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Ligand an aldehyde

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

non-pathway related

KEGG

Fatty acid degradation

MetaCyc

2-aminoethylphosphonate degradation I, 2-deoxy-alpha-D-ribose 1-phosphate degradation, 2-deoxy-D-ribose degradation I, 2-hydroxypenta-2,4-dienoate degradation, 5'-deoxyadenosine degradation I, 5'-deoxyadenosine degradation II, acetaldehyde biosynthesis I, acetaldehyde biosynthesis II, acetoin degradation, acetylene degradation (anaerobic), alkylnitronates degradation, atrazine degradation II, ceramide degradation (generic), choline degradation III, cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion), cytosolic NADPH production (yeast), ethanol degradation I, ethanol degradation II, ethanol degradation III, ethanol degradation IV, ethanolamine utilization, fluoroacetate and fluorothreonine biosynthesis, geraniol and nerol degradation, glycine biosynthesis IV, heterolactic fermentation, homofuraneol biosynthesis, hypotaurine degradation, L-threonine degradation IV, long chain fatty acid ester synthesis (engineered), methylthiopropanoate degradation I (cleavage), mitochondrial NADPH production (yeast), mixed acid fermentation, nitroethane degradation, preQ0 biosynthesis, pyruvate fermentation to acetate VIII, pyruvate fermentation to acetoin III, pyruvate fermentation to ethanol I, pyruvate fermentation to ethanol II, pyruvate fermentation to ethanol III, sulfoacetaldehyde degradation IV, superpathway of fermentation (Chlamydomonas reinhardtii), triethylamine degradation, two-component alkanesulfonate monooxygenase more

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Natural Substrate (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

aldehyde + NADPH + H+ = alcohol + NADP+

684751

-

1.14.14.3

an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu

711341, 711486, 713371

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hn

657751, 657939, 658147, 657855

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hnu

689388

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hv

726677, 726679

-

1.14.14.3

4 entries

1.2.1.3

an aldehyde + NAD+ + H2O = an acid + NADH + H+

696996, 697280, 697845

-

1.2.1.4

an aldehyde + NADP+ + H2O = an acid + NADPH + H+

673477, 677193, 655889

-

1.2.1.5

an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+

671511

-

1.2.1.5

an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+

740294

-

1.2.1.5

an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+

740294

-

1.2.1.5

3 entries

1.2.7.5

an aldehyde + H2O + oxidized ferredoxin = an acid + H+ + reduced ferredoxin

11938, 644686, 644689, 644691, 11935

-

In Vivo Product in Enzyme-catalyzed Reactions (12 results)

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Show Natural Product (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

a primary alcohol + NAD+ = an aldehyde + NADH + H+

0

-

1.1.2.7

a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+

0

-

1.1.2.B3

alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550

0

-

1.14.14.5

an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O

0

-

1.14.14.5

an alkansulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O

0

-

1.14.14.5

R-CH2-SO3H + FMNH2 + O2 = R-CHO + FMN + sulfite + H2O

438770

-

1.14.14.5

3 entries

1.4.3.21

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

0

-

1.4.3.22

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391922

-

1.4.3.4

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

0, 394574, 394568, 394573

-

3.3.2.2

1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = aldehyde + sn-glycero-3-phosphocholine

137152, 137151, 137153, 137154, 137155, 137156, 137157

-

3.3.2.2

1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = aldehyde + sn-glycero-3-phosphoethanolamine

137154, 137155, 137157, 137160, 137161

-

3.3.2.2

2 entries

4.1.1.1

a 2-oxo acid = an aldehyde + CO2

0

-

Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Substrate (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

aldehyde + NADPH + H+ = alcohol + NADP+

684751

-

1.14.14.3

aldehyde + FMNH2 + O2 = ?

698992

-

1.14.14.3

an aldehyde + FMNH2 + O2 = a carboxylate + FMN + H2O + hnu

711341, 711486, 713371

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hn

657751, 657927, 657939, 657994, 658147, 657855, 657923, 658060

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hnu

689388, 726678

-

1.14.14.3

RCHO + FMNH2 + O2 = RCOOH + FMN + H2O + hv

726677, 726679, 728822, 728017

-

1.14.14.3

5 entries

1.17.3.2

aldehyde + indophenol = ?

644648

-

1.2.1.23

aldehydes + NAD+ + H2O = carboxylic acids + NADH

288137, 288139, 288138, 288140

-

1.2.1.3

an aldehyde + NAD+ + H2O = an acid + NADH + H+

696996, 697280, 697845

-

1.2.1.4

an aldehyde + NADP+ + H2O = an acid + NADPH + H+

673477, 677193, 655889

-

1.2.1.5

an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+

671511

-

1.2.1.5

an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+

740294

-

1.2.1.5

an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+

348781, 740294

-

1.2.1.5

3 entries

1.2.7.5

an aldehyde + H2O + oxidized ferredoxin = an acid + H+ + reduced ferredoxin

11938, 644686, 644689, 644687, 644688, 644691, 11935, 644690

-

1.2.99.7

aldehyde + H2O + acceptor = carboxylate + reduced acceptor

644705, 644707

-

Product in Enzyme-catalyzed Reactions (21 results)

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Show Product (21 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

ethanol + NAD+ = aldehyde + NADH + H+

0

-

1.1.1.1

secondary alcohol + NAD+ = aldehyde + NADH

0

-

1.1.1.1

a primary alcohol + NAD+ = an aldehyde + NADH + H+

0

-

1.1.1.1

3 entries

1.1.2.7

a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+

0

-

1.1.2.B3

alcohol + cytochrome c550 = aldehyde + reduced cytochrome c550

0

-

1.1.99.20

primary alcohol + acceptor = aldehyde + reduced acceptor

389910, 389911, 0, 389908, 389906, 389904, 389905, 389907, 389909

-

1.14.14.5

an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O

0

-

1.14.14.5

an alkansulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O

0

-

1.14.14.5

R-CH2-SO3H + FMNH2 + O2 = R-CHO + FMN + sulfite + H2O

438770

-

1.14.14.5

3 entries

1.4.3.13

n-alkylamine + O2 + H2O = aldehyde + NH3 + H2O2

0

-

1.4.3.21

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391910, 391914, 391915, 391916, 391932, 391937, 391908, 0, 391949, 391956, 391960

-

1.4.3.22

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

391940, 391941, 391922, 209612, 391931, 391947, 391909, 391911, 391917, 391918, 391920, 391933, 391934, 391955, 391952, 391953, 391912, 391913, 391928, 391944, 391948, 391958, 391942, 391950, 391926, 391945, 391954, 391927, 391951, 391919, 391935, 391923, 391943, 391925, 391959

-

1.4.3.4

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2

0, 394548, 394573, 394549, 394559, 394574, 394568

-

1.4.3.4

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2

0

-

1.4.3.4

2 entries

1.4.9.1

RCH2NH2 + acceptor + H2O = RCHO + NH3 + reduced acceptor

0

-

1.7.3.1

1-nitroalkane + O2 + H2O = aldehyde + H2O2 + nitrite

0

-

3.3.2.2

1-(1-alkenyl)-sn-glycero-3-phosphocholine + H2O = aldehyde + sn-glycero-3-phosphocholine

137152, 137151, 137153, 137154, 137155, 137156, 137157

-

3.3.2.2

1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = aldehyde + sn-glycero-3-phosphoethanolamine

137154, 137155, 137157, 137160, 137161

-

3.3.2.2

lysoplasmenylethanolamine + H2O = aldehyde + sn-glycero-3-phosphoethanolamine

0

-

3.3.2.2

lysoplasmenylcholine + H2O = an aldehyde + sn-glycero-3-phosphocholine

0

-

3.3.2.2

4 entries

4.1.1.1

a 2-oxo acid = an aldehyde + CO2

0

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.3.2

e.g. formaldehyde, 4-pyridinecarboxaldehyde, propionaldehyde, glycolaldehyde

644654

-

1.2.7.5

substrate inhibition at high concentrations, overview

11935

-

Enzyme Kinetic Parameters

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.14.3

0.001

0.01

-

348579

1.17.3.2

20

-

cofactor 2,6-dichlorophenolindophenol

644648

References & Links

Literature References (114)

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Show Reference (114 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

137151

2712287

Continuous spectrophotometric assay of phospholipase A2 activity hydrolyzing plasmalogens using coupling enzymes

1989

Hirashima, Y.; Jurkowitz-Alexander, M.S.; Farooqui, A.A.; Horrocks, L.A.

Anal. Biochem.

176

180-184

137152

3753461

The catabolism of plasmenylcholine in the guinea pig heart

1986

Arthur, G.; Page, L.; Mock, T.; Choy, P.C.

Biochem. J.

236

475-480

137153

13783189

The metabolism of plasmalogen: enzymatic hydrolysis of the vinyl ether

1961

Warner, H.R.; Lands, W.E.M.

J. Biol. Chem.

236

2404-2409

137154

10064898

dentification and characterization of alkenyl hydrolase (lysoplasmalogenase) in microsomes and identification of a plasmalogen-active phospholipase A2 in cytosol of small intestinal epithelium

1999

Jurkowitz, M.S.; Horrocks, L.A.; Litsky, M.L.

Biochim. Biophys. Acta

1437

142-156

137155

2930768

Solubilization, purification and characterization of lysoplasmalogen alkenylhydrolase (lysoplasmalogenase) from rat liver microsomes

1989

Jurkowitz-Alexander, M.; Ebata, H.; Mills, J.S.; Murphy, E.J.; Horrocks, L.A.

Biochim. Biophys. Acta

1002

203-212

137156

2764893

Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver

1989

Hirashima, Y.; Farooqui, A.A.; Horrocks, L.A.

Biochem. J.

260

605-608

137157

-

Assay procedures and properties of plasmalogenase, lysoplasmalogenase and plasmalogen specific phospholipase A2

1989

Hirashima, Y.; Farooqui, A.A.; Horrocks, L.A.

Front. Chem.

1

91-102

137160

7239443

Liberation of free aldehyde from 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) by rat liver microsomes

1981

Gunawan, J.; Debuch, H.

Hoppe-Seyler's Z. Physiol. Chem.

362

445-452

137161

7097275

Lysoplasmalogenase - a microsomal enzyme from rat brain

1982

Gunawan, J.; Debuch, H.

J. Neurochem.

39

693-699

209612

409634

The purification and preliminary investigation of fumarase, peroxidase, diamine oxidase and adenosine deaminase from human seminal plasma

1977

Crabbe, M.J.; Kavanagh, J.P.

Biochem. Soc. Trans.

5

735-737

288137

2721637

Purification of alpha-ketoaldehyde dehydrogenase from the human liver and its possible significance in the control of glycation

1989

Oimomi, M.; Hata, F.; Nakamichi, T.; Baba, S.; Kato, H.

Experientia

45

463-466

288138

-

Metabolism of 2-ketoaldehydes in bacteria: oxidative conversion of methylglyoxal to pyruvate by an enzyme from Pseudomonas putida

1987

Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.

Agric. Biol. Chem.

51

1059-1066

288139

-

Glucose formation from methylglyoxal in rat hepatocytes

1985

Saez, G.T.; Blay, P.; Vina, J.R.; Vina, J.

Biochem. Soc. Trans.

13

945-946

288140

7107625

Purification and characterization of NAD and NADP-linked alpha-ketoaldehyde dehydrogenases involved in catalyzing the oxidation of methylglyoxal to pyruvate

1982

Ray, S.; Ray, M.

J. Biol. Chem.

257

10566-10570

348579

309549

Bacterial luciferase: FMNH2-aldehyde oxidase

1978

Hastings, J.W.; Presswood, R.P.

Methods Enzymol.

53

558-570

348781

-

Purification and characterization of the bovine cerebral mitochondrial aldehyde dehydrogenase

1991

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

Korean Biochem. J.

24

224-230

389904

-

Identification of the prosthetic group and further characterization of a novel enzyme, polyethylne glycol dehydrogenase

1985

Kawai, F.; Yamanaka, H.; Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.

Agric. Biol. Chem.

49

1071-1076

389905

-

Identification of reaction products of polyethylene glycol dehydrogenase

1983

Kawai, F.; Kimura, T.; Tani, Y.; Yamada, H.; Ueno, T.; Fukami, H.

Agric. Biol. Chem.

47

1669-1671

389906

6999995

Purification and characterization of polyethylene glycol dehydrogenase involved in the bacterial metabolism of polyethylene glycol

1980

Kawai, F.; Kimura, T.; Yoshiki, T.; Yamada, H.; Mamoru, K.

Appl. Environ. Microbiol.

40

701-705

389907

-

Inducible or constitutive polyethylene glycol dehydrogenase involved in the aerobic metabolism of polyethylene glycol

1989

Yamanaka, H.; Kawai, F.

J. Ferment. Bioeng.

67

300-302

389908

-

Purification and characterization of constitutive polyethylene glycol (PEG) dehydrogenase of a PEG 4000-utilizing Flavobacterium sp. No. 203

1989

Yamanaka, H.; Kawai, F.

J. Ferment. Bioeng.

67

324-330

389909

3800554

Biodegradation of polyethylene glycol by symbiotic mixed culture (obligate mutualism)

1986

Kawai, F.; Yamanaka, H.

Arch. Microbiol.

146

125-129

389910

-

Polyethylene glycol dehydrogenase activity of Rhodopseudomonas acidophila derives from a type I quinohemoprotein alcohol dehydrogenase

1996

Yasuda, M.; Cherepanov, A.; Duine, J.A.

FEMS Microbiol. Lett.

138

23-28

389911

11673442

The first step in polyethylene glycol degradation by Sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide

2001

Sugimoto, M.; Tanabe, M.; Hataya, M.; Enokibara, S.; Duine, J.A.; Kawai, F.

J. Bacteriol.

183

6694-6698

391908

14002223

Monoamine oxidase II. Copper, one of the prosthetic groups of plasma monamine oxidase

1962

Yamada, H.; Yasunobu, K.T.

J. Biol. Chem.

237

3077-3082

391909

4964016

Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase

1967

Mondovi, B.; Costa, M.T.; Agro, A.F.; Rotilio, G.

Arch. Biochem. Biophys.

119

373-381

391910

-

Pig liver monoamine oxidase I: isolation and characterization

1974

Carper, W.R.; Stoddard, D.D.; Martin, D.F.

Biochim. Biophys. Acta

334

287-296

391911

826412

Purification of pig kidney diamine oxidase by gel-exclusion chromatography

1976

Floris, G.; Fadda, M.B.; Pellegrini, M.; Corda, M.; Agro, A.F.

FEBS Lett.

72

179-181

391912

-

Purification and properties of pea cotyledon and embryo diamine oxidase

1977

Srivastava, S.K.; Prakash, V.

Phytochemistry

16

189-190

391913

4218929

Kinetic and other characteristics of diamine oxidase of pea seedlings

1974

Nylen, U.; Szybek, P.

Acta Chem. Scand. B

28

1153-1160

391914

6615797

Heterogeneity of pig plasma amine oxidase: molecular and catalytic properties of chromatographically isolated forms

1983

Falk, M.C.; Staton, A.J.; Williams, T.J.

Biochemistry

22

3746-3751

391915

4375031

Effect of azide on some spectral and kinetic properties of pig-plasma benzylamine oxidase

1974

Lindström, A.; Olsson, B.; Petterson, G.

Eur. J. Biochem.

48

237-243

391916

4364395

Kinetics of the interaction between pig-plasma benzylamine oxidase and hydrazine derivatives

1974

Lindström, A.; Olsson, B.; Petterson, G.

Eur. J. Biochem.

42

177-182

391917

4198360

Kinetics of the diamine oxidase reaction

1973

Bardsley, W.G.; Crabbe, M.J.C.; Shindler, J.S.

Biochem. J.

131

459-469

391918

5000447

On the active site of diamine oxidase: kinetic studies

1971

Costa, M.T.; Rotilio, G.; Agro, A.F.; Vallogini, M.P.; Mondovi, B.

Arch. Biochem. Biophys.

147

8-13

391919

11945979

Modification of catalytic properties of amine oxidases

1971

Stesina, L.N.; Akopyan, Z.I.; Gorkin, V.Z.

FEBS Lett.

16

349-351

391920

2503012

Characterization of free and immobilized amine oxidases

1989

Stevanato, R.; Porchia, M.; Befani, O.; Mondovi, B.; Rigo, A.

Biotechnol. Appl. Biochem.

11

266-272

391922

6403048

Distribution and properties of human intestinal diamine oxidase and its relevance for the histamine catabolism

1983

Bieganski, T.; Kusche, J.; Lorenz, W.; Hesterberg, R.; Stahlknecht, C.D.; Feussner, K.D.

Biochim. Biophys. Acta

756

196-203

391923

808238

Purification of histaminase (diamine oxidase) from human pregnancy plasma by affinity chromatography

1975

Baylin, S.B.; Margolis, S.

Biochim. Biophys. Acta

397

294-306

391925

-

Diamine oxidase from Lens esculenta seedlings: purification and properties

1983

Floris, G.; Giartosio, A.; Rinaldi, A.

Phytochemistry

22

1871-1874

391926

-

Purification and characterization of diamine oxidase from rice embryos

1984

Chaudhuri, M.M.; Ghosh, B.

Phytochemistry

23

241-243

391927

-

Purification and characterization of diamine oxidase from clover leaves

1987

Delhaize, E.; Webb, J.

Phytochemistry

26

641-643

391928

-

Purification and properties of diamine oxidase from pea epicotyls

1981

Yanagisawa, H.; Hirasawa, E.; Suzuki, Y.

Phytochemistry

20

2105-2108

391931

182134

Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity

1976

Crabbe, M.J.C.; Waight, R.D.; Bardsley, W.G.; Barker, R.W.; Kelly, I.D.; Knowles, P.F.

Biochem. J.

155

679-687

391932

218560

Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods

1979

Barker, R.; Boden, N.; Cayley, G.; Charlton, S.C.; Henson, R.; Holmes, M.C.; Kelly, I.D.; Knowles, P.F.

Biochem. J.

177

289-302

391933

2498301

Kinetic studies on the inhibition mechanism of diamine oxidase from porcine kidney by aminoguanidine

1989

Tamura, H.; Horiike, K.; Fukuda, H.; Watanabe, T.

J. Biochem.

105

299-306

391934

6403525

Spectroscopic and kinetics studies of the inhibition of pig kidney diamine oxidase by anions

1983

Dooley, D.M.; Golnik, K.C.

J. Biol. Chem.

258

4245-4248

391935

6814913

Purification and properties of diamine oxidase from Euphorbia latex

1982

Rinaldi, A.; Floris, G.; Finazzi-Agro, A.

Eur. J. Biochem.

127

417-422

391937

2848544

Purification of benzylamine oxidase from cultured porcine aortic smooth muscle cells

1988

Hysmith, R.M.; Boor, P.J.

Biochem. Cell Biol.

66

821-829

391940

2798365

Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: purification and properties

1989

Cogoni, A.; Farci, R.; Medda, R.; Rinaldi, A.; Floris, G.

Prep. Biochem.

19

95-112

391941

-

Purification and properties of the diamine oxidase from Vicia faba leaves

1981

Matsuda, H.; Suzuki, Y.

Plant Cell Physiol.

22

737-746

391942

-

Partial purification and characterization of diamine oxidase from groundnut embryo

1980

Sindhu, R.K.; Desai, H.V.

Indian J. Biochem. Biophys.

17

194-197

391943

-

Diamine oxidase from sainfon (Onobrychis viciifolia). Purification and some properties

1989

Pec, P.; Zajoncova, L.; Jilek, M.

Biologia (Bratisl. )

44

1177-1184

391944

-

Purification and properties of diamine oxidase from soybean (Glycine max)

1989

Kang, J.H.; Cho, Y.D.

Hanguk Saenghwahakhoe Chi

22

361-366

391945

-

Lentil seedlings amine oxidase: preparation and properties of the copper-free enzyme

1986

Matsumiya, M.; Otake, S.

Nippon Suisan Gakkaishi

52

1617-1623

391947

-

Purification and properties of diamine oxidase from human kidney

1987

Suzuki, O.; Matsumoto, T.

Biogenic Amines

4

237-245

391948

8239662

Purification and characterization of amine oxidase from soybean seedlings

1993

Vianello, F.; Di Paolo, M.L.; Stevanato, R.; Gasparini, R.; Rigo, A.

Arch. Biochem. Biophys.

307

35-39

391949

8011631

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Links to other databases for an aldehyde

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