Enzymes
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline indole Identifier CHEBI:16881 (Beilstein: 107693; CAS: 120-72-9) help_outline Charge 0 Formula C8H7N InChIKeyhelp_outline SIKJAQJRHWYJAI-UHFFFAOYSA-N SMILEShelp_outline c1cc2ccccc2[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,779 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-formamidobenzaldehyde Identifier CHEBI:18033 Charge 0 Formula C8H7NO2 InChIKeyhelp_outline PVIMSPYDDGDCTG-UHFFFAOYSA-N SMILEShelp_outline [H]C(=O)Nc1ccccc1C([H])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:11212 | RHEA:11213 | RHEA:11214 | RHEA:11215 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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AN INDOLE OXIDASE ISOLATED FROM THE LEAVES OF TECOMA STANS.
NAIR P.M., VAIDYANATHAN C.S.
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Purification and Characterization of a New Indole Oxygenase from the Leaves of Tecoma stans L.
Kunapuli S.P., Vaidyanathan C.S.
A new indole oxygenase from the leaves of Tecoma stans was isolated and purified to homogenity. The purified enzyme system catalyzes the conversion of indole to anthranilic acid. It is optimally active at pH 5.2 and 30 degrees C. Two moles of oxygen are consumed and one mole of anthranilic acid is ... >> More
A new indole oxygenase from the leaves of Tecoma stans was isolated and purified to homogenity. The purified enzyme system catalyzes the conversion of indole to anthranilic acid. It is optimally active at pH 5.2 and 30 degrees C. Two moles of oxygen are consumed and one mole of anthranilic acid is formed for every mole of indole oxidized. Dialysis resulted in complete loss of the activity. The inactive enzyme could be reactivated by the addition of concentrated dialysate. The enzyme is not inhibited by copper-specific chelators, non-heme iron chelators or atebrin. It is not a cuproflavoprotein, unlike the other indole oxygenases and oxidases. << Less
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Detection of an indole oxidizing system in maize leaves.
Chauhan Y.S., Rathore V.S., Garg G.K., Bhargava A.
Biochem Biophys Res Commun 83:1237-1245(1978) [PubMed] [EuropePMC]