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Ligand 4-hydroxy-2-hexenal

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Substrate (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.184

4-hydroxy-2-hexenal + NADPH + H+ = ?

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1.3.1.27

4-hydroxy-2-hexenal + NADPH + H+ = 4-hydroxyhexadecanal + NADP+

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1.3.1.48

4-hydroxy-2-hexenal + NADPH = 4-hydroxyhexanal + NADP+

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1.3.1.74

4-hydroxy-(2E)-hexenal + NAD(P)H = 4-hydroxyhexenal + NAD(P)+

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1.6.5.5

4-hydroxy-2-hexenal + NADPH = 4-hydroxy-hexanal + NADP+

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Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.2.3

(3Z)-hexenal + H2O2 = (2E)-4-hydroxy-2-hexenal + H2O

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Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.19.12

carbonyl modification in a dose-dependent manner

680081

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.1.27

1.33

-

wild-type, pH 7.5, temperature not specified in the publication

724703

1.3.1.48

13.4

-

-

390830

1.3.1.74

0.7

-

pH 6

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1.6.5.5

1.33

-

pH 7, 25°C, wild-type

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1.6.5.5

2.16

-

pH 7, 25°C, mutant T59F

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1.6.5.5

3.67

-

pH 7, 25°C, mutant T53F

724703

1.6.5.5

3 entries

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.1.27

0.13

-

wild-type, pH 7.5, temperature not specified in the publication

724703

1.3.1.27

1.26

-

mutant Y59F, pH 7.5, temperature not specified in the publication

724703

1.3.1.27

3.67

-

mutant Y53F, pH 7.5, temperature not specified in the publication

724703

1.3.1.27

3 entries

1.3.1.48

0.21

-

-

390830

1.3.1.74

0.145

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pH 6

636484

1.6.5.5

0.08

-

pH 7, 25°C, mutant T53F

724703

1.6.5.5

0.13

-

pH 7, 25°C, wild-type

724703

1.6.5.5

1.26

-

pH 7, 25°C, mutant T59F

724703

1.6.5.5

3 entries

References & Links

Literature References (5)

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Show Reference (5 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

636484

12514241

The NADPH:quinone oxidoreductase P1-x-crystallin in Arabidopsis catalyzes the alpha,beta-hydrogenation of 2-alkenals: Detoxication of the lipid peroxide-derived reactive aldehydes

2002

Mano, J.i.; Torii, Y.; Hayashi, S.i.; Takimoto, K.; Matsui, K.; Nakamura, K.; Inze, D.; Babiychuk, E.; Kushnir, S.; Asada, K.

Plant Cell Physiol.

43

1445-1455

680081

18250096

Aberrant molecular properties shared by familial Parkinsons disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1

2008

Kabuta, T.; Setsuie, R.; Mitsui, T.; Kinugawa, A.; Sakurai, M.; Aoki, S.; Uchida, K.; Wada, K.

Hum. Mol. Genet.

17

1482-1496

724703

20835842

Kinetic and structural evidence of the alkenal/one reductase specificity of human zeta-crystallin

2011

Porte, S.; Moeini, A.; Reche, I.; Shafqat, N.; Oppermann, U.; Farres, J.; Pares, X.

Cell. Mol. Life Sci.

68

1065-1077

760865

28274719

Kinetic features of carbonyl reductase 1 acting on glutathionylated aldehydes

2017

Moschini, R.; Rotondo, R.; Renzone, G.; Balestri, F.; Cappiello, M.; Scaloni, A.; Mura, U.; Del-Corso, A.

Chem. Biol. Interact.

276

127-132

Links to other databases for 4-hydroxy-2-hexenal

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Show Links (1 entry)

ChEBI

PubChem

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