Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline indole-3-ethanol Identifier CHEBI:17890 (Beilstein: 125553; CAS: 526-55-6) help_outline Charge 0 Formula C10H11NO InChIKeyhelp_outline MBBOMCVGYCRMEA-UHFFFAOYSA-N SMILEShelp_outline OCCc1c[nH]c2ccccc12 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,186 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline indole-3-acetaldehyde Identifier CHEBI:18086 (Beilstein: 121586; CAS: 2591-98-2) help_outline Charge 0 Formula C10H9NO InChIKeyhelp_outline WHOOUMGHGSPMGR-UHFFFAOYSA-N SMILEShelp_outline O=CCc1c[nH]c2ccccc12 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,116 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:14873 | RHEA:14874 | RHEA:14875 | RHEA:14876 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Indoleacetaldehyde Reductase of Cucumis sativus L: KINETIC PROPERTIES AND ROLE IN AUXIN BIOSYNTHESIS.
Brown H.M., Purves W.K.
Indoleacetaldehyde reductase catalyzes the conversion of indoleacetaldehyde to indole ethanol in extracts of Cucumis sativus L., with reduced pyridine nucleotide required as co-substrate. NADH and NADPH result in markedly different enzyme behavior, as reflected in reaction kinetics and in response ... >> More
Indoleacetaldehyde reductase catalyzes the conversion of indoleacetaldehyde to indole ethanol in extracts of Cucumis sativus L., with reduced pyridine nucleotide required as co-substrate. NADH and NADPH result in markedly different enzyme behavior, as reflected in reaction kinetics and in responses to inhibitors and activators. It is not yet clear whether there are two separate enzymes, one specific for NADH and the other for NADPH, or whether there is a single enzyme differentially influenced by the two co-substrates.In the presence of NADH, the indoleacetaldehyde reductase activity was inhibited by NaCl and displayed hyperbolic kinetics under all conditions tested. However, in the presence of NADPH the enzyme was activated by NaCl at concentrations up to 0.1 molar. Under certain conditions with NADPH as co-substrate, the enzyme showed kinetics sigmoidal with respect to indoleacetaldehyde concentration and was strongly inhibited by high concentrations of NADPH. It is possible that this substrate inhibition of the NADPH-linked indoleacetaldehyde reductase activity by NADPH, as well as the sigmoidicity with respect to indoleacetaldehyde concentration, may function in the regulation of auxin biosynthesis. << Less
Plant Physiol 65:107-113(1980) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.