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  • Metals and Ions
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• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
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  • K_i Value
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Ligand Indole-3-acetaldehyde

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for Indole-3-acetaldehyde

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.190

indole-3-acetaldehyde + NADH = indole-3-ethanol + NAD+

286151, 286153, 286152, 286154

-

1.1.1.191

indole-3-acetaldehyde + NADPH = indole-3-ethanol + NADP+

286157, 286158, 286152, 286154, 286153, 286155

-

1.2.3.7

indole-3-acetaldehyde + O2 + H2O = indole-3-acetate + H2O2

390443, 390441

-

1.2.3.7

indole-3-acetaldehyde + O2 = indole-3-acetate + H2O2

726191

-

1.2.3.7

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.21

tryptamine + H2O + O2 = (1H-indol-3-yl)acetaldehyde + NH3 + H2O2

-

-

1.4.3.4

tryptamine + H2O + O2 = (1H-indol-3-yl)acetaldehyde + NH3 + H2O2

-

-

1.4.3.4

tryptamine + H2O + O2 = 1-H-indol-3-yl-acetaldehyde + NH3 + H2O2

-

-

4.1.1.74

(indol-3-yl)pyruvate = (indole-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

3-(indol-3-yl)pyruvate = (indole-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2

-

-

1.4.3.4

2 entries

4.1.1.74

3 entries

Substrate in Enzyme-catalyzed Reactions (24 results)

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Show Substrate (24 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.184

indole 3-acetaldehyde + NADPH = indole-3-ol + NADP+

347749

-

1.1.1.190

indole-3-acetaldehyde + NADH = indole-3-ethanol + NAD+

286151, 286153, 286152, 286154

-

1.1.1.191

indole-3-acetaldehyde + NADPH = indole-3-ethanol + NADP+

286157, 286158, 286152, 286154, 286153, 286155

-

1.1.1.2

indol-3-ylacetaldehyde + NADPH = indol-3-ethanol + NADP+

286172, 286166, 286181, 286184

-

1.1.1.2

indolacetaldehyde + NADPH = ? + NADP+

286165, 286172

-

1.1.1.2

2 entries

1.1.1.21

indole-3-acetaldehyde + NAD(P)H = indole-3-ethanol + NAD(P)+

286240, 286241

-

1.13.99.3

3-indoleacetaldehyde + O2 = ?

439304

-

1.17.1.4

indole-3-acetaldehyde + NAD+ + H2O = indole-3-acetate + NADH + H+

660263

-

1.17.3.2

indole-3-acetaldehyde + H2O + O2 = ?

644655

-

1.2.1.3

indole-3-acetaldehyde + NAD+ + H2O = indole-3-acetate + NADH + H+

348694, 348705, 348699

-

1.2.1.39

indoleacetaldehyde + NAD+ + H2O = indoleacetate + NADH

390292

-

1.2.1.5

indole-3-acetaldehyde + NAD+ + H2O = indole-3-acetate + NADH + H+

348781

-

1.2.1.88

indole-3-acetaldehyde + NAD+ + H2O = indole-3-acetate + NADH + H+

392065

-

1.2.3.1

indole 3-acetaldehyde + H2O + O2 = indole 3-acetic acid + H2O2

390381, 700829

-

1.2.3.7

indole-3-acetaldehyde + O2 + H2O = indole-3-acetate + H2O2

390440, 390442, 390443, 390441, 390439

-

1.2.3.7

indole-3-acetaldehyde + O2 = indole-3-acetate + H2O2

726191

-

1.2.3.7

indole-3-acetaldehyde + oxidized 2,6-dichloroindophenol + H2O = indole-3-acetate + reduced 2,6-dichloroindophenol

726191

-

1.2.3.7

indole-3-acetaldehyde + phenazine methosulfate = indole-3-acetate + ?

390441

-

1.2.3.7

4 entries

1.2.7.5

indoleacetaldehyde + H2O + oxidized benzyl viologen = indoleacetate + H+ + reduced benzyl viologen

644691, 11935

-

1.2.7.B2

indole-3-acetaldehyde + H2O + oxidized benzyl viologen = indole-3-acetate + H+ + reduced benzyl viologen

644691

-

1.2.7.B2

indole-3-acetaldehyde + H2O + oxidized benzyl viologen = indole-3-acetate + reduced benzyl viologen + H+

644689

-

1.2.7.B2

2 entries

1.2.99.6

Indoleacetaldehyde + benzyl viologen = Indoleacetate + reduced benzyl viologen

11939, 11935

-

1.2.99.8

indoleacetaldehyde + 2,6-dichlorophenolindophenol + H2O = indoleacetate + reduced 2,6-dichlorophenolindophenol

741251

-

4.1.1.74

indole-3-acetaldehyde = ?

651291

-

Product in Enzyme-catalyzed Reactions (22 results)

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Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.10

tryptamine + O2 + H2O = 1H-indol-3-yl-acetaldehyde + NH3 + H2O2

-

-

1.4.3.21

tryptamine + H2O + O2 = (1H-indol-3-yl)acetaldehyde + NH3 + H2O2

-

-

1.4.3.21

tyramine + H2O + O2 = (1H-indol-3-yl)acetaldehyde + NH3 + H2O2

-

-

1.4.3.21

tryptamine + H2O + O2 = 1H-indol-3-ylacetaldehyde + NH3 + H2O2

-

-

1.4.3.22

tryptamine + H2O + O2 = 1H-indol-3-ylacetaldehyde + NH3 + H2O2

-

-

1.4.3.22

tyramine + H2O + O2 = 1H-indol-3-ylacetaldehyde + NH3 + H2O2

-

-

1.4.3.22

tyramine + O2 + H2O = 1H-indol-3-ylacetaldehyde + NH3 + H2O2

-

-

1.4.3.4

tryptamine + H2O + O2 = (1H-indol-3-yl)acetaldehyde + NH3 + H2O2

-

-

1.4.3.4

tryptamine + H2O + O2 = 1-H-indol-3-yl-acetaldehyde + NH3 + H2O2

-

-

1.4.3.4

tryptamine + H2O + O2 = 1H-indol-3-yl-acetaldehyde + NH3 + H2O2

394560, 394557, 394548, 394580

-

1.4.3.21

3 entries

1.4.3.22

3 entries

1.4.3.4

3 entries

1.4.9.2

tryptamine + acceptor + H2O = 1H-indole-3-acetaldehyde + NH3 + reduced acceptor

-

-

4.1.1.1

3-(1H-indol-3-yl)-2-oxopropanoic acid = 1H-indol-3-ylacetaldehyde + CO2

-

-

4.1.1.1

indole-3-pyruvate = 2-(indol-3-yl)-ethanal + CO2

-

-

4.1.1.43

indole-3-pyruvate = indoleacetaldehyde + CO2

-

-

4.1.1.43

indolepyruvate = indoleacetaldehyde + CO2

-

-

4.1.1.43

Indolepyruvate = Indoleethanal + CO2

-

-

4.1.1.1

2 entries

4.1.1.43

3 entries

4.1.1.72

(indol-3-yl)pyruvate = (indol-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

(indol-3-yl)pyruvate = (indole-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

(indole-3-yl)pyruvate = (indole-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

3-(indol-3-yl)pyruvate = (indole-3-yl)acetaldehyde + CO2

-

-

4.1.1.74

3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2

651152, , 651291

-

4.1.1.74

3-(Indol-3-yl)pyruvate = Indole-3-acetaldehyde + CO2

4826, 4827, 4824, 4823, 4825

-

4.1.1.74

5 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.12.3

weak

439341

-

1.2.1.3

substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition

348704

-

4.1.1.28

-

4203

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (9 results)

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Show Turnover Number (9 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.3

9.33

-

enzyme ALDH-2

348694

1.2.1.3

11.3

-

enzyme ALDH-1

348694

1.2.1.3

2 entries

1.2.3.1

1904

-

partially purified protein, pH 7.0, 30°C

700829

1.2.7.5

55

-

pH 8.4, 85°C, benzyl viologen as electron acceptor

11935

1.2.7.B2

2300

-

80°C, pH 8.4

644689

1.2.99.6

55

-

with benzyl viologen as cosubstrate, at 85°C

11935

1.2.99.8

2.77

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

3.46

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

3.58

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

3 entries

K_M Value (38 results)

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Show KM Value (38 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.190

0.4

-

-

286153

1.1.1.190

0.5

-

marked function of the NaCl concentration

286154

1.1.1.191

0.025

-

-

286155

1.1.1.191

0.067

-

at pH 7.0, isoenzyme TH

286153

1.1.1.191

0.125

-

-

286154, 286158

1.1.1.191

0.133

-

at pH 7.0, isoenzyme TL

286153

1.1.1.191

0.2

-

-

286157

1.1.1.191

0.2

-

at pH 5.2, isoenzyme TH

286153

1.1.1.191

0.25

-

at pH 5.2, isoenzyme TL

286153

1.1.1.2

0.0059

-

low-Km reductase

286166

1.1.1.2

0.2

-

high-Km aldehyde reductase

286166

1.1.1.2

0.32

-

AR2

286181

1.1.1.2

0.6

-

-

286172

1.1.1.2

3

-

AR3

286181

1.1.1.2

3.7

-

AR1

286184

1.1.1.190

2 entries

1.1.1.191

7 entries

1.1.1.2

6 entries

1.1.1.21

0.016

-

-

286241

1.17.3.2

0.3

-

-

644655

1.2.1.3

0.00015

-

enzyme ALDH-2

348694

1.2.1.3

0.00031

-

enzyme ALDH-1

348694

1.2.1.3

0.0007

-

isoenzyme I

348705

1.2.1.3

0.001

-

isoenzyme III

348705

1.2.1.3

0.002

-

-

348699

1.2.1.3

5 entries

1.2.1.5

0.5

-

reaction with NAD+

348781

1.2.1.88

0.2

-

isoform A

392065

1.2.3.1

0.0032

-

O2 as electron acceptor

390381

1.2.3.1

0.005

-

2,6-dichlorophenol-indophenol as electron acceptor

390381

1.2.3.1

2.07

-

partially purified protein, pH 7.0, 30°C

700829

1.2.3.7

0.345

-

-

390441

1.2.3.7

1.4

-

-

390440

1.2.7.5

0.05

-

pH 8.4, 85°C, benzyl viologen as electron acceptor

11935, 644691

1.2.7.5

25

-

pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor

644691

1.2.3.1

3 entries

1.2.3.7

2 entries

1.2.7.5

2 entries

1.2.7.B2

25

-

80°C, pH 8.4

644689, 644691

1.2.99.6

0.05

-

reduced carbamoyl methyl viologen, with benzoate as cosubstrate

11939

1.2.99.6

0.05

-

with benzyl viologen as cosubstrate, at 85°C

11935

1.2.99.8

0.037

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

0.092

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

0.113

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.6

2 entries

1.2.99.8

3 entries

4.1.1.74

0.009

-

70°C, pH 8.0

651291

References & Links

Literature References (51)

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Show Reference (51 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4203

-

Partial purification and some properties of tryptophan decarboxylase from Phalaris tuberosa

1972

Baxter, C.; Slaytor, M.

Phytochemistry

11

2763-2766

4823

9608743

Identification and isolation of the indole-3-pyruvate decarboxylase gene from Azospirillum brasilense Sp7: sequencing and functional analysis of the gene locus

1998

Zimmer, W.; Wesche, M.; Timmermans, L.

Curr. Microbiol.

36

327-331

4824

8900003

Cloning and characterization of a locus encoding an indolepyruvate decarboxylase involved in indole-3-acetic acid synthesis in Erwinia herbicola

1996

Brandl, M.T.; Lindow, S.E.

Appl. Environ. Microbiol.

62

4121-4128

4825

9973364

Auxins upregulate expression of the indole-3-pyruvate decarboxylase gene in Azospirillum brasilense

1999

vande Broek, A.; Lambrecht, M.; Eggermont, K.; Vanderleyden, J.

J. Bacteriol.

181

1338-1342

4826

1639814

Purification and characterization of indolepyruvate decarboxylase: A novel enzyme for indole-3-acetic acid biosynthesis in Enterobacter cloacae

1992

Koga, J.; Adachi, T.; Hidaka, H.

J. Biol. Chem.

267

15823-15828

4827

7766676

Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis

1995

Koga, J.

Biochim. Biophys. Acta

1249

1-13

11935

7642503

Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1

1995

Heider, J.; Ma, K.; Adams, M.W.W.

J. Bacteriol.

177

4757-4764

11939

-

Pterin cofactor, substrate specificity, and observations on the kinetics of the reversible tungsten-containing aldehyde oxidoreductase from Clostridium thermoaceticum

1995

Huber, C.; Skopan, H.; Feicht, R.; White, H.; Simon, H.

Arch. Microbiol.

164

110-118

286151

16660376

Indole-3-acetic acid synthesis in tumorous and nontumorous species of Nicotiana

1978

Liu, S.T.; Katz, C.D.; Knight, C.A.

Plant Physiol.

61

743-747

286152

16659584

Auxin biogenesis. Subcellular compartimentation of indoleacetaldehyde reductases in cucumber seedlings

1976

Bower, P.J.; Brown, H.M.; Purves, W.K.

Plant Physiol.

57

850-854

286153

2607

Isolation and characterization of indole-3-acetaldehyde reductases from Cucumis sativus

1976

Brown, H.M.; Purves, W.K.

J. Biol. Chem.

251

907-913

286154

16661122

Indoleacetaldehyde reductase of Cucumis sativus L. Kinetic properties and role in auxin biosynthesis

1980

Brown, H.M.; Purves, W.K.

Plant Physiol.

65

107-113

286155

-

Purification of NADPH-specific indole-3-acetaldehyde reductase from Cucumis sativus by two-dimensional native polyacrylamide gel electrophoresis

1989

Ludwig-Muller, J.; Hilgenberg, W.

Physiol. Plant.

77

613-619

286157

-

Indole-3-acetaldehyde reductase in Phycomyces blakesleeanus. Characterization of the enzyme

1990

Ludwig-Muller, J.; Schramm, P.; Hilgenberg, W.

Physiol. Plant.

80

472-478

286158

-

Identification of indole-3-acetaldehyde and indole-3-acetaldehyde reductase in Chinese cabbage

1990

Ludwig-Muller, J.; Hilgenberg, W.

Physiol. Plant.

80

541-548

286165

4402936

Triphosphopyridine nucleotide-linked aldehyde reductase I. Purification and properties of the enzyme from pig kidney cortex

1972

Bosron, W.F.; Prairie, R.L.

J. Biol. Chem.

217

4480-4485

286166

4146452

The characterization of two reduced nicotinamide-adenine dinucleotide phosphate-linked aldehyde reductases from pig brain

1972

Turner, A.J.; Tipton, K.F.

Biochem. J.

130

765-772

286172

6989609

Purification and some properties of aldehyde reductases from pig liver

1980

Branlant, G.M; Biellmann, J.F.

Eur. J. Biochem.

105

611-621

286181

6753936

Purification and properties of human liver aldehyde reductases

1982

Petrash, J.M.; Srivastava, S.K.

Biochim. Biophys. Acta

707

105-114

286184

6343086

Isolation and characterization of multiforms of aldehyde reductase in chicken kidney

1983

Hara, A.; Deyashiki, Y.; Nakayama, T.; Sawada, H.

Eur. J. Biochem.

133

207-214

286240

6815419

Aldose reductase from human tissues

1982

Wermuth, B.; von Wartburg, J.P.

Methods Enzymol.

89

181-186

286241

6814912

Purification and characterization of human-brain aldose reductase

1982

Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.

Eur. J. Biochem.

127

279-284

347749

7005231

Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase

1981

Wermuth, B.

J. Biol. Chem.

256

1206-1213

348694

8605195

Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes

1996

Klyosov, A.A.

Biochemistry

35

4457-4467

348699

2753207

Aldehyde dehydrogenase: kinetics and mechanism

1989

Dickinson, F.M.

Biochem. Soc. Trans.

17

299-300

348704

-

Steady-state kinetics of aldehyde by pig liver cytosolic aldehyde dehydrogenase

1988

Hill, J.P.; Dickinson, F.M.

Biochem. Soc. Trans.

16

857-858

348705

3592683

Purification and characterization of aldehyde dehydrogenase from human brain

1987

Ryzlak, M.T.; Pietruszko, R.

Arch. Biochem. Biophys.

255

409-418

348781

-

Purification and characterization of the bovine cerebral mitochondrial aldehyde dehydrogenase

1991

Choi, S.D.; Joo, C.N.

Korean Biochem. J.

24

224-230

390292

-

Metabolism of phenylalanine (Achromobacter eurydice)

1970

Fujioka, M.; Morino, Y.; Wada, H.

Methods Enzymol.

17A

585-596

390381

12226218

Purification and properties of flavin- and molybdenum-containing aldehyde oxidase from coleoptiles of maize

1996

Koshiba, T.; Saito, E.; Ono, N.; Yamamoto, N.; Sato, M.

Plant Physiol.

110

781-789

390439

16660220

Cucumber seedlings indoleacetaldehyde oxidase

1978

Bower, P.J.; Brown, H.M.; Purves, W.K.

Plant Physiol.

61

107-110

390440

-

Indole-3-acetyldehyde oxidase of pea seedlings

1981

Miyata, S.; Suzuki, Y.; Kamisaka, S.; Masuda, Y.

Physiol. Plant.

51

402-406

390441

-

Metabolism of indole-3-acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles

1971

Rajagopal, R.

Physiol. Plant.

24

272-281

390442

12231908

An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts

1993

Koshiba, T.; Matsuyama, H.

Plant Physiol.

102

1319-1324

390443

9489015

Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana

1998

Seo, M.; Akaba, S.; Oritani, T.; Delarue, M.; Bellini, C.; Caboche, M.; Koshiba, T.

Plant Physiol.

116

687-693

392065

9418013

Enzymes of DELTA1-pyrroline-5-carboxylate metabolism in the camel tick Hyalomma dromedarii during embryogenesis. Purification and characterization of DELTA1-pyrroline-5-carboxylate dehydrogenases

1997

Fahmy, A.S.; Mohamed, S.A.; Girgis, R.B.; Abdel-Ghaffar, F.A.

Comp. Biochem. Physiol. B

118

229-237

394548

6061707

Mitochondrial monoamine oxidase. I. Purification and characterization of the bovine kidney enzyme

1967

Erwin, V.G.; Hellerman, L.

J. Biol. Chem.

242

4230-4238

394557

5165518

Purification and properties of pig liver mitochondrial monoamine oxidase

1971

Oreland, L.

Arch. Biochem. Biophys.

146

410-412

394560

4357526

Rapid screening assay for revertants derived from MSV-transformed cells

1973

Tipton, M.F.; Houslay, M.D.; Garrett, N.J.

Nature

246

213-214

394580

434814

Monoamine oxidase from beef liver mitochondria: simplified isolation procedure, properties, and determination of its cysteinyl flavin content

1979

Salach, J.I.

Arch. Biochem. Biophys.

192

128-137

439304

3037258

Purification and properties of tryptophan side chain oxidase types I and II from Pseudomonas

1987

Takai, K.; Hayaishi, O.

Methods Enzymol.

142

195-217

439341

5916389

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Links to other databases for Indole-3-acetaldehyde

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ChEBI

PubChem

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