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Ligand 4-methylsalicylic acid

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 4-methylsalicylic acid

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.1

4-methylsalicylate + NADH + 2 H+ + O2 = 4-methylcatechol + NAD+ + H2O + CO2

680483

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Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Substrate (6 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.4

4-methylsalicylate + O2 = (2Z,4Z)-3-methyl-6-oxohepta-2,4-dienoate

748157

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1.13.11.4

4-methylsalicylate + O2 = ?

698728

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1.14.13.1

4-methylsalicylate + NADH + 2 H+ + O2 = 4-methylcatechol + NAD+ + H2O + CO2

680483, 684569

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1.14.13.1

4-methylsalicylate + NADH + H+ + O2 = 4-methylbenzene-1,2-diol + NAD+ + H2O + CO2

741666

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1.14.13.1

4-methylsalicylate + NADH + O2 = 1,2-dihydroxy-4-methylbenzene + CO2 + NAD+ + H2O

657732

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1.13.11.4

2 entries

1.14.13.1

3 entries

1.14.99.15

4-methylsalicylic acid + NADH + O2 = ? + NAD+ + H2O

671746

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Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.18.1

-

699195

-

4.1.1.52

-

4703

-

6.2.1.2

competitive with respect to hexanoate

682

-

6.2.1.27

strong

648909

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Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.4

0.3

-

pH 8.0

698728

1.13.11.4

0.3

-

pH 8.0, temperature not specified in the publication

748157

1.13.11.4

2 entries

1.14.13.1

6.4

-

pH not specified in the publication, 25°C

680483

K_M Value (3 results)

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Show KM Value (3 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.4

0.028

-

pH 8.0

698728

1.13.11.4

0.028

-

pH 8.0, temperature not specified in the publication

748157

1.13.11.4

2 entries

1.14.13.1

0.0158

-

pH not specified in the publication, 25°C

680483

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

6.2.1.27

0.0014

-

pH 7.8, 37°C

648909

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.14.18.1

1.65

-

-

699195

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

682

8937481

Inhibition of a medium chain acyl-CoA synthetase involved in glycine conjugation by carboxylic acids

1996

Kasuya, F.; Igarashi, K.; Fukui, M.

Biochem. Pharmacol.

52

1643-1646

4703

237216

6-Methylsalicylic acid (2,6-cresotic acid) decarboxylase

1975

Light, R.J.; Vogel, G.

Methods Enzymol.

43

530-540

648909

8477728

Enzymes of anarobic metabolism pf phenolic compounds. 4-Hydroxybenzoate-CoA ligase from a denitrifying Pseudomonas species

1993

Biegert, T.; Altenschmidt, U.; Eckerskorn, C.; Fuchs, G.

Eur. J. Biochem.

213

555-561

657732

12565867

Identification of three novel salicylate 1-hydroxylases involved in the phenanthrene degradation of Sphingobium sp. strain P2

2003

Pinyakong, O.; Habe, H.; Yoshida, T.; Nojiri, H.; Omori, T.

Biochem. Biophys. Res. Commun.

301

350-357

671746

16472768

Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris

2006

Bell, S.G.; Hoskins, N.; Xu, F.; Caprotti, D.; Rao, Z.; Wong, L.L.

Biochem. Biophys. Res. Commun.

342

191-196

680483

17172348

A gene cluster involved in degradation of substituted salicylates via ortho cleavage in Pseudomonas sp. strain MT1 encodes enzymes specifically adapted for transformation of 4-methylcatechol and 3-methylmuconate

2007

Camara, B.; Bielecki, P.; Kaminski, F.; dos Santos, V.M.; Plumeier, I.; Nikodem, P.; Pieper, D.H.

J. Bacteriol.

189

1664-1674

684569

17905882

Purification and characterization of a three-component salicylate 1-hydroxylase from Sphingomonas sp. strain CHY-1

2007

Jouanneau, Y.; Micoud, J.; Meyer, C.

Appl. Environ. Microbiol.

73

7515-7521

698728

15220336

Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidize (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans

2004

Hintner, J.P.; Reemtsma, T.; Stolz, A.

J. Biol. Chem.

279

37250-37260

699195

18256890

Quantitative structure-activity relationship studies of mushroom tyrosinase inhibitors

2008

Xue, C.B.; Luo, W.C.; Ding, Q.; Liu, S.Z.; Gao, X.X.

J. Comput. Aided Mol. Des.

22

299-309

741666

26027357

Properties of non-homologous salicylate hydroxylases of Pseudomonas bacteria

2015

Puntus, I.; Vlasova, E.; Sokolov, A.; Zakharchenko, N.; Funtikova, T.

Appl. Biochem. Microbiol.

51

215-221

748157

15220336

Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidize (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans

2004

Hintner, J.P.; Reemtsma, T.; Stolz, A.

J. Biol. Chem.

279

37250-37260

Links to other databases for 4-methylsalicylic acid

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Show Links (1 entry)

ChEBI

PubChem

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