5-epiaristolochene 1,3-dihydroxylase | |||||||||
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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 | ||||||||
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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). 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.
External links
- 5-epiaristolochene+1,3-dihydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) | |
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1.14.11: 2-oxoglutarate | |
1.14.13: NADH or NADPH | |
1.14.14: reduced flavin or flavoprotein | |
1.14.15: reduced iron–sulfur protein | |
1.14.16: reduced pteridine (BH4 dependent) | |
1.14.17: reduced ascorbate | |
1.14.18-19: other | |
1.14.99 - miscellaneous |
Enzymes | |
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Regulation | |
Classification | |
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