|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
|Pseudomonas fluorescens :||tryptophan side chain oxidase / tryptophan 2'-dioxygenase
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: tryptophan 2′-dioxygenase
Enzyme Commission Synonyms: indole-3-alkane α-hydroxylase, tryptophan side-chain α,β-oxidase, tryptophan side chain oxidase II, tryptophan side-chain oxidase, TSO, indolyl-3-alkan α-hydroxylase, tryptophan side chain oxidase type I, TSO I , TSO II, tryptophan side chain oxidase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -109.23899 [Latendresse13]
Enzyme Commission Summary:
A hemoprotein. Acts on a number of indole-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position. Best substrates were L-tryptophan and 5-hydroxy-L-tryptophan.
Roberts77: Roberts J, Rosenfeld HJ (1977). "Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme." J Biol Chem 252(8);2640-7. PMID: 15994
Takai77: Takai K, Ushiro H, Noda Y, Narumiya S, Tokuyama T (1977). "Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives." J Biol Chem 252(8);2648-56. PMID: 15995
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