| Entry |
|
| Name |
ipsdienol synthase;
myrcene hydroxylase;
CYP9T2;
CYP9T3
|
| Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
 |
| Sysname |
myrcene,NADPH---hemoprotein reductase:O2 oxidoreductase (hydroxylating)
|
| Reaction(IUBMB) |
myrcene + [reduced NADPH---hemoprotein reductase] + O2 = (R)-ipsdienol + [oxidized NADPH---hemoprotein reductase] + H2O [RN: R11055]
|
| Reaction(KEGG) |
|
| Substrate |
myrcene [CPD: C06074];
[reduced NADPH---hemoprotein reductase] [CPD: C03024];
O2 [CPD: C00007]
|
| Product |
(R)-ipsdienol [CPD: C20943];
[oxidized NADPH---hemoprotein reductase] [CPD: C03161];
H2O [CPD: C00001]
|
| Comment |
A cytochrome P-450 heme-thiolate protein. Involved in the insect aggregation pheromone production. Isolated from the pine engraver beetle, Ips pini. A small amount of (S)-ipsdienol is also formed. In vitro it also hydroxylated (+)- and (-)-alpha-pinene, 3-carene, and (+)-limonene, but not alpha-phellandrene, (-)-beta-pinene, gamma-terpinene, or terpinolene.
|
| History |
EC 1.14.14.31 created 2015 as EC 1.14.13.207, transferred 2016 to EC 1.14.14.31
|
| Pathway |
| Monoterpenoid biosynthesis | | Biosynthesis of secondary metabolites |
|
| Orthology |
|
| Reference |
|
| Authors |
Sandstrom P, Welch WH, Blomquist GJ, Tittiger C |
| Title |
Functional expression of a bark beetle cytochrome P450 that hydroxylates myrcene to ipsdienol. |
| Journal |
Insect. Biochem. Mol. Biol. 36 (2006) 835-45. |
| Sequence |
|
| Reference |
|
| Authors |
Song M, Kim AC, Gorzalski AJ, MacLean M, Young S, Ginzel MD, Blomquist GJ, Tittiger C |
| Title |
Functional characterization of myrcene hydroxylases from two geographically distinct Ips pini populations. |
| Journal |
Insect. Biochem. Mol. Biol. 43 (2013) 336-43. |
| Sequence |
|
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |