MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsComposite Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Nicotiana tabacum: 5-epi-aristolochene-1,3-dihydroxylaseInferred from experiment: 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): -181.4065Inferred by computational analysis [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.

Citations: [Ralston01, Takahashi05]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R09573, Rhea:28226

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:

Created 07-Dec-2010 by Caspi R, SRI International


Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.5 on Sun Nov 29, 2015, BIOCYC13B.