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Ligand crotonaldehyde

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

crotyl alcohol + NAD+ = crotonaldehyde + NADH

0

-

Substrate in Enzyme-catalyzed Reactions (40 results)

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Show Substrate (40 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

(2E)-but-2-enal + NADPH + H+ = (2E)-but-2-en-1-ol + NADP+

735498

-

1.1.1.184

crotonaldehyde + NADPH = 2-buten-1-ol + NADP+

347750

-

1.1.1.21

trans-2-buten-1-al + NADPH + H+ = ?

695881

-

1.1.1.283

crotonaldehyde + NADPH = (2Z)-but-2-en-1-ol + NADP+

670170

-

1.1.1.90

crotonaldehyde + NADPH + H+ = crotonyl alcohol + NADP+

735498

-

1.1.1.91

crotonaldehyde + NADPH + H+ = crotonyl alcohol + NADP+

735498

-

1.2.1.22

crotonaldehyde + NAD+ + H2O = crotonate + NADH

674270

-

1.2.1.3

crotonaldehyde + NAD+ + H2O = crotonate + NADH

348682

1o01, 3D-view

1.2.1.32

crotonaldehyde + NAD+ + H2O = crotonate + NADH

390254

-

1.2.1.4

crotonaldehyde + NADP+ + H2O = crotonate + NADPH + H+

712174

-

1.2.1.4

crotonaldehyde + NADP+ = crotonate + NADPH

437834

-

1.2.1.4

2 entries

1.2.1.48

crotonaldehyde + NAD+ + H2O = crotonic acid + NADH

390324

-

1.2.3.1

crotonaldehyde + H2O + O2 = crotonate + H2O2

763618, 654321

-

1.2.3.1

crotonaldehyde + H2O + O2 = crotonic acid + H2O2

390387, 656311

-

1.2.7.5

crotonaldehyde + CoA + 2 oxidized ferredoxin = crotonate + CO2 + 2 reduced ferredoxin + 2 H+

721578

-

1.2.7.5

crotonaldehyde + H2O + 2 NAD+ = crotonate + 2 NADH + 2 H+

763075

-

1.2.7.5

crotonaldehyde + H2O + 2 oxidized benzyl viologen = crotonate + 2 H+ + 2 reduced benzyl viologen

763075

-

1.2.7.5

crotonaldehyde + H2O + oxidized benzyl viologen = crotonate + H+ + reduced benzyl viologen

644691, 11935, 722490, 644689, 740626

-

1.2.7.5

crotonaldehyde + H2O + oxidized benzyl viologen = crotonate + reduced benzyl viologen

656293

-

1.2.7.5

crotonaldehyde + H2O + oxidized benzyl viologen = crotonate + reduced benzyl viologen + H+

745202

-

1.2.7.5

crotonaldehyde + H2O + oxidized ferredoxin = crotonate + H+ + reduced ferredoxin

11935, 11938

-

1.2.7.5

crotonaldehyde + H2O + oxidized ferredoxin = crotonate + reduced ferredoxin

722057, 656293

-

1.2.7.5

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + H+ + reduced methyl viologen

674251, 11938

-

1.2.7.5

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + reduced methyl viologen + H+

745210

-

1.2.3.1

2 entries

1.2.7.5

10 entries

1.2.7.B2

crotonaldehyde + H2O + oxidized methyl viologen = crotonate + reduced methyl viologen + H+

674251

-

1.2.98.1

formaldehyde + H2O + crotonaldehyde = formate + crotonyl alcohol

390487, 390491

-

1.2.99.6

crotonaldehyde + benzyl viologen = crotonic acid + reduced benzyl viologen

655482

-

1.2.99.6

Crotonaldehyde + benzyl viologen = E-2-Butenoate + reduced benzyl viologen

11935

-

1.2.99.6

Crotonaldehyde + ES-1 ferredoxin = Crotonate + reduced ES-1 ferredoxin

11935

-

1.2.99.6

Crotonaldehyde + methyl viologen = Crotonate + reduced methyl viologen

11938, 11935

-

1.2.99.6

4 entries

1.3.1.27

trans-2-butenal + NAD(P)H = butanal + NAD(P)+

390627

-

1.3.1.48

trans-2-butenal + NAD(P)H = butanal + NAD(P)+

390826, 390830

-

1.3.1.74

crotonaldehyde + NADH = butanal + NAD+

725462

-

1.3.1.74

crotonaldehyde + NADPH = butanal + NADP+

725462

-

1.3.1.74

2 entries

2.5.1.18

glutathione + crotonaldehyde = ?

759263

-

4.1.2.45

crotonaldehyde + pyruvate = (3E,5E)-2-oxohepta-3,5-dienoate + H2O

695728

-

4.1.2.46

cyanide + crotonaldehyde = (2R)-2-hydroxy-3-pentenenitrile

5143, 706342

-

4.1.2.47

cyanide + (2E)-but-2-enal = (3E)-2-hydroxypent-3-enenitrile

706800

-

4.1.2.47

cyanide + (2E)-but-2-enal = (3S,3E)-2-hydroxypent-3-enenitrile

5153

-

4.1.2.47

HCN + (E)-2-butenal = (3E)-2-hydroxypent-3-enenitrile

650926

-

4.1.2.47

3 entries

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

(2E)-but-2-en-1-ol + NADP+ = (2E)-but-2-enal + NADPH + H+

0

-

1.1.1.1

crotyl alcohol + NAD+ = crotonaldehyde + NADH

0

-

1.1.1.1

2 entries

1.1.1.165

2-butene-1-ol + NAD+ = 2-butene-1-al + NADH

286099

-

1.1.1.54

2-buten-2-ol + NADPH = but-2-enal

0

-

1.1.1.71

cis-2-butenol + NAD(P)H = trans-2-butenal + NAD(P)+

287280

-

1.1.1.90

crotonyl alcohol + NADP+ = crotonaldehyde + NADPH + H+

0

-

1.1.1.91

crotonyl alcohol + NADP+ = crotonaldehyde + NADPH + H+

0

-

1.1.3.13

crotyl alcohol + O2 = (2E)-but-2-enal + H2O2

0

-

1.14.18.3

trans-2-butene + duroquinol + O2 = trans-2,3-epoxybutane + trans-2-butane-1-al + duroquinone + H2O

0

-

4.99.1.2

crotonyl mercuric bromide + H+ = crotonaldehyde + Hg2+ + Br-

0

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.7.5

50% inhibition at 20 mM

11935

-

1.2.7.5

substrate inhibition above 0.2 mM

11938

-

1.2.7.5

2 entries

1.2.7.6

25% inhibition at 10 mM

644692

-

1.2.99.6

above 0.2 mM

11938

-

3.1.3.48

85% remaining activity at 0.5 mM

679201

-

4.1.2.4

the enzyme produces crotonaldehyde as side reaction from acetaldehyde which is then an irreversible inhibitor forming a covalent Michael-adduct within the active site in particular with cysteine 47

748275

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

1.2.1.3

1o01, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (14 results)

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Show Turnover Number (14 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

405

-

pH 6.5, 65°C

735498

1.1.1.21

0.78

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

1.1.1.91

405

-

at pH 8.0 and 55°C

735498

1.2.3.1

1.22

-

wild-type, pH 8.0, 37°C

763618

1.2.3.1

2.11

-

pH 8, 37°C

763618

1.2.3.1

7.76

-

pH 8, 37°C

763618

1.2.3.1

8.32

-

pH 8, 37°C

763618

1.2.7.5

22

-

pH 8.4, 45°C, benzyl viologen as electron acceptor

11935

1.2.7.5

269

-

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

11935

1.2.99.6

22

-

with benzyl viologen as cosubstrate, at 45°C

11935

1.2.99.6

269

-

with benzyl viologen as cosubstrate, at 85°C

11935

1.2.3.1

4 entries

1.2.7.5

2 entries

1.2.99.6

2 entries

1.3.1.48

8.05

-

-

390830

1.3.1.74

1.3

-

pH 7.0, 25°C

725462

1.3.1.74

42

-

pH 7.0, 25°C

725462

1.3.1.74

2 entries

K_M Value (21 results)

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Show KM Value (21 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.1

3.3

-

pH 6.5, 65°C

735498

1.1.1.184

0.12

-

cofactor NADPH

347750

1.1.1.184

250

-

cofactor NADH

347750

1.1.1.184

2 entries

1.1.1.21

0.25

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

1.1.1.91

3.3

-

at pH 8.0 and 55°C

735498

1.2.1.3

0.032

-

-

348682

1.2.1.48

0.8

-

-

390324

1.2.3.1

0.0148

-

wild-type, pH 8.0, 37°C

763618

1.2.3.1

0.0848

-

pH 8, 37°C

763618

1.2.3.1

0.3806

-

pH 8, 37°C

763618

1.2.3.1

1.647

-

pH 8, 37°C

763618

1.2.7.5

0.04

-

pH 8.4, 80°C, with methyl viologen as electron acceptor

11938

1.2.7.5

0.13

-

pH 8.4, 45°C, benzyl viologen as electron acceptor

11935

1.2.7.5

0.14

-

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

11935, 644691

1.2.7.5

0.3

-

pH 8.4, 60°C

656293

1.2.99.6

0.04

-

-

11938

1.2.99.6

0.13

-

with benzyl viologen as cosubstrate, at 45°C

11935

1.2.99.6

0.136

-

with benzyl viologen as cosubstrate, at 85°C

11935

1.2.3.1

4 entries

1.2.7.5

4 entries

1.2.99.6

3 entries

1.3.1.48

3.9

-

-

390830

1.3.1.74

1.8

-

pH 7.0, 25°C

725462

1.3.1.74

29.8

-

pH 7.0, 25°C

725462

1.3.1.74

2 entries

References & Links

Literature References (46)

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Show Reference (46 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5143

8387315

Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range

1993

Albrecht, J.; Jansen, I.; Kula, M.R.

Biotechnol. Appl. Biochem.

17

191-203

5153

-

The first recombinent hydroxynitrile lyase in the synthesis of (S)-cyanohydrins

1996

Foerster, S.; Roos, J.; Effenberger, F.; Wajant, H.; Sprauer, A.

Angew. Chem. Int. Ed. Engl.

35

437-439

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

11938

1907273

The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

1991

Mukund, S.; Adams, M.W.W.

J. Biol. Chem.

266

14208-14216

286099

-

Purification and characterization of 2-alkyne-1-ol dehydrogenase induced by 2-butyne-1,4-diol in Fusarium merismoides B11

1974

Miyoshi, T.; Sato, H.; Harada, T.

Biochim. Biophys. Acta

358

231-239

287280

-

Purification and properties of alcohol dehydrogenase from Leuconostoc mesenteroides

1974

Hatanaka, A.; Kajiwara, T.; Tomohiro, S.

Agric. Biol. Chem.

38

1819-1833

347750

6753749

Purification and characterization of a novel pyrazole-sensitive carbonyl reductase in guinea pig lung

1982

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

Arch. Biochem. Biophys.

217

564-573

348682

10852

Localization and characteristics of rat liver mitochondrial aldehyde dehydrogenases

1976

Siew, C.; Deitrich, R.A.

Arch. Biochem. Biophys.

176

638-649

390254

9721300

Purification, characterization, and sequence analysis of 2-aminomuconic 6-semialdehyde dehydrogenase from Pseudomonas pseudoalcaligenes JS45

1998

He, Z.; Davis, J.K.; Spain, J.C.

J. Bacteriol.

180

4591-4595

390324

9133646

Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization

1997

Kelson, T.L.; Secor McVoy, J.R.; Rizzo, W.B.

Biochim. Biophys. Acta

1335

99-110

390387

-

Purification and properties of bovine liver aldehyde oxidase: comparison with xanthine oxidase

1987

Cabre, F.; Canela, E.I.

Biochem. Soc. Trans.

15

882-883

390487

-

Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61

1984

Kato, N.; Kobayashi, H.; Shimano, M.; Sakazawa, C.

Agric. Biol. Chem.

48

2017-2023

390491

-

The dismutation of aldehydes by a bacterial enzyme

1983

Kato, N.; Shirakawa, K.; Kobayashi, H.; Sakazawa, C.

Agric. Biol. Chem.

47

39-46

390627

-

Purification and some properties of 2-alkenal reductase of Muco griseo-cyanus AHU6044

1984

Miyamaura, N.; Matsui, H.; Tahara, S.; Mizutani, J.; Chiba, S.

Agric. Biol. Chem.

48

185-192

390826

7693121

Purification of a 15-ketoprostaglandin DELTA13-reductase from rat liver and its ability to reduce the double bond of xenobiotics

1993

Kitamura, S.; Katsura, H.; Tatsumi, K.

Biochem. Mol. Biol. Int.

30

839-847

390830

11524419

Antioxidative function and substrate specificity of NAD(P)H-dependent alkenal/one oxidoreductase. A new role for leukotriene B4 12-hydroxydehydrogenase/15-oxoprostaglandin 13-reductase

2001

Dick, R.A.; Kwak, M.K.; Sutter, T.R.; Kensler, T.W.

J. Biol. Chem.

276

40803-40810

437834

-

Purification and properties of five NADP-dependent aldehyde dehydrogenases from Acetobacter aceti

1980

Muraoka, H.; Watabe, Y.; Ogasawara, N.; Takahashi, H.

J. Ferment. Technol.

58

501-507

644689

9973343

Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus: the third of a putative five-member tungstoenzyme family

1999

Roy, R.; Mukund, S.; Schut, G.J.; Dunn, D.M.; Weiss, R.; Adams, M.W.

J. Bacteriol.

181

1171-1180

644691

11265456

Aldehyde oxidoreductases from Pyrococcus furiosus

2001

Roy, R.; Menon, A.L.; Adams, M.W.W.

Methods Enzymol.

331

132-144

644692

7721730

Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus

1995

Mukund, S.; Adams, M.W.

J. Biol. Chem.

270

8389-8392

650926

11102786

Hydroxynitrile lyases in stereoselective catalysis

2000

Effenberger, F.; Foerster, S.; Wajant, H.

Curr. Opin. Biotechnol.

11

532-539

654321

15657722

Characterization and potential application of purified aldehyde oxidase from Pseudomonas stutzeri IFO12695

2005

Uchida, H.; Fukuda, T.; Satoh, Y.; Okamura, Y.; Toriyama, A.; Yamashita, A.; Aisaka, K.; Sakurai, T.; Nagaosa, Y.; Uwajima, T.

Appl. Microbiol. Biotechnol.

68

53-56

655482

14686934

Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum. Isolation, characterization and molecular analysis

2004

Rauh, D.; Graentzdoerffer, A.; Granderath, K.; Andreesen, J.R.; Pich, A.

Eur. J. Biochem.

271

212-219

656293

15772818

Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum

2005

Hagedoorn, P.L.; Chen, T.; Schroder, I.; Piersma, S.R.; Vries, S.D.; Hagen, W.R.

J. Biol. Inorg. Chem.

10

259-269

656311

16233281

Production of aldehyde oxidases by microorganisms and their enzymatic properties

2002

Yasuhara, A.; Akiba-Goto, M.; Fujishiro, K.; Uchida, H.; Uwajima, T.; Aisaka, K.

J. Biosci. Bioeng.

94

124-129

670170

16804176

Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002

2006

Xu, D.; Liu, X.; Guo, C.; Zhao, J.

Microbiology

152

2013-2021

674251

16199576

WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate specificity

2005

Bevers, L.E.; Bol, E.; Hagedoorn, P.L.; Hagen, W.R.

J. Bacteriol.

187

7056-7061

674270

16585745

Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis

2006

Grochowski, L.L.; Xu, H.; White, R.H.

J. Bacteriol.

188

2836-2844

679201

17655273

Kinetics and mechanism of protein tyrosine phosphatase 1B inactivation by acrolein

2007

Seiner, D.R.; LaButti, J.N.; Gates, K.S.

Chem. Res. Toxicol.

20

1315-1320

695728

10831455

trans-o-Hydroxybenzylidenepyruvate hydratase-aldolase as a biocatalyst

2000

Eaton, R.W.

Appl. Environ. Microbiol.

66

2668-2672

695881

19464995

Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids

2009

Endo, S.; Matsunaga, T.; Mamiya, H.; Ohta, C.; Soda, M.; Kitade, Y.; Tajima, K.; Zhao, H.T.; El-Kabbani, O.; Hara, A.

Arch. Biochem. Biophys.

487

1-9

706342

-

Expression of the Zn2+-containing hydroxynitrile lyase from flax (Linum usitatissimum) in Pichia pastoris - utilization of the recombinant enzyme for enzymatic analysis and site-directed mutagenesis

1998

Trummler, K.; Roos, J.; Schwaneberg, U.; Effenberger, F.; Förster, S.; Pfizenmaier, K.; Wajant, H.

Plant Sci.

139

19-27

706800

-

Synthesis of alpha,beta-unsaturated (S)-cyanohydrins using the oxynitrilase from Hevea brasiliensis

1995

Klempier, N.; Pichler, U.; Griengl, H.

Tetrahedron Asymmetry

6

845-848

712174

20833259

Substrate profiling and aldehyde dismutase activity of the Kvbeta2 subunit of the mammalian Kv1 potassium channel

2010

Alka, K.; Ryan, B.J.; Dolly, J.O.; Henehan, G.T.

Int. J. Biochem. Cell Biol.

42

2012-2018

721578

9283079

Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions

1997

Zhou, Z.H.; Adams, M.W.

Biochemistry

36

10892-10900

722057

-

Redox chemistry of biological tungsten: an EPR study of the aldehyde oxidoreductase from Pyrococcus furiosus

1996

Arendsen, A.F.; de Vocht, M.; Bulsink, Y.B.M.; Hagen, W.R.

Chemistry

1

292-296

722490

8550411

Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus

1996

Mukund, S.; Adams, M.W.

J. Bacteriol.

178

163-167

725462

21169366

NADPH-dependent reductases involved in the detoxification of reactive carbonyls in plants

2011

Yamauchi, Y.; Hasegawa, A.; Taninaka, A.; Mizutani, M.; Sugimoto, Y.

J. Biol. Chem.

286

6999-7009

735498

24509923

Characterization of an allylic/benzyl alcohol dehydrogenase from Yokenella sp. strain WZY002, an organism potentially useful for the synthesis of alpha,beta-unsaturated alcohols from allylic aldehydes and ketones

2014

Ying, X.; Wang, Y.; Xiong, B.; Wu, T.; Xie, L.; Yu, M.; Wang, Z.

Appl. Environ. Microbiol.

80

2399-2409

740626

24214948

Simultaneous involvement of a tungsten-containing aldehyde:ferredoxin oxidoreductase and a phenylacetaldehyde dehydrogenase in anaerobic phenylalanine metabolism

2014

Debnar-Daumler, C.; Seubert, A.; Schmitt, G.; Heider, J.

J. Bacteriol.

196

483-492

745202

11133967

Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus

2001

Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.

J. Bacteriol.

183

716-724

745210

20562313

Molybdenum incorporation in tungsten aldehyde oxidoreductase enzymes from Pyrococcus furiosus

2010

Sevcenco, A.; Bevers, L.; Pinkse, M.; Krijger, G.; Wolterbeek, H.; Verhaert, P.; Hagen, W.; Hagedoorn, P.

J. Bacteriol.

192

4143-4152

748275

28347769

Probing the acetaldehyde-sensitivity of 2-deoxy-ribose-5-phosphate aldolase (DERA) leads to resistant variants

2017

Bramski, J.; Dick, M.; Pietruszka, J.; Classen, T.

J. Biotechnol.

258

56-58

759263

31068955

Detoxification of reactive carbonyl species by glutathione transferase tau isozymes

2019

Mano, J.; Kanameda, S.; Kuramitsu, R.; Matsuura, N.; Yamauchi, Y.

Front. Plant Sci.

10

487

763075

30766522

Characterization of an aldehyde oxidoreductase from the mesophilic bacterium Aromatoleum aromaticum EbN1, a member of a new subfamily of tungsten-containing enzymes

2019

Arndt, F.; Schmitt, G.; Winiarska, A.; Saft, M.; Seubert, A.; Kahnt, J.; Heider, J.

Front. Microbiol.

10

71

763618

29370288

Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities

2018

Kuecuekgoeze, G.; Leimkuehler, S.

PLoS ONE

13

e0191819

Links to other databases for crotonaldehyde

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ChEBI

PubChem