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Basic Ligand Information
Roles as Enzyme Ligand
Enzyme Kinetic Parameters
References & Links
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Ligand 4-tert-butylcatechol

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Basic Ligand Information

Molecular Structure

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Molecular Formula

BRENDA Name

InChIKey

C₁₀H₁₄O₂

4-tert-butylcatechol

XESZUVZBAMCAEJ-UHFFFAOYSA-N

Synonyms:

4-t-butylcatechol, 4-tertiary butylcatechol, tert-butyl-catechol, tert-butylcatechol, tert-butylcathechol

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (12 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

4-tert-butylcatechol + O2 = 4-tert-butyl-1,2-benzoquinone + H2O

712216, 686666, 674108

1.10.3.1

4-tert-butylcatechol + O2 = ?

701876, 686666

1.10.3.1

tert-butyl-catechol + O2 = ?

671593

1.10.3.1

tert-butylcatechol + O2 = ?

4-tert-butylcatechol + O2 = ?

675235

1.13.11.1

4-tert-butylcatechol + O2 = ?

697316

1.14.18.1

4-tert-butylcatechol + 1/2 O2 = 4-(tert-butyl)benzo-1,2-quinone + H2O

687224, 685662

1.14.18.1

4-tert-butylcatechol + 1/2 O2 = 4-tert-butylcyclohexa-3,5-diene-1,2-dione + H2O

685018

1.14.18.1

4-tert-butylcatechol + O2 = 4-tert-butyl-o-benzoquinone + H2O

636442, 636439

1.14.18.1

4-tert-butylcatechol + O2 = ?

745746, 745998

1.14.18.1

tert-butylcatechol + 1/2 O2 = 4-(tert-butyl)benzo-1,2-quinone + H2O

S-adenosyl-L-methionine + 4-tert-butylcatechol = S-adenosyl-L-homocysteine + ?

658517

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.1

field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol

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

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EC NUMBER

ENZYME 3D STRUCTURE

1.11.1.15

4k7o, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

48.05

641.8

3320

20.5

recombinant enzyme, pH 7.2, 37Â°C

294

640.1

642

1650

recombinant enzyme, pH 7.2, 37Â°C

K_M Value (17 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.10.3.1

0.91

675458

1.10.3.1

1.2

pH 4.5, 25Â°C, soluble, active enzyme form

671593

1.10.3.1

1.23

pH 4.5, 25Â°C, particulate, latent enzyme form

2.8

3.9

4.1

0.263

soluble (PPO-S) peach polyphenol oxidase without SDS

687224

1.14.18.1

0.3

membrane-bound (PPO-B) peach polyphenol oxidase without SDS

687224

1.14.18.1

0.6

recombinant enzyme, pH 7.2, 37Â°C

745746

1.14.18.1

0.65

recombinant enzyme, pH 7.2, 37Â°C

745746

1.14.18.1

0.85

membrane-bound (PPO-B) peach polyphenol oxidase with 2 mM SDS

1.2

1.45

1.84

soluble (PPO-S) peach polyphenol oxidase with 2 mM SDS

2.8

136

IC₅₀ Value (3 results)

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EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.14.11.29

0.03

pH 7.0, 37Â°C

725647

1.14.11.30

0.12

pH 7.0, 37Â°C

725647

2.1.3.2

0.031

at pH 8.0 and 45Â°C

755966

References & Links

Literature References (19)

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Show Reference (19 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

636439

10691963

Kinetic characterization of the substrate specificity and mechanism of mushroom tyrosinase

2000

Espin, J.C.; Varon, R.; Fenoll, L.G.; Gilabert, M.A.; Garcia-Ruiz, P.A.; Tudela, J.; Garcia-Canovas, F.

Eur. J. Biochem.

267

1270-1279

636442

10725136

Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase

2000

Perez-Gilabert, M.; Garcia Carmona, F.

J. Agric. Food Chem.

695-700

658517

12920175

Conjugation of catechols by recombinant human sulfotransferases, UDP-glucuronosyltransferases, and soluble catechol O-methyltransferase: structure-conjugation relationships and predictive models

2003

Taskinen, J.; Ethell, B.T.; Pihlavisto, P.; Hood, A.M.; Burchell, B.; Coughtrie, M.W.H.

Drug Metab. Dispos.

1187-1197

671593

16406214

Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): kinetic characterization and comparison with the active form

2006

Selles-Marchart, S.; Casado-Vela, J.; Bru-Martinez, R.

Arch. Biochem. Biophys.

446

175-185

674108

16104806

Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate

2005

Gandia-Herrero, F.; Nez-Atieanzar, M.J.; Cabanes, J.; Garcia-Carmona, F.; Escribano, J.

J. Agric. Food Chem.

6825-6830

675235

16959319

Enzymatic and spectroscopic studies on the activation or inhibition effects by substituted pHenolic compounds in the oxidation of aryldiamines and catechols catalyzed by Rhus vernicifera laccase

2006

Casella, L.; Gullotti, M.; Monzani, E.; Santagostini, L.; Zoppellaro, G.; Sakurai, T.

J. Inorg. Biochem.

100

2127-2139

675458

Kinetic study of monophenol and o-diphenol binding to oxytyrosinase

2005

Garcia-Molina, F.; Penalver, M.J.; Fenoll, L.G.; Rodriguez-Lopez, J.N.; Varon, R.; Gracia-Canovas, F.; Tudela, J.

J. Mol. Catal. B

185-192

685018

18647136

Phenolic substrates and suicide inactivation of tyrosinase: kinetics and mechanism

2008

Munoz-Munoz, J.L.; Garcia-Molina, F.; Garcia-Ruiz, P.A.; Molina-Alarcon, M.; Tudela, J.; Garcia-Canovas, F.; Rodriguez-Lopez, J.N.

Biochem. J.

416

431-440

685662

17617709

Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko

2007

Kawamura-Konishi, Y.; Tsuji, M.; Hatana, S.; Asanuma, M.; Kakuta, D.; Kawano, T.; Mukouyama, E.B.; Goto, H.; Suzuki, H.

Biosci. Biotechnol. Biochem.

1752-1760

686666

17651437

Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity

2007

Kanade, S.R.; Suhas, V.L.; Chandra, N.; Gowda, L.R.

FEBS J.

274

4177-4187

687224

17994689

Partial purification of latent polyphenol oxidase from peach (Prunus persica L. Cv. Catherina). Molecular properties and kinetic characterization of soluble and membrane-bound forms

2007

Cabanes, J.; Escribano, J.; Gandia-Herrero, F.; Garcia-Carmona, F.; Jimenez-Atienzar, M.

J. Agric. Food Chem.

10446-10451

688438

Kinetic characterization of diphenolase activity from Streptomyces antibioticus tyrosinase in the presence and absence of cyclodextrins

2007

Orenes-Pinero, E.; Garcia-Carmona, F.; Sanchez-Ferrer, A.

J. Mol. Catal. B

143-148

697316

19301316

Fine-tuning of catalytic properties of catechol 1,2-dioxygenase by active site tailoring

2009

Caglio, R.; Valetti, F.; Caposio, P.; Gribaudo, G.; Pessione, E.; Giunta, C.

ChemBioChem

1015-1024

701876

19798497

Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: production and characterization of an Aspergillus oryzae catechol oxidase

2009

Gasparetti, C.; Faccio, G.; Arvas, M.; Buchert, J.; Saloheimo, M.; Kruus, K.

Appl. Microbiol. Biotechnol.

213-226

712216

20039636

Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase

2010

Virador, V.M.; Reyes Grajeda, J.P.; Blanco-Labra, A.; Mendiola-Olaya, E.; Smith, G.M.; Moreno, A.; Whitaker, J.R.

J. Agric. Food Chem.

1189-1201

725647