|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Composite Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
|Nicotiana tabacum:||5-epi-aristolochene-1,3-dihydroxylase: EAH|
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 5-epiaristolochene 1,3-dihydroxylase
Enzyme Commission Synonyms: 5-epi-aristolochene 1,3-dihydroxylase, EAH
Taxonomic Range: Viridiplantae
(+)-5-epi-aristolochene + NADPH + oxygen + H+ → 3-deoxy-capsidiol + NADP+ + H2O,
3-deoxy-capsidiol + NADPH + oxygen + H+ → capsidiol + NADP+ + H2O,
(+)-5-epi-aristolochene + NADPH + oxygen + H+ → 1-deoxy-capsidiol + NADP+ + H2O,
1-deoxy-capsidiol + NADPH + oxygen + H+ → capsidiol + NADP+ + H2O
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -181.4065 [Latendresse13]
A heme-thiolate protein (P-450). Kinetic studies suggest that 3-deoxy-capsidiol is mainly formed first followed by hydroxylation at C-3. However the reverse order via 1-deoxy-capsidiol does occur.
Enzyme Commission Summary:
A heme-thiolate protein (P-450). Kinetic studies suggest that 1β-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3α-hydroxyepiaristolochene does occur.
Ralston01: Ralston L, Kwon ST, Schoenbeck M, Ralston J, Schenk DJ, Coates RM, Chappell J (2001). "Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum)." Arch Biochem Biophys 393(2);222-35. PMID: 11556809
Takahashi05: Takahashi S, Zhao Y, O'maille PE, Greenhagen BT, Noel JP, Coates RM, Chappell J (2005). "Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome p450 enzyme catalyzing successive hydroxylations of sesquiterpenes." J Biol Chem 280(5);3686-96. PMID: 15522862
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