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. 2013 Jun;195(12):2768-75.
doi: 10.1128/JB.00141-13. Epub 2013 Apr 5.

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

Minjiao Chen  1 , Xinyu Ma, Xiaolei Chen, Ming Jiang, Haigang Song, Zhihong Guo
Affiliations

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

Minjiao Chen et al. J Bacteriol. 2013 Jun.

Abstract

Escherichia coli is used as a model organism for elucidation of menaquinone biosynthesis, for which a hydrolytic step from 1,4-dihydroxy-2-naphthoyl-coenzyme A (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate is still unaccounted for. Recently, a hotdog fold thioesterase has been shown to catalyze this conversion in phylloquinone biosynthesis, suggesting that its closest homolog, YbgC in Escherichia coli, may be the DHNA-CoA thioesterase in menaquinone biosynthesis. However, this possibility is excluded by the involvement of YbgC in the Tol-Pal system and its complete lack of hydrolytic activity toward DHNA-CoA. To identify the hydrolytic enzyme, we have performed an activity-based screen of all nine Escherichia coli hotdog fold thioesterases and found that YdiI possesses a high level of hydrolytic activity toward DHNA-CoA, with high substrate specificity, and that another thioesterase, EntH, from siderophore biosynthesis exhibits a moderate, much lower DHNA-CoA thioesterase activity. Deletion of the ydiI gene from the bacterial genome results in a significant decrease in menaquinone production, which is little affected in ΔybgC and ΔentH mutants. These results support the notion that YdiI is the DHNA-CoA thioesterase involved in the biosynthesis of menaquinone in the model bacterium.

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Figures

Fig 1
Fig 1
Biosynthesis of menaquinone (vitamin K2) in Escherichia coli. SHCHC, (1R,6R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate; SEPHCHC, (1R,2S,5S,6S)-2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate; OSB, o-succinylbenzoate; DHNA, 1,4-dihydroxy-2-naphthoate, AdoMet: S-adenosylmethionine; AdoHcy, S-adenosylhomocysteine.
Fig 2
Fig 2
SDS-PAGE of the recombinant hotdog fold thioesterases.
Fig 3
Fig 3
Normalized specific DHNA-CoA thioesterase activity of hotdog fold thioesterases from E. coli. The activity of YdiI is set at 100%. The hydrolytic activities were assayed in 200 mM sodium phosphate buffer, pH 7.0, at 25°C, with the DHNA-CoA concentration set at 100.0 μM.
Fig 4
Fig 4
Contents of ubiquinone and naphthoquinones in the deletion mutants of menaquinone biosynthetic genes or hotdog fold thioesterase genes under anaerobic (A) and aerobic (B) conditions. BW25113 is the parent strain of the deletion mutants. Note that the amount of both naphthoquinones and ubiquinone is arbitrary, assuming that all these quinones are the same as menaquinone-4 in molar absorption coefficient at 245 nm.
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