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Ligand 1,4-dihydroxy-2-naphthoyl-CoA

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 1,4-dihydroxy-2-naphthoyl-CoA

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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

3.1.2.28

1,4-dihydroxy-2-naphthoyl-CoA + H2O = CoA + 1,4-dihydroxy-2-naphthoate

706538

-

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

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.36

o-succinylbenzoate + CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O

0

-

4.1.3.36

o-succinylbenzoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O

0

-

4.1.3.36

2 entries

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.2.28

1,4-dihydroxy-2-naphthoyl-CoA + H2O = CoA + 1,4-dihydroxy-2-naphthoate

729928, 730609, 706538

-

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.3.36

2-succinylbenzoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O

0

-

4.1.3.36

o-succinylbenzoate + CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O

0

-

4.1.3.36

o-succinylbenzoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O

0, 93962, 93958, 93960, 93959

-

4.1.3.36

3 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.1.2.28

0.13

-

pH 7.0, 25°C

729928

3.1.2.28

6.2

-

pH 7.0, 25°C

729928

3.1.2.28

2 entries

K_M Value (2 results)

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Show KM Value (2 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.1.2.28

0.0025

-

pH 7.0, 25°C

729928

3.1.2.28

0.033

-

pH 7.0, 25°C

729928

3.1.2.28

2 entries

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

93958

500558

Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes

1979

Meganathan, R.; Bentley, R.

J. Bacteriol.

140

92-98

93959

2966501

4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis

1987

Kolkmann, R.; Leistner, E.

Z. Naturforsch. C

42

1207-1214

93960

7262311

Enzymatic synthesis of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis

1981

Heide, L.; Leistner, E.

FEBS Lett.

128

201-204

93962

7045104

Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis

1982

Heide, L.; Arendt, S.; Leistner, E.

J. Biol. Chem.

257

7396-7400

706538

19321747

A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1

2009

Widhalm, J.R.; van Oostende, C.; Furt, F.; Basset, G.J.

Proc. Natl. Acad. Sci. USA

106

5599-5603

729928

23564174

Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli

2013

Chen, M.; Ma, X.; Chen, X.; Jiang, M.; Song, H.; Guo, Z.

J. Bacteriol.

195

2768-2775

730609

22372525

Phylloquinone (vitamin K(1)) biosynthesis in plants: two peroxisomal thioesterases of Lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl-CoA

2012

Widhalm, J.R.; Ducluzeau, A.L.; Buller, N.E.; Elowsky, C.G.; Olsen, L.J.; Basset, G.J.

Plant J.

71

205-215

Links to other databases for 1,4-dihydroxy-2-naphthoyl-CoA

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ChEBI

PubChem