The Enzyme Database

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EC 3.1.2.28     
Accepted name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Reaction: 1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA
For diagram of vitamin K biosynthesis, click here
Other name(s): menI (gene name); ydiL (gene name)
Systematic name: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
Comments: 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Muller, W. and Leistner, E. 1,4-Naphthoquinone, an intermediate in juglone (5-hydroxy-1,4-naphthoquinone) biosynthesis. Phytochemistry 15 (1976) 407–410.
2.  Eichinger, D., Bacher, A., Zenk, M.H. and Eisenreich, W. Quantitative assessment of metabolic flux by 13C NMR analysis. Biosynthesis of anthraquinones in Rubia tinctorum. J. Am. Chem. Soc. 121 (1999) 7469–7475.
3.  Widhalm, J.R., van Oostende, C., Furt, F. and Basset, G.J. A dedicated thioesterase of the Hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. Proc. Natl. Acad. Sci. USA 106 (2009) 5599–5603. [PMID: 19321747]
4.  Chen, M., Ma, X., Chen, X., Jiang, M., Song, H. and Guo, Z. Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. J. Bacteriol. 195 (2013) 2768–2775. [PMID: 23564174]
[EC 3.1.2.28 created 2010]
 
 


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