Biology:5-epiaristolochene 1,3-dihydroxylase
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Short description: Class of enzymes
5-epiaristolochene 1,3-dihydroxylase | |||||||||
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Identifiers | |||||||||
EC number | 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).[1][2] This enzyme catalyses the following chemical reaction
- 5-epiaristolochene + 2 NADPH + 2 H+ + 2 O2 [math]\displaystyle{ \rightleftharpoons }[/math] capsidiol + 2 NADP+ + 2 H2O
5-epiaristolochene 1,3-dihydroxylase is a heme-thiolate protein (P-450).
References
- ↑ "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. September 2001. doi:10.1006/abbi.2001.2483. PMID 11556809.
- ↑ "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. February 2005. doi:10.1074/jbc.M411870200. PMID 15522862.
External links
- 5-epiaristolochene+1,3-dihydroxylase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/5-epiaristolochene 1,3-dihydroxylase.
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