Chemoenzymatic synthesis of 3-ethyl-2,5-dimethylpyrazine by L-threonine 3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase/L-threonine aldolase
| Autor: | Fumihito Hasebe, Tomoharu Motoyama, Shogo Nakano, Noriyuki Miyoshi, Shigenori Kumazawa, Sohei Ito, Ryo Miyata |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Stereochemistry Reaction intermediate Biochemistry Threonine aldolase activity 03 medical and health sciences chemistry.chemical_compound symbols.namesake 0302 clinical medicine Materials Chemistry Environmental Chemistry Threonine QD1-999 chemistry.chemical_classification DNA ligase biology Aldolase A Acetaldehyde General Chemistry Condensation reaction Chemistry Maillard reaction 030104 developmental biology chemistry symbols biology.protein 030217 neurology & neurosurgery |
| Zdroj: | Communications Chemistry, Vol 4, Iss 1, Pp 1-10 (2021) |
| ISSN: | 2399-3669 |
| DOI: | 10.1038/s42004-021-00545-8 |
| Popis: | Pyrazines are typically formed from amino acids and sugars in chemical reactions such as the Maillard reaction. In this study, we demonstrate that 3-ethyl-2,5-dimethylpyrazine can be produced from L-Thr by a simple bacterial operon. We conclude that EDMP is synthesized chemoenzymatically from L-Thr via the condensation reaction of two molecules of aminoacetone and one molecule of acetaldehyde. Aminoacetone is supplied by L-threonine 3-dehydrogenase using L-Thr as a substrate via 2-amino-3-ketobutyrate. Acetaldehyde is supplied by 2-amino-3-ketobutyrate CoA ligase bearing threonine aldolase activity from L-Thr when CoA was at low concentrations. Considering the rate of EDMP production, the reaction intermediate is stable for a certain time, and moderate reaction temperature is important for the synthesis of EDMP. When the precursor was supplied from L-Thr by these enzymes, the yield of EDMP was increased up to 20.2%. Furthermore, we demonstrate that this reaction is useful for synthesizing various alkylpyrazines. Threonine is a biosynthetic precursor to dimethylpyrazine derivatives, but the pathway by which this occurs is not fully established. Here l-throenine-3-dehydrogenase and 2-amino-3-ketobutyrate CoA ligase together are shown to convert l-threonine to dimethylpyrazine derivatives as a byproduct of glycine metabolism. |
| Databáze: | OpenAIRE |
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