1,8-Cineole 2-endo-monooxygenase

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1,8-Cineole 2-endo-monooxygenase
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EC no. 1.14.14.133
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1,8-Cineole 2-endo-monooxygenase (EC 1.14.14.133, Formerly EC 1.14.13.156, P450cin, CYP176A, CYP176A1) is an enzyme with systematic name 1,8-cineole,NADPH:oxygen oxidoreductase (2-endo-hydroxylating). [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

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

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

Related Research Articles

Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system.

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Epi-isozizaene 5-monooxygenase (EC 1.14.13.106, CYP170A1) is an enzyme with systematic name (+)-epi-isozizaene,NADPH:oxygen oxidoreductase (5-hydroxylating). This enzyme catalyses the following chemical reaction

Angelicin synthase (EC 1.14.13.115, CYP71AJ4 (gene)) is an enzyme with systematic name (+)-columbianetin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction:

Isoleucine N-monooxygenase (EC 1.14.13.117, CYP79D3, CYP79D4) is an enzyme with systematic name L-isoleucine,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reaction

Valine N-monooxygenase (EC 1.14.13.118, CYP79D1, CYP79D2) is an enzyme with systematic name L-valine,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reaction

Premnaspirodiene oxygenase (EC 1.14.13.121, HPO, Hyoscymus muticus premnaspirodiene oxygenase) is an enzyme with systematic name (-)-vetispiradiene,NADPH:oxygen 2alpha-oxidoreductase. This enzyme catalyses the following chemical reaction

Phenylalanine N-monooxygenase (EC 1.14.14.40, phenylalanine N-hydroxylase, CYP79A2) is an enzyme with systematic name L-phenylalanine,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reaction

Tryptophan N-monooxygenase (EC 1.14.13.125, tryptophan N-hydroxylase, CYP79B1, CYP79B2, CYP79B3) is an enzyme with systematic name L-tryptophan,NADPH:oxygen oxidoreductase (N-hydroxylating). This enzyme catalyses the following chemical reaction

Cholest-4-en-3-one 26-monooxygenase (EC 1.14.13.141, CYP125, CYP125A1, cholest-4-en-3-one 27-monooxygenase) is an enzyme with systematic name cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating). This enzyme catalyses the following chemical reaction

Erythromycin 12 hydroxylase (EC 1.14.13.154, EryK) is an enzyme with systematic name erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating) . This enzyme catalyses the following chemical reaction

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). This enzyme catalyses the following chemical reaction

Sphinganine C4-monooxygenase (EC 1.14.13.169, sphingolipid C4-hydroxylase, SUR2 (gene), SBH1 (gene), SBH2 (gene)) is an enzyme with systematic name sphinganine,NADPH:oxygen oxidoreductase (C4-hydroxylating). This enzyme catalyses the following chemical reaction

Biflaviolin synthase (EC 1.14.21.7, CYP158A2, CYP 158A2, cytochrome P450 158A2) is an enzyme with systematic name flaviolin,NADPH:oxygen oxidoreductase. This enzyme catalyses the following chemical reaction

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<span class="mw-page-title-main">L-ornithine N5 monooxygenase</span> Enzyme

L-ornithine N5 monooxygenase (EC 1.14.13.195 or EC 1.14.13.196) is an enzyme which catalyzes one of the following chemical reactions:

L-ornithine + NADPH + O2 N(5)-hydroxy-L-ornithine + NADP+ + H2O L-ornithine + NAD(P)H + O2 N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O

References

  1. ↑ Hawkes DB, Adams GW, Burlingame AL, Ortiz de Montellano PR, De Voss JJ (August 2002). "Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization". The Journal of Biological Chemistry. 277 (31): 27725–32. doi: 10.1074/jbc.M203382200 . PMID   12016226.
  2. ↑ Meharenna YT, Li H, Hawkes DB, Pearson AG, De Voss J, Poulos TL (July 2004). "Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam". Biochemistry. 43 (29): 9487–94. doi:10.1021/bi049293p. PMID   15260491.
  3. ↑ Kimmich N, Das A, Sevrioukova I, Meharenna Y, Sligar SG, Poulos TL (September 2007). "Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin". The Journal of Biological Chemistry. 282 (37): 27006–11. doi: 10.1074/jbc.M703790200 . PMID   17606612.
  4. ↑ Meharenna YT, Slessor KE, Cavaignac SM, Poulos TL, De Voss JJ (April 2008). "The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin". The Journal of Biological Chemistry. 283 (16): 10804–12. doi: 10.1074/jbc.M709722200 . PMC   2447660 . PMID   18270198.
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