IntEnz

EC 4.1.3.36 - 1,4-dihydroxy-2-naphthoyl-CoA synthase

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IntEnz Enzyme Nomenclature
EC 4.1.3.36

Names

Accepted name:

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

Other names:

1,4-dihydroxy-2-naphthoate synthase
dihydroxynaphthoate synthase
dihydroxynaphthoic acid synthetase
DHNA synthetase
o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing)
naphthoate synthase
MenB
o-succinylbenzoyl-CoA dihydratase (cyclizing)

Systematic name:

4-(2-carboxyphenyl)-4-oxobutanoyl-CoA dihydratase (cyclizing)

Reaction

26562 [IUBMB]

2-succinylbenzoyl-CoA

2-succinylbenzoyl-CoA

Name origin: UniProt - CHECKED (C)

CHEBI:57364

Formula: C32H39N7O20P3S
Charge: -5

ChEBI compound status: CHECKED (C)

+

H⁺

H(+)

Name origin: UniProt - CHECKED (C)

CHEBI:15378

Formula: H
Charge: 1

ChEBI compound status: CHECKED (C)

=

1,4-dihydroxy-2-naphthoyl-CoA

1,4-dihydroxy-2-naphthoyl-CoA

Name origin: UniProt - CHECKED (C)

CHEBI:58897

Formula: C32H38N7O19P3S
Charge: -4

ChEBI compound status: CHECKED (C)

+

H₂O

H2O

Name origin: UniProt - CHECKED (C)

CHEBI:15377

Formula: H2O
Charge: 0

ChEBI compound status: CHECKED (C)

Comments:

This enzyme is involved in the synthesis of 1,4-dihydroxy-2-naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K₂, in bacteria), phylloquinone (vitamin K₁ in plants), and many plant pigments. The coenzyme A group is subsequently removed from the product by EC 3.1.2.28, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway

Protein domains and families: PROSITE:PDOC00150

Structural data: CSA , EC2PDB

Gene Ontology: GO:0008935

CAS Registry Number: 61328-42-5

UniProtKB/Swiss-Prot: (21) [show] [UniProt]

References

Meganathan, R., Bentley, R.

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

J. Bacteriol. 140: 92-98 (1979). [PMID: 500558]
Kolkmann, R., Leistner, E.

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

Z. Naturforsch. C: Biosci. 42: 1207-1214 (1987). [PMID: 2966501]
Johnson, T. W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I. R., Bryant, D. A., Jones, A. D., Golbeck, J. H., Chitnis, P. R.

Recruitment of a foreign quinone into the A₁ site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803.

J. Biol. Chem. 275: 8523-8530 (2000). [PMID: 10722690]
Truglio, J. J., Theis, K., Feng, Y., Gajda, R., Machutta, C., Tonge, P. J., Kisker, C.

Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K₂ biosynthesis.

J. Biol. Chem. 278: 42352-42360 (2003). [PMID: 12909628]

[EC 4.1.3.36 created 1992, modified 2010]

EC 4 - Lyases