Entry |
|
Name |
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
menI (gene name);
ydiL (gene name)
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Class |
Hydrolases;
Acting on ester bonds;
Thioester hydrolases
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Sysname |
1,4-dihydroxy-2-naphthoyl-CoA hydrolase
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Reaction(IUBMB) |
1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA [RN: R07262]
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Reaction(KEGG) |
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Substrate |
1,4-dihydroxy-2-naphthoyl-CoA [CPD: C15547];
H2O [CPD: C00001]
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Product |
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Comment |
This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3].
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History |
EC 3.1.2.28 created 2010
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Pathway |
ec00130 | Ubiquinone and other terpenoid-quinone biosynthesis |
ec01110 | Biosynthesis of secondary metabolites |
|
Orthology |
K12073 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase |
K19222 | 1,4-dihydroxy-2-naphthoyl-CoA hydrolase |
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Genes |
» show all
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Reference |
1 |
Authors |
Muller, W. and Leistner, E. |
Title |
1,4-Naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis. |
Journal |
Phytochemistry 15:407-410 (1976) |
Reference |
2 |
Authors |
Eichinger, D., Bacher, A., Zenk, M.H. and Eisenreich, W. |
Title |
Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum. |
Journal |
J Am Chem Soc 121:7469-7475 (1999) |
Reference |
|
Authors |
Widhalm JR, van Oostende C, Furt F, Basset GJ |
Title |
A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. |
Journal |
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Sequence |
|
Reference |
|
Authors |
Chen M, Ma X, Chen X, Jiang M, Song H, Guo Z |
Title |
Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 3.1.2.28 |
ExPASy - ENZYME nomenclature database: | 3.1.2.28 |
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