod. Lett. |year = 2001 |volume = 15 |pages = 49–53 |pmid = 11547423 |doi=10.1080/10575630108041257 |issue=1}}</ref><ref>{{cite journal | title = Roles of cytochrome ''P''<sub>450</sub> 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes |author = Miyazawa, M., Shindo, M. and Shimada, T. |journal = Xenobiotica |year = 2001 |volume = 31 |pages = 713–723 |pmid = 11695850 |doi=10.1080/00498250110065595}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
'''1,8-Cineole 2-exo-monooxygenase''' ({{EC number|1.14.13.157}}, ''[[CYP3A4]]'') is an [[enzyme]] with [[List of enzymes|systematic name]] ''1,8-cineole,NADPH:oxygen oxidoreductase (2-exo-hydroxylating)''.<ref>{{cite journal | vauthors = Miyazawa M, Shindo M, Shimada T | title = Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes | journal = Drug Metabolism and Disposition | volume = 29 | issue = 2 | pages = 200–5 | date = February 2001 | pmid = 11159812 }}</ref><ref>{{cite journal | vauthors = Miyazawa M, Shindo M | title = Biotransformation of 1,8-cineole by human liver microsomes | journal = Natural Product Letters | volume = 15 | issue = 1 | pages = 49–53 | year = 2001 | pmid = 11547423 | doi = 10.1080/10575630108041257 }}</ref><ref>{{cite journal | vauthors = Miyazawa M, Shindo M, Shimada T | title = Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes | journal = Xenobiotica; The Fate of Foreign Compounds in Biological Systems | volume = 31 | issue = 10 | pages = 713–23 | date = October 2001 | pmid = 11695850 | doi = 10.1080/00498250110065595 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]


: 1,8-[[cineole]] + NADPH + H<sup>+</sup> + O<sub>2</sub> <math>\rightleftharpoons</math> 2-exo-hydroxy-1,8-cineole + NADP<sup>+</sup> + H<sub>2</sub>O
: 1,8-[[cineole]] + NADPH + H<sup>+</sup> + O<sub>2</sub> <math>\rightleftharpoons</math> 2-exo-hydroxy-1,8-cineole + NADP<sup>+</sup> + H<sub>2</sub>O
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== External links ==
== External links ==
* {{MeshName|1,8-cineole+2-exo-monooxygenase}}
* {{MeshName|1,8-cineole+2-exo-monooxygenase}}

{{Dioxygenases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}


[[Category:EC 1.14.13]]
[[Category:EC 1.14.13]]

Latest revision as of 12:24, 26 August 2023

1,8-Cineole 2-exo-monooxygenase
Identifiers
EC no.1.14.13.157
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

1,8-Cineole 2-exo-monooxygenase (EC 1.14.13.157, CYP3A4) is an enzyme with systematic name 1,8-cineole,NADPH:oxygen oxidoreductase (2-exo-hydroxylating).[1][2][3] This enzyme catalyses the following chemical reaction

1,8-cineole + NADPH + H+ + O2 2-exo-hydroxy-1,8-cineole + NADP+ + H2O

1,8-Cineole 2-exo-monooxygenase is a heme-thiolate protein (P-450).

References

[edit]
  1. ^ Miyazawa M, Shindo M, Shimada T (February 2001). "Oxidation of 1,8-cineole, the monoterpene cyclic ether originated from eucalyptus polybractea, by cytochrome P450 3A enzymes in rat and human liver microsomes". Drug Metabolism and Disposition. 29 (2): 200–5. PMID 11159812.
  2. ^ Miyazawa M, Shindo M (2001). "Biotransformation of 1,8-cineole by human liver microsomes". Natural Product Letters. 15 (1): 49–53. doi:10.1080/10575630108041257. PMID 11547423.
  3. ^ Miyazawa M, Shindo M, Shimada T (October 2001). "Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes". Xenobiotica; The Fate of Foreign Compounds in Biological Systems. 31 (10): 713–23. doi:10.1080/00498250110065595. PMID 11695850.
[edit]
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