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The enzyme appears in viruses and cellular organisms
Synonyms
indoleacetaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase, more
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indoleacetaldehyde (reduced nicotinamide adenine dinucleotide phosphate) reductase
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(indol-3-yl)ethanol + NADP+ = (indol-3-yl)acetaldehyde + NADPH + H+
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MetaCyc
L-tryptophan degradation X (mammalian, via tryptamine)
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(indol-3-yl)ethanol:NADP+ oxidoreductase
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acetaldehyde + NADPH + H+
ethanol + NADP+
benzaldehyde + NADPH
benzyl alcohol + NADP+
butyraldehyde + NADPH
butanol + NADP+
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Substrates: low activity
Products: -
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dihydroxyacetonephosphate + NADPH
glycerol 1-phosphate + NADP+
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Substrates: well accepted substrate
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
indole-3-aldehyde + NADPH
indole-3-ol + NADP+
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Substrates: 19% of the activity of indole-3-acetaldehyde
Products: -
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phenylacetaldehyde + NADPH + H+
phenylethanol + NADP+
phenylacetone + NADPH
phenylethanol + NADP+
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Substrates: low activity
Products: -
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propionaldehyde + NADPH
propanol + NADP+
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Substrates: very low activity only for isoenzyme TL
Products: -
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trans-cinnamaldehyde + NADPH
(2E)-3-phenylprop-2-en-1-ol + NADP+
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Substrates: very low activity
Products: -
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acetaldehyde + NADPH + H+

ethanol + NADP+
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Substrates: 5fold higher activity than for indole-3-acetaldehyde
Products: -
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acetaldehyde + NADPH + H+
ethanol + NADP+
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Substrates: very low activity only for isoenzyme TH
Products: -
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acetaldehyde + NADPH + H+
ethanol + NADP+
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Substrates: very low activity
Products: -
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benzaldehyde + NADPH

benzyl alcohol + NADP+
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Substrates: 65% of the activity compared to indole-3-acetaldehyde
Products: -
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benzaldehyde + NADPH
benzyl alcohol + NADP+
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Substrates: 2.5fold higher activity than for indole-3-acetaldehyde
Products: -
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indole-3-acetaldehyde + NADPH

indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: substrates hold key positions in the regulation of indole-3-acetic acid content in higher plants
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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phenylacetaldehyde + NADPH + H+

phenylethanol + NADP+
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Substrates: 2.4fold higher activity than for indole-3-acetaldehyde
Products: -
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phenylacetaldehyde + NADPH + H+
phenylethanol + NADP+
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Substrates: well accepted substrate
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
indole-3-acetaldehyde + NADPH

indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
ir
indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: substrates hold key positions in the regulation of indole-3-acetic acid content in higher plants
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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indole-3-acetaldehyde + NADPH
indole-3-ethanol + NADP+
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Substrates: -
Products: -
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NADP+

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NADP+
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with NAD+ 10times lower activity
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Ca2+
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29% activation at 2 mM
Fe3+
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22% activation at 0.1 mM
Mg2+
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29% activation at 2 mM
Mn2+
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39% activation at 2 mM
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Cd2+
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complete inhibition at 2 mM
dihydroxyacetonephosphate
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non-competitive inhibition, Ki: 0.35 mM
EDTA
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40% inhibition at 1 mM
indole-3-acetic acid
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inhibitory above 0.05 mM
Indole-3-aldehyde
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slight inhibition at 0.2 mM
indole-3-glycolate
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62% inhibition at 0.2 mM
KCN
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73% inhibition at 1 mM
KI
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23% inhibition at 1 mM
Mn2+
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46% inhibition at 1 mM
N-ethylmaleimide
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46% inhibition at 1 mM
NADP+
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non-competitive inhibition, half-maximal inhibition at 0.2 mM
NaF
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35% inhibition at 1 mM
NaN3
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slight inhibition at 1 mM
p-chloromercuribenzoate
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17% inhibition at 0.1 mM
p-chloromercuriphenylsulfonic acid
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46% inhibition at 0.1 mM
p-hydroxymercuribenzoate
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40% inhibition at 0.1 mM
tryptophan
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inhibition at low concentrations
Zn2+
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36% inhibition at 1 mM
Cu2+

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complete inhibition at 2 mM
Cu2+
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59% inhibition at 1 mM
Hg2+

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complete inhibition at 2 mM
Hg2+
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50% inhibition at 0.01 mM
iodoacetate

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33% inhibition at 0.1 mM
iodoacetate
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22% inhibition at 1 mM
NADPH

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inhibitory above 0.2 mM
NADPH
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inhibition at high concentrations
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hydroxymethylindole
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42% activation at 0.2 mM
indole-3-acetic acid
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activation up to 0.05 mM
indole-3-ethanol
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activation up to 0.1 mM
NaCl
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activation up to 0.1 M
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0.645
dihydroxyacetone phosphate
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0.025 - 0.25
Indole-3-acetaldehyde
0.5
phenylacetaldehyde
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0.025
Indole-3-acetaldehyde

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0.067
Indole-3-acetaldehyde
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at pH 7.0, isoenzyme TH
0.125
Indole-3-acetaldehyde
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0.125
Indole-3-acetaldehyde
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0.133
Indole-3-acetaldehyde
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at pH 7.0, isoenzyme TL
0.2
Indole-3-acetaldehyde
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0.2
Indole-3-acetaldehyde
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at pH 5.2, isoenzyme TH
0.25
Indole-3-acetaldehyde
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at pH 5.2, isoenzyme TL
0.011
NADPH

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0.002
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partial purified from seedlings
0.014
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partial purified from fruits
0.04
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cytosolic fraction
0.24
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purified from fruits
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5.2
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second pH optimum at pH 7.0
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brenda
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brenda
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brenda
chinese cabbage
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brenda
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brenda
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brenda
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brenda
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maximum enzyme activity from cultures after 48 h
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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two isoenzymes, TH and TL
brenda
Highest Expressing Human Cell Lines
Cell Line Links
Gene Links
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I3ACR_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
284
0
31570
Swiss-Prot
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17000
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isoenzyme TL, gel filtration
52000
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isoenzyme TH, gel filtration
32000

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gel filtration
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to homogeneity, chromatography steps, native PAGE
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partial

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Bower, P.J.; Brown, H.M.; Purves, W.K.
Auxin biogenesis. Subcellular compartimentation of indoleacetaldehyde reductases in cucumber seedlings
Plant Physiol.
57
850-854
1976
Cucumis sativus
brenda
Brown, H.M.; Purves, W.K.
Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus
J. Biol. Chem.
251
907-913
1976
Cucumis sativus
brenda
Brown, H.M.; Purves, W.K.
Indoleacetaldehyde reductase of Cucumis sativus L. Kinetic properties and role in auxin biosynthesis
Plant Physiol.
65
107-113
1980
Cucumis sativus
brenda
Ludwig-Muller, J.; Hilgenberg, W.
Purification of NADPH-specific indole-3-acetaldehyde reductase from Cucumis sativus by two-dimensional native polyacrylamide gel electrophoresis
Physiol. Plant.
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613-619
1989
Cucumis sativus
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brenda
Ludwig-Muller, J.; Schramm, P.; Hilgenberg, W.
Indole-3-acetaldehyde reductase in Phycomyces blakesleeanus. Characterization of the enzyme
Physiol. Plant.
80
472-478
1990
Phycomyces blakesleeanus
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brenda
Ludwig-Muller, J.; Hilgenberg, W.
Identification of indole-3-acetaldehyde and indole-3-acetaldehyde reductase in Chinese cabbage
Physiol. Plant.
80
541-548
1990
Arabidopsis thaliana, Brassica napus, Brassica oleracea, Brassica rapa subsp. pekinensis, Sinapis alba
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brenda
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