|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
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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, and some reactions have been computationally balanced for hydrogen by adding free protons. 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.
Unification Links: Rhea:28226
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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