5-epiaristolochene 1,3-dihydroxylase
| 5-epiaristolochene 1,3-dihydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.119 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
5-epiaristolochene 1,3-dihydroxylase (EC 1.14.13.119, 5-epi-aristolochene 1,3-dihydroxylase, EAH) is an enzyme with systematic name 5-epiaristolochene,NADPH:oxygen oxidoreductase (1- and 3-hydroxylating).[1][2] This enzyme catalyses the following chemical reaction
- 5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2 capsidiol + 2 NADP+ + 2 H2O
5-epiaristolochene 1,3-dihydroxylase is a heme-thiolate protein (P-450).
References
- ^ Ralston L, Kwon ST, Schoenbeck M, Ralston J, Schenk DJ, Coates RM, Chappell J (September 2001). "Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum)". Archives of Biochemistry and Biophysics. 393 (2): 222–35. doi:10.1006/abbi.2001.2483. PMID 11556809.
- ^ Takahashi S, Zhao Y, O'Maille PE, Greenhagen BT, Noel JP, Coates RM, Chappell J (February 2005). "Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome P450 enzyme catalyzing successive hydroxylations of sesquiterpenes". The Journal of Biological Chemistry. 280 (5): 3686–96. doi:10.1074/jbc.M411870200. PMC 2859954. PMID 15522862.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
External links
- 5-epiaristolochene+1,3-dihydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
