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Ligand 1-hydroxy-2-naphthoic acid

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.38

1-hydroxy-2-naphthoate + O2 = (3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

639268, 698710

-

1.13.11.38

1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

725836, 724021

-

1.13.11.38

1-hydroxy-2-naphthoic acid + O2 = 2-carboxybenzylpyruvic acid

705566

-

1.14.13.135

1-hydroxy-2-naphthoate + NAD(P)H + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2

715057

-

1.14.13.135

1-hydroxy-2-naphthoate + NADH + O2 = 1,2-dihydroxynaphthalene + NAD+ + H2O + CO2

712039

-

1.14.13.135

1-hydroxy-2-naphthoate + NADPH + O2 = 1,2-dihydroxynaphthalene + NADP+ + H2O + CO2

712039

-

1.13.11.38

3 entries

1.14.13.135

3 entries

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.38

1-hydroxy-2-naphthoate + O2 = (3E)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

639268, 639269, 698710, 698556

-

1.13.11.38

1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

705566, 725836, 724021

-

1.13.11.38

1-hydroxy-2-naphthoate + O2 = ?

698560

-

1.13.11.38

1-hydroxy-2-naphthoic acid + O2 = 2-carboxybenzylpyruvic acid

705566

-

1.13.11.38

4 entries

1.13.11.4

1-hydroxy-2-naphthoate + O2 = ?

698560, 724975, 672692

3nkt, 3D-view

1.13.11.86

1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate

748114

-

1.14.13.1

1-hydroxy-2-naphthoate + NADH + 2 H+ + O2 = ?

684569

-

1.14.13.1

1-hydroxy-2-naphthoate + NADH + H+ + O2 = ?

741666

-

1.14.13.1

1-hydroxy-2-naphthoate + NADH + O2 = 1,2-dihydroxynaphthalene + CO2 + H2O + NAD+

390017

-

1.14.13.135

1-hydroxy-2-naphthoate + NAD(P)H + O2 = 1,2-dihydroxynaphthalene + NAD(P)+ + H2O + CO2

715057

-

1.14.13.135

1-hydroxy-2-naphthoate + NADH + O2 = 1,2-dihydroxynaphthalene + NAD+ + H2O + CO2

712039

-

1.14.13.135

1-hydroxy-2-naphthoate + NADPH + O2 = 1,2-dihydroxynaphthalene + NADP+ + H2O + CO2

712039

-

1.14.13.1

3 entries

1.14.13.135

3 entries

2.5.1.74

farnesyl diphosphate + 1-hydroxy-2-naphthoate = 2-farnesyl-1-naphthol + phosphate + CO2

698675

-

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.2.28

1-hydroxy-2-naphthoyl-CoA + H2O = CoA + 1-hydroxy-2-naphthoate

0

-

Inhibitor in Enzyme-catalyzed Reactions (4 results)

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Show Inhibitors (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.38

substrate inhibition

705566

-

1.13.11.4

0.33 mM, 19% of wild type enzyme activity remaining

672692

3nkt, 3D-view

1.14.13.1

strong competitive inhibition of salicylate hydroxylation

684569

-

5.1.2.2

reversible

285171

-

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

1.13.11.4

3nkt, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (13 results)

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Show Turnover Number (13 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.13.11.38

2.2

-

pH 8.0, temperature not specified in the publication, mutant L38Q

725836

1.13.11.38

3.31

-

pH 8.0, temperature not specified in the publication, mutant A85H

725836

1.13.11.38

4.6

-

pH 8.0, temperature not specified in the publication, mutant W104Y

725836

1.13.11.38

17

-

pH 8.0, temperature not specified in the publication, mutant M46V

725836

1.13.11.38

24

-

pH 8.0, temperature not specified in the publication, wild-type enzyme

725836

1.13.11.38

44

-

-

698560

1.13.11.38

70.4

-

-

705566

1.13.11.38

114

-

-

639268

1.13.11.38

114

-

pH 7.5, 25°C

698710

1.13.11.4

0.565

-

-

672692

1.13.11.4

6.08

-

-

672692

1.13.11.4

24

-

wild-type enzyme, pH and temperature not specified in the publication

724975

1.13.11.4

44

-

-

698560

1.13.11.38

9 entries

1.13.11.4

4 entries

K_M Value (15 results)

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Show KM Value (15 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.38

0.01

-

-

639268

1.13.11.38

0.01

-

pH 7.5, 25°C

698710

1.13.11.38

0.0135

-

-

705566

1.13.11.38

0.046

-

pH 8.0, temperature not specified in the publication, mutant M46V

725836

1.13.11.38

0.08

-

pH 8.0, temperature not specified in the publication, mutant A85H

725836

1.13.11.38

0.08

-

pH 8.0, temperature not specified in the publication, mutant L38Q

725836

1.13.11.38

0.134

-

-

698560

1.13.11.38

0.14

-

pH 8.0, temperature not specified in the publication, wild-type enzyme

725836

1.13.11.38

0.144

-

pH 8.0, temperature not specified in the publication, mutant W104Y

725836

1.13.11.4

0.0209

-

-

672692

1.13.11.4

0.134

-

-

698560

1.13.11.4

0.14

-

wild-type enzyme, pH and temperature not specified in the publication

724975

1.13.11.38

9 entries

1.13.11.4

3 entries

1.14.13.1

0.004

-

-

390017

1.14.13.135

0.0716

-

pH 7.5, 30°C, with NADH

712039

1.14.13.135

0.0755

-

pH 7.5, 30°C, with NADPH

712039

1.14.13.135

2 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.13.11.38

0.116

-

substrate inhibition

705566

1.14.13.1

0.00068

-

30°C, pH 7.0

684569

References & Links

Literature References (18)

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Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285171

386722

Mandelate racemase

1979

Kenyon, G.L.; Hegeman, G.D.

Adv. Enzymol. Relat. Areas Mol. Biol.

50

325-360

390017

11826899

Purification and characterization of a salicylate hydroxylase involved in 1-hydroxy-2-naphthoic acid hydroxylation from the naphthalene and phenanthrene-degrading bacterial strain Pseudomonas putida BS202-P1

2001

Balashova, N.V.; Stolz, A.; Knackmuss, H.J.; Kosheleva, I.A.; Naumov, A.V.; Boronin, A.M.

Biodegradation

12

179-188

639268

9335300

Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7

1997

Iwabuchi, T.; Harayama, S.

J. Bacteriol.

179

6488-6494

639269

6833175

Phthalate pathway of phenanthrene metabolism: formation of 2-carboxybenzalpyruvate

1983

Barnsley, E.A.

J. Bacteriol.

154

113-117

672692

17213679

Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W

2007

Hirano, S.; Morikawa, M.; Takano, K.; Imanaka, T.; Kanaya, S.

Biosci. Biotechnol. Biochem.

71

192-199

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

698556

9922237

Structure of the ring cleavage product of 1-hydroxy-2-naphthoate, an intermediate of the phenanthrene-degradative pathway of Nocardioides sp. strain KP7

1999

Adachi, K.; Iwabuchi, T.; Sano, H.; Harayama, S.

J. Bacteriol.

181

757-763

698560

11698383

Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudaminobacter salicylatoxidans

2001

Hintner, J.P.; Lechner, C.; Riegert, U.; Kuhm, A.E.; Storm, T.; Reemtsma, T.; Stolz, A.

J. Bacteriol.

183

6936-6942

698675

7275947

Biosynthesis of menaquinones. Enzymic prenylation of 1,4-dihydroxy-2-naphthoate by Micrococcus luteus membrane fractions

1981

Saito, Y.; Ogura, K.

J. Biochem.

89

1445-1452

698710

9525941

Biochemical and molecular characterization of 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7

1998

Iwabuchi, T.; Harayama, S.

J. Biol. Chem.

273

8332-8336

705566

19574301

Biodegradation of phenanthrene by Pseudomonas sp. strain PPD: purification and characterization of 1-hydroxy-2-naphthoic acid dioxygenase

2009

Deveryshetty, J.; Phale, P.S.

Microbiology

155

3083-3091

712039

20727010

Biodegradation of phenanthrene by Alcaligenes sp. strain PPH: partial purification and characterization of 1-hydroxy-2-naphthoic acid hydroxylase

2010

Deveryshetty, J.; Phale, P.S.

FEMS Microbiol. Lett.

311

93-101

715057

21545490

A catabolic pathway for the degradation of chrysene by Pseudoxanthomonas sp. PNK-04

2011

Nayak, A.S.; Sanjeev Kumar, S.; Santosh, Kumar, M.; Anjaneya, O.; Karegoudar, T.B.

FEMS Microbiol. Lett.

320

128-134

724021

22101055

Heterologous expression and characterization of two 1-hydroxy-2-naphthoic acid dioxygenases from Arthrobacter phenanthrenivorans

2012

Vandera, E.; Kavakiotis, K.; Kallimanis, A.; Kyrpides, N.C.; Drainas, C.; Koukkou, A.I.

Appl. Environ. Microbiol.

78

621-627

724975

23384287

The salicylate 1,2-dioxygenase as a model for a conventional gentisate 1,2-dioxygenase: crystal structures of the G106A mutant and its adducts with gentisate and salicylate

2013

Ferraroni, M.; Matera, I.; Buerger, S.; Reichert, S.; Steimer, L.; Scozzafava, A.; Stolz, A.; Briganti, F.

FEBS J.

280

1643-1652

725836

22960182

The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase - rational design of mutants and the crystal structures of the A85H and W104Y variants

2012

Ferraroni, M.; Steimer, L.; Matera, I.; Buerger, S.; Scozzafava, A.; Stolz, A.; Briganti, F.

J. Struct. Biol.

180

563-571

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

748114

29038259

Novel Gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme

2018

Yu, H.; Zhao, S.; Guo, L.

J. Bacteriol.

200

e00395-17

Links to other databases for 1-hydroxy-2-naphthoic acid

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Show Links (1 entry)

ChEBI

PubChem