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Ligand 4'-hydroxyacetophenone

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.84

(4-hydroxyphenyl)ethan-1-one + NADPH + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O

659744, 674475, 677172, 697753

-

1.14.13.84

4-hydroxyacetophenone + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O

690108, 649387, 644553, 651670, 687422, 695775

-

1.14.13.84

2 entries

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.311

4'-hydroxyacetophenone + NADH + H+ = (S)-4-(1-hydroxyethyl)phenol + NAD+

763319, 739947

-

1.1.1.B3

4'-hydroxyacetophenone + NADH + H+ = (S)-4-(1-hydroxyethyl)phenol + NAD+

741747

-

1.11.1.19

4-hydroxyacetophenone + H2O2 + H+ = ?

743089

-

1.14.13.84

(4-hydroxyphenyl)ethan-1-one + NADPH + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O

644553, 659744, 674475, 677172, 697753

-

1.14.13.84

4-hydroxyacetophenone + NADH + H+ + O2 = 4-hydroxyphenyl acetate + NAD+ + H2O

651172

-

1.14.13.84

4-hydroxyacetophenone + NADPH + H+ + O2 = 4-hydroxyphenyl acetate + NADP+ + H2O

690108, 687422, 651172, 651670, 649387, 644553, 695775

-

1.14.13.84

3 entries

1.14.13.92

4-hydroxyacetophenone + NADPH + O2 = acetic acid 4-hydroxyphenyl ester + NADP+ + O2

657625

-

2.4.1.218

UDP-glucose + 4-hydroxyacetophenone = UDP + (4-acetophenyl)-beta-D-glucopyranoside

393095, 393094

-

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.38

4-ethylphenol + O2 = 1-(4'-hydroxyphenyl)ethanol + 4-vinylphenol + 4-hydroxyacetophenone

10664, 10671, 0

-

1.14.99.15

4-methoxyacetophenone + AH2 + O2 = 4-hydroxyacetophenone + formaldehyde + A + H2O

0

-

2.8.2.22

4-acetylphenyl sulfate + phenol = 4-acetylphenol + phenyl sulfate

0

-

2.8.2.22

4-acetylphenyl sulfate + tyramine = 4-(2-aminoethyl)phenyl sulfate + 4-acetylphenol

0

-

2.8.2.22

2 entries

3.1.1.2

4-acetoxyacetophenone + H2O = 4-hydroxyacetophenone + acetate

0

-

3.1.6.1

4-acetylphenyl sulfate + H2O = 4-acetylphenol + sulfate

0

-

3.1.6.2

p-acetylphenyl sulfate + H2O = p-acetylphenol + sulfate

0

-

3.1.8.1

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate + H2O = 4-acetylphenol + (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate + H2O = 4-acetylphenol + (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (R)-methylphosphonate + H2O = 4-acetylphenol + 4-acetylphenol + (2S)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate + H2O = 4-acetylphenol + (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl (R)-2-methylpropyl methylphosphonate + H2O = (R)-2-methylpropyl methylphosphonate + 4-acetylphenol

0

-

3.1.8.1

4-acetylphenyl (S)-2-methylpropyl methylphosphonate + H2O = (S)-2-methylpropyl methylphosphonate + 4-acetylphenol

0

-

3.1.8.1

4-acetylphenyl 2-methylpropyl (R)-methylphosphonate + H2O = 4-acetylphenol + 2-methylpropyl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl 2-methylpropyl (S)-methylphosphonate + H2O = 4-acetylphenol + 2-methylpropyl (S)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl cyclohexyl (R)-methylphosphonate + H2O = 4-acetylphenol + cyclohexyl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl cyclohexyl (S)-methylphosphonate + H2O = 4-acetylphenol + cyclohexyl (S)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl cyclohexyl methyl (R)-phosphate + H2O = cyclohexyl methyl (R)-phosphate + 4-acetylphenol

0

-

3.1.8.1

4-acetylphenyl cyclohexyl methyl (S)-phosphate + H2O = cyclohexyl methyl (S)-phosphate + 4-acetylphenol

0

-

3.1.8.1

4-acetylphenyl ethyl (R)-methylphosphonate + H2O = 4-acetylphenol + ethyl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl ethyl (S)-methylphosphonate + H2O = 4-acetylphenol + ethyl (S)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl propan-2-yl (R)-methylphosphonate + H2O = 4-acetylphenol + propan-2-yl (R)-methylphosphonate

0

-

3.1.8.1

4-acetylphenyl propan-2-yl (S)-methylphosphonate + H2O = 4-acetylphenol + propan-2-yl (S)-methylphosphonate

0

-

3.1.8.1

4-diethyl phosphate acetophenone + H2O = 4-hydroxyacetophenone + diethyl phosphate

0

-

3.1.8.1

dibutyl 4-acetophenyl phosphate + H2O = dibutyl phosphate + 4-hydroxyacetophenone

0

-

3.1.8.1

diethyl 4-acetophenyl phosphate + H2O = diethyl phosphate + 4-hydroxyacetophenone

0

-

3.1.8.1

19 entries

Inhibitor in Enzyme-catalyzed Reactions (8 results)

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Show Inhibitors (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.179

-

684150

-

1.1.1.62

weak inhibitor with 20.8% inhibition at 0.1 mM

699839

-

1.1.1.64

IC50: 1.70892 mM

667983

-

1.2.1.3

-

675118

-

1.2.1.48

0.25 mM causes 46% inhibition

390324

-

1.3.1.20

-

286128, 349254, 684150, 689972, 701119

2o48, 3D-view

1.3.1.20

competitive inhibitor

686023

2o48, 3D-view

1.3.1.20

inhibits dihydrodiol and D-xylose dehydrogenase activity

286128

2o48, 3D-view

1.3.1.20

3 entries

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

1.3.1.20

2o48, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (4 results)

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Show Turnover Number (4 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.13.84

9.8

-

312 microM NADPH, 50 mM Tris-HCl, pH 8.0, 30°C

695775

1.14.13.84

10.1

-

pH 8, 30°C

644553

1.14.13.84

12.6

-

pH 7.5, 30°C

649387

1.14.13.84

3 entries

1.14.13.92

0.34

-

30°C, pH 7.5, 0.1 mM NADPH

657625

K_M Value (5 results)

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Show KM Value (5 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.84

0.0092

-

pH 7.5, 30°C, pH-dependent

649387

1.14.13.84

0.0381

-

312 microM NADPH, 50 mM Tris-HCl, pH 8.0, 30°C

695775

1.14.13.84

0.039

-

pH 8, 30°C

644553

1.14.13.84

0.047

-

pH 8, 30°C

651670

1.14.13.84

4 entries

1.14.13.92

2.2

-

30°C, pH 7.5, 0.1 mM NADPH

657625

IC₅₀ Value (15 results)

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Show IC50 Value (15 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.1.1.64

1.70892

-

IC50: 1.70892 mM

667983

1.3.1.20

0.00097

-

determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone

684150

1.3.1.20

0.00097

-

the hydroxyl group of 4-hydroxyacetophenone forms hydrogen bond interactions with the side-chain oxygen and the main chain nitrogen of Asp280, the benzene ring and methyl group make a number of hydrophobic contacts with Phe279, Leu158 and Leu177

701119

1.3.1.20

0.00097

-

wild type enzyme

689972

1.3.1.20

0.00097

-

wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.006

-

mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.006

-

mutant W254Y

684150

1.3.1.20

0.075

-

mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.075

-

rmutant F279A

684150

1.3.1.20

0.078

-

mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.078

-

mutant F154A

684150

1.3.1.20

0.083

-

mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.083

-

mutant W254A

684150

1.3.1.20

0.136

-

mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C

684150

1.3.1.20

0.136

-

mutant W125Y

684150

1.3.1.20

14 entries

References & Links

Literature References (30)

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Show Reference (30 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

10664

9791114

Regio- and stereospecific conversion of 4-alkylphenols by the covalent flavoprotein vanillyl-alcohol oxidase

1998

Van der Heuvel, R.H.H.; Fraaije, M.W.; Laane, C.; van Berkel, W.J.H.

J. Bacteriol.

180

5646-5651

10671

10099328

Enantioselective hydroxylation of 4-alkylphenols by vanillyl alcohol oxidase

1998

Drijfhout, F.P.; Fraaije, M.W.; Jongejan, H.; van Berkel, W.J.H.; Franssen, M.C.R.

Biotechnol. Bioeng.

59

171-177

286128

11306093

Identity of dimeric dihydrodiol dehydrogenase as NADP+-dependent D-xylose dehydrogenase in pig liver

2001

Aoki, S.; Ishikura, S.; Asada, Y.; Usami, N.; Hara, A.

Chem. Biol. Interact.

130-132

775-784

349254

7852295

Purification and characterization of dimeric dihydrodiol dehydrogenase from dog liver

1994

Sato, K.; Nakanishi, M.; Deyashiki, Y.; Hara, A.; Matsuura, K.; Ohya, I.

J. Biochem.

116

711-717

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

393094

11937332

Arbutin synthase, a novel member of the NRD1beta glycosyltransferase family, is a unique multifunctional enzyme converting various natural products and xenobiotics

2002

Hefner, T.; Arend, J.; Warzecha, H.; Siems, K.; Stöckigt, J.

Bioorg. Med. Chem.

10

1731-1741

393095

11505382

Utilizing genetically engineered bacteria to produce plant-specific glucosides

2001

Arend, J.; Warzecha, H.; Hefner, T.; Stöckigt, J.

Biotechnol. Bioeng.

76

126-131

644553

11322873

4- Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds

2001

Kamerbeek, N.M.; Moonen, M.J.; van der Ven, J.G.; van Berkel, W.J.H.; Fraaije, M.W.; Janssen, D.B.

Eur. J. Biochem.

268

2547-2557

649387

12514023

Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenase

2003

Kamerbeek, N.M.; Olsthoorn, A.J.J.; Fraaije, M.W.; Janssen, D.B.

Appl. Environ. Microbiol.

69

419-426

651172

15153101

Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases

2004

Kamerbeek, N.M.; Fraaije, M.W.; Janssen, D.B.

Eur. J. Biochem.

271

2107-2116

651670

11073896

Conversion of 4-hydroxyacetophenone into 4-phenyl acetate by a flavin adenine dinucleotide-containing Baeyer-Villiger-type monooxygenase

2000

Tanner, A.; Hopper, D.J.

J. Bacteriol.

182

6565-6569

657625

15599520

Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining

2005

Fraaije, M.W.; Wu, J.; Heuts, D.P.; van Hellemond, E.W.; Spelberg, J.H.; Janssen, D.B.

Appl. Microbiol. Biotechnol.

66

393-400

659744

-

Biooxidation of ketones with a cyclobutanone structural motif by recombinant whole-cells expressing 4-hydroxyacetophenone monooxygenase

2005

Mihovilovic, M.D.; Kapitan, P.; Rydz, J.; Rudroff, F.; Ogink, F.H.; Fraaije, M.W.

J. Mol. Catal. B

32

135-140

667983

16797984

Synthesis, biochemical evaluation and rationalisation of the inhibitory activity of a series of 4-hydroxyphenyl ketones as potential inhibitors of 17beta-hydroxysteroid dehydrogenase type 3 (17beta-HSD3)

2006

Lota, R.K.; Dhanani, S.; Owen, C.P.; Ahmed, S.

Bioorg. Med. Chem. Lett.

16

4519-4522

674475

16049018

Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase

2005

van den Heuvel, R.H.; Tahallah, N.; Kamerbeek, N.M.; Fraaije, M.W.; van Berkel, W.J.; Janssen, D.B.; Heck, A.J.

J. Biol. Chem.

280

32115-32121

675118

16441583

Characterization of an aldehyde dehydrogenase from Euglena gracilis

2006

Rodriguez-Zavala, J.S.; Ortiz-Cruz, M.A.; Moreno-Sanchez, R.

J. Eukaryot. Microbiol.

53

36-42

677172

-

4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides

2006

de Gonzalo, G.; Torres Pazmino, D.E.; Ottolina, G.; Fraaije, M.W.; Carrea, G.

Tetrahedron Asymmetry

17

130-135

684150

18453689

Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid

2008

Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.

Acta Crystallogr. Sect. D

64

532-542

686023

18264804

Structural and functional features of dimeric dihydrodiol dehydrogenase

2008

Carbone, V.; Hara, A.; El-Kabbani, O.

Cell. Mol. Life Sci.

65

1464-1474

687422

18502868

Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACB

2008

Moonen, M.J.; Kamerbeek, N.M.; Westphal, A.H.; Boeren, S.A.; Janssen, D.B.; Fraaije, M.W.; van Berkel, W.J.

J. Bacteriol.

190

5190-5198

689972

-

Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis

2007

Carbone, V.; Endo, S.; Sumii, R.; Chung, R.P.; Matsunaga, T.; Hara, A.; El-Kabbani, O.

Proteins Struct. Funct. Bioinform.

70

176-187

690108

-

Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases

2007

Rodriguez, C.; De Gonzalo, G.; Fraaije, M.W.; Gotor, V.

Tetrahedron Asymmetry

18

1338-1344

695775

19251889

Cloning, expression, characterization, and biocatalytic investigation of the 4-hydroxyacetophenone monooxygenase from Pseudomonas putida JD1

2009

Rehdorf, J.; Zimmer, C.L.; Bornscheuer, U.T.

Appl. Environ. Microbiol.

75

3106-3114

697753

-

Enzymatic Baeyer-Villiger oxidation of Benzo-Fused ketones: Formation of regiocomplementary lactones

2009

Rioz-Martinez, A.; De Gonzal, D.G.; Torres Pazmino, D.; Fraaije, M.; Gotor, V.

Eur. J. Org. Chem.

15

2526-2532

699839

18620056

Synthesis, biochemical evaluation and rationalisation of the inhibitory activity of a range of 4-hydroxyphenyl ketones as potent and specific inhibitors of the type 3 of 17beta-hydroxysteroid dehydrogenase (17beta-HSD3)

2008

Lota, R.K.; Olusanjo, M.S.; Dhanani, S.; Owen, C.P.; Ahmed, S.

J. Steroid Biochem. Mol. Biol.

111

128-137

701119

17654552

Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site-directed mutagenesis

2008

Carbone, V.; Endo, S.; Sumii, R.; Chung, R.; Matsunaga, T.; Hara, A.; El-Kabbani, O.

Proteins Struct. Funct. Genet.

70

176-187

739947

25549618

Asymmetric reduction of ketones and beta-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum

2015

Dudzik, A.; Snoch, W.; Borowiecki, P.; Opalinska-Piskorz, J.; Witko, M.; Heider, J.; Szaleniec, M.

Appl. Microbiol. Biotechnol.

99

5055-5069

741747

25549618

Asymmetric reduction of ketones and beta-keto esters by (S)-1-phenylethanol dehydrogenase from denitrifying bacterium Aromatoleum aromaticum

2015

Dudzik, A.; Snoch, W.; Borowiecki, P.; Opalinska-Piskorz, J.; Witko, M.; Heider, J.; Szaleniec, M.

Appl. Microbiol. Biotechnol.

99

5055-5069

743089

-

Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases

2014

Liers, C.; Aranda, E.; Strittmatter, E.; Piontek, K.; Plattner, D.; Zorn, H.; Ullrich, R.; Hofrichter, M.

J. Mol. Catal. B

103

41-46

763319

28550607

DFT-based prediction of reactivity of short-chain alcohol dehydrogenase

2017

Stawoska, I.; Dudzik, A.; Wasylewski, M.; Jemiola-Rzeminska, M.; Skoczowski, A.; Strzalka, K.; Szaleniec, M.

J. Comput. Aided Mol. Des.

31

587-602

Links to other databases for 4'-hydroxyacetophenone

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Show Links (1 entry)

ChEBI

PubChem