print visible entries

print all entries

Ligand caffeoyl aldehyde

Basic Ligand Information

Molecular Structure

close all tables

open all tables

Roles as Enzyme Ligand

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

top print hide

Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.68

S-adenosyl-L-methionine + caffeoyl aldehyde = ?

485067

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

top print hide

Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffealdehyde + CoA + NADP+

0

-

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffeolylaldehyde + CoA + NADP+

0

-

1.2.1.44

2 entries

Substrate in Enzyme-catalyzed Reactions (13 results)

top print hide

Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.195

caffeoyl aldehyde + NADPH + H+ = caffeoyl alcohol + NADP+

712611

-

1.1.1.195

caffeyl aldehyde + NADPH = caffeyl alcohol + NADP+

670458

-

1.1.1.195

caffeylaldehyde + NADP+ = caffeyl alcohol + NADPH + H+

739335

-

1.1.1.195

caffeylaldehyde + NADPH + H+ = caffeyl alcohol + NADP+

739335

-

1.1.1.195

4 entries

1.3.1.102

caffeoyl aldehyde + NADP+ = dihydrocaffeoyl aldehyde + NADPH + H+

744897

-

2.1.1.104

S-adenosyl-L-methionine + caffeoyl aldehyde = ?

758068

-

2.1.1.104

S-adenosyl-L-methionine + caffeoyl aldehyde = S-adenosyl-L-homocysteine + ?

757943, 702477

-

2.1.1.104

S-adenosyl-L-methionine + caffeoyl aldehyde = S-adenosyl-L-homocysteine + coniferaldehyde

757935

-

2.1.1.104

S-adenosyl-L-methionine + caffeoylaldehyde = ?

720716

-

2.1.1.68

S-adenosyl-L-methionine + caffeoyl aldehyde = ?

720616, 720680, 485067

-

2.1.1.68

S-adenosyl-L-methionine + caffeoyl aldehyde = S-adenosyl-L-homocysteine + ?

718207

-

2.1.1.68

S-adenosyl-L-methionine + caffeoyl aldehyde = S-adenosyl-L-homocysteine + coniferyl aldehyde

485067, 485531, 702477

-

2.1.1.68

S-adenosyl-L-methionine + caffeoyl aldehyde = S-adenosyl-L-homocysteine + ferulic aldehyde

658800

-

2.1.1.104

4 entries

2.1.1.68

4 entries

Product in Enzyme-catalyzed Reactions (6 results)

top print hide

Show Product (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.30

caffeic acid + NADPH + ATP = 3-(3,4-dihydroxyphenyl)-2-propen-1-al + NADP+ + AMP + H2O

288183

-

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffealdehyde + CoA + NADP+

0

-

1.2.1.44

caffeoyl-CoA + NADPH = caffeic aldehyde + CoA + NADP+

288230, 0, 288234

-

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffeolylaldehyde + CoA + NADP+

0

-

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffeylaldehyde + CoA + NADP+

0

-

1.2.1.44

caffeoyl-CoA + NADPH + H+ = caffeylaldehyde + NADP+

0

-

1.2.1.44

5 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (7 results)

top print hide

Show Turnover Number (7 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.195

0.062

-

isoform CAD2, at pH 6.0 and 25°C

739335

1.1.1.195

0.072

-

isoform CAD1, at pH 6.0 and 25°C

739335

1.3.1.102

0.068

-

pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V

744897

1.3.1.102

0.132

-

pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1

744897

1.3.1.102

0.238

-

pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2

744897

1.3.1.102

0.277

-

pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y

744897

1.1.1.195

2 entries

1.3.1.102

4 entries

2.1.1.68

1.55

-

pH 7.5, temperature not specified in the publication

720616

K_M Value (14 results)

top print hide

Show KM Value (14 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.195

0.06592

-

isoform CAD2, at pH 6.0 and 25°C

739335

1.1.1.195

0.0891

-

pH not specified in the publication, temperature not specified in the publication

712611

1.1.1.195

0.09463

-

isoform CAD1, at pH 6.0 and 25°C

739335

1.3.1.102

0.1437

-

pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y

744897

1.3.1.102

0.1812

-

pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2

744897

1.3.1.102

0.1933

-

pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V

744897

1.3.1.102

0.2214

-

pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1

744897

1.1.1.195

3 entries

1.3.1.102

4 entries

2.1.1.104

0.0437

-

-

702477

2.1.1.68

0.0069

-

recombinant enzyme

485067

2.1.1.68

0.01

-

wild type

485531

2.1.1.68

0.0148

-

pH 7.5, 30°C

658800

2.1.1.68

0.0197

-

pH 7.5, temperature not specified in the publication

720616

2.1.1.68

0.032

-

pH and temperature not specified in the publication

718207

2.1.1.68

0.04372

-

-

702477

2.1.1.68

6 entries

References & Links

Literature References (18)

top print hide

Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

288183

4386171

Reduction of cinnamic acid to cinnamaldehyde and alcohol

1968

Gross, G.G.; Bolkart, K.H.; Zenk, M.H.

Biochem. Biophys. Res. Commun.

32

173-178

288230

7454

Enzymic synthesis of lignin precursors. Purification and properties of a cinnamoyl-CoA: NADPH reductase from cell suspension cultures of soybean (Glycine max)

1976

Wengenmayer, H.; Ebel, J.; Grisebach, H.

Eur. J. Biochem.

65

529-536

288234

236926

Reduction of coenzyme A thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia

1975

Gross, G.G.; Kreiten, W.

FEBS Lett.

54

259-262

485067

11169195

Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols

2001

Parvathi, K.; Chen, F.; Guo, D.; Blount, J.W.; Dixon, R.A.

Plant J.

25

193-202

485531

12084826

Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase

2002

Zubieta, C.; Kota, P.; Ferrer, J.L.; Dixon, R.A.; Noel, J.P.

Plant Cell

14

1265-1277

658800

32688895

Transgenic down-regulation of caffeic acid O-methyltransferase (COMT) led to improved digestibility in tall fescue (Festuca arundinacea)

2004

Chen, L.; Auh, C.K.; Dowling, P.; Bell, J.; Lehmann, D.; Wang, Z.Y.

Funct. Plant Biol.

31

235-245

670458

16633561

Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4

2006

Youn, B.; Camacho, R.; Moinuddin, S.G.; Lee, C.; Davin, L.B.; Lewis, N.G.; Kang, C.

Org. Biomol. Chem.

4

1687-1697

702477

17976886

Characterization of a caffeic acid 3-O-methyltransferase from wheat and its function in lignin biosynthesis

2008

Ma, Q.; Xu, Y.

Biochimie

90

515-524

712611

20400532

Functional analysis of a cinnamyl alcohol dehydrogenase involved in lignin biosynthesis in wheat

2010

Ma, Q.H.

J. Exp. Bot.

61

2735-2744

718207

15118832

Characterization of a multifunctional methyltransferase from the orchid Vanilla planifolia

2004

Pak, F.E.; Gropper, S.; Dai, W.D.; Havkin-Frenkel, D.; Belanger, F.C.

Plant Cell Rep.

22

959-966

720616

20652169

Insights into lignin primary structure and deconstruction from Arabidopsis thaliana COMT (caffeic acid O-methyl transferase) mutant Atomt1

2010

Moinuddin, S.G.; Jourdes, M.; Laskar, D.D.; Ki, C.; Cardenas, C.L.; Kim, K.W.; Zhang, D.; Davin, L.B.; Lewis, N.G.

Org. Biomol. Chem.

8

3928-3946

720680

21177481

Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference

2010

Louie, G.V.; Bowman, M.E.; Tu, Y.; Mouradov, A.; Spangenberg, G.; Noel, J.P.

Plant Cell

22

4114-4127

720716

21629984

Functional characterization of two new members of the caffeoyl CoA O-methyltransferase-like gene family from Vanilla planifolia reveals a new class of plastid-localized O-methyltransferases

2011

Widiez, T.; Hartman, T.G.; Dudai, N.; Yan, Q.; Lawton, M.; Havkin-Frenkel, D.; Belanger, F.C.

Plant Mol. Biol.

76

475-488

739335

23774375

Molecular cloning and biochemical characterization of two cinnamyl alcohol dehydrogenases from a liverwort Plagiochasma appendiculatum

2013

Sun, Y.; Wu, Y.; Zhao, Y.; Han, X.; Lou, H.; Cheng, A.

Plant Physiol. Biochem.

70

133-141

744897

23954295

A single amino acid determines the catalytic efficiency of two alkenal double bond reductases produced by the liverwort Plagiochasma appendiculatum

2013

Wu, Y.; Cai, Y.; Sun, Y.; Xu, R.; Yu, H.; Han, X.; Lou, H.; Cheng, A.

FEBS Lett.

587

3122-3128

757935

26277769

Functional characterization of a plastidal cation-dependent O-methyltransferase from the liverwort Plagiochasma appendiculatum

2015

Xu, R.X.; Zhao, Y.; Gao, S.; Zhang, Y.Y.; Li, D.D.; Lou, H.X.; Cheng, A.X.

Phytochemistry

118

33-41

757943

30634081

The identification and functional characterization of three liverwort class I O-methyltransferases

2019

Liu, H.; Xu, R.X.; Zhang, X.S.; Zhu, T.T.; Lou, H.X.; Cheng, A.X.

Phytochemistry

159

190-198

758068

30685696

Isolation and functional characterization of two caffeoyl coenzyme A 3-O-methyltransferases from the fern species Polypodiodes amoena

2019

Zhang, X.S.; Ni, R.; Wang, P.Y.; Zhu, T.T.; Sun, C.J.; Lou, H.X.; Cheng, A.X.

Plant Physiol. Biochem.

136

169-177

Links to other databases for caffeoyl aldehyde

top print hide

Show Links (1 entry)

ChEBI

PubChem