1.4.3.23: 7-chloro-L-tryptophan oxidase

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For detailed information about 7-chloro-L-tryptophan oxidase, go to the full flat file.

Reaction

Synonyms

RebO

ECTree

     1 Oxidoreductases

         1.4 Acting on the CH-NH₂ group of donors

             1.4.3 With oxygen as acceptor

                1.4.3.23 7-chloro-L-tryptophan oxidase

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122	AA Sequence
3	Cloned(Commentary)
3	Cofactor
4	kcat/KM [mM/s]
4	KM Value [mM]
3	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
3	Organism
9	Pathway
24	PDB ID
3	Purification (Commentary)
1	Reaction
3	Reference
11	Substrates and Products (Substrate)
3	Subunits
4	Synonyms
1	Systematic Name
4	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.4.3.23 - 7-chloro-L-tryptophan oxidase

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SYSTEMATIC NAME

IUBMB Comments

7-chloro-L-tryptophan:oxygen oxidoreductase

Contains a noncovalently bound FAD [1,2]. This enzyme catalyses a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes. During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide. The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan [1].