TOMT

Last update 08 May 2025

Basic Info

Synonyms

Catechol O-methyltransferase 2, COMT2, LRTOMT

+ [3]

Introduction

Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones (By similarity). Required for auditory function (PubMed:18794526). Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity (By similarity).

100 Clinical Results associated with TOMT

100 Translational Medicine associated with TOMT

0 Patents (Medical) associated with TOMT

Literatures (Medical) associated with TOMT

20 Sep 2024·ACS Synthetic Biology

Pathway-Adapted Biosensor for High-Throughput Screening of O-Methyltransferase and its Application in Vanillin Synthesis

Article

Author: Huo, Yi-Xin ; Guo, Shuyuan ; Sun, Lichao ; Fan, Yunjuan ; Dong, Pengyu

Vanillin is a widely used flavoring compound in the food, pharmaceutical, and cosmetics area. However, the biosynthesis of vanillin from low-cost shikimic acid is significantly hindered by the low activity of the rate-limiting enzyme, caffeate O-methyltransferase (COMT). To screen COMT variants with improved conversion rates, we designed a biosensing system that is adaptable to the COMT-mediated vanillin synthetic pathway. Through the evolution of aldehyde transcriptional factor YqhC, we obtained a dual-responsive variant, MuYqhC, which positively responds to the product and negatively responds to the substrate, with no response to intermediates. Using the MuYqhC-based vanillin biosensor, we successfully identified a COMT variant, Mu176, that displayed a 7-fold increase in the conversion rate compared to the wild-type COMT. This variant produced 2.38 mM vanillin from 3 mM protocatechuic acid, achieving a conversion rate of 79.33%. The enhanced activity of Mu176 was attributed to an enlarged binding pocket and strengthened substrate interaction. Applying Mu176 to Bacillus subtilis increased the level of vanillin production from shikimic acid by 2.39-fold. Further optimization of the production chassis, increasing the S-adenosylmethionine supply and the precursor concentration, elevated the vanillin titer to 1 mM, marking the highest level of vanillin production from shikimic acid in Bacillus. Our work highlights the significance of the MuYqhC-based biosensing system and the Mu176 variant in vanillin production.

15 May 2024·Journal of Agricultural and Food Chemistry

Novel Catechol O-methyltransferases from Lentinula edodes Catalyze the Generation of Taste-Active Flavonoids

Article

Author: Ley, Jakob P ; Zorn, Holger ; Kanter, Jean-Philippe ; Biabani, Ali ; Gand, Martin ; Milke, Lars ; Metz, Judith K ; Schlüter, Hartmut

Due to the increasing demand for natural food ingredients, including taste-active compounds, enzyme-catalyzed conversions of natural substrates, such as flavonoids, are promising tools to align with the principles of Green Chemistry. In this study, a novel O-methyltransferase activity was identified in the mycelium of Lentinula edodes, which was successfully applied to generate the taste-active flavonoids hesperetin, hesperetin dihydrochalcone, homoeriodictyol, and homoeriodictyol dihydrochalcone. Furthermore, the mycelium-mediated OMT activity allowed for the conversion of various catecholic substrates, yielding their respective (iso-)vanilloids, while monohydroxylated compounds were not converted. By means of a bottom-up proteomics approach, three putative O-methyltransferases were identified, and subsequently, synthetic, codon-optimized genes were heterologously expressed in Escherichia coli. The purified enzymes confirmed the biocatalytic O-methylation activity against targeted flavonoids containing catechol motifs.

01 Dec 2023·Synthetic and Systems Biotechnology

Methylation in hangtaimycin biosynthesis and its antibacterial activities

Article

Author: Deng, Zixin ; Sun, Yuhui ; Dong, Yulu ; Luo, Minghe

About two-thirds of small molecule drugs contain methyl group and it plays a very important role in the drug development. So, methyltransferases catalyzing the methylation have always attracted great attention. Hangtaimycin (HTM) is a potent hepatoprotective agent. Previous study showed that its biosynthetic gene cluster contained three methyltransferase domains, but their characteristics in HTM biosynthetic pathway has not been revealed. In this study, we clarified multi-methylations in HTM biosynthesis in vivo. It showed that the two S-adenosylmethionine-dependent methyltransferases (SAM-MTs) of HtmA2(-module 6)-MT domain and HtmB2(-module 18)-MT domain are responsible for the installation of methyl group at C-45 and N-12, respectively, whereas the FK506 methyltransferase (FKMT) type O-methyltransferase of HtmB1(-module 16)-MT domain take care of the methylation at O-21 of HTM. We also reported the antibacterial activities of HTM in this study, and found that it showed activities against M. luteus, B. thuringiensis and A. baumannii with MIC of 4 μg/mL, 4 μg/mL, and 64 μg/mL, respectively.

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TOMT

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