Enzymatic Cascade in Pseudomonas that Produces Pyrazine from α-Amino Acids
| Autor: | Hajime Minakawa, Naoki Takaya, Tomohito Namai, Shunsuke Masuo, Yusuke Tsuda, Ryosuke Shigemoto |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Amine oxidase
Pyrazine Stereochemistry Pseudomonas fluorescens 010402 general chemistry medicine.disease_cause 01 natural sciences Biochemistry chemistry.chemical_compound Acetyltransferases medicine Amino Acids Molecular Biology Escherichia coli chemistry.chemical_classification Oxidase test biology Molecular Structure 010405 organic chemistry Organic Chemistry biology.organism_classification 0104 chemical sciences Amino acid Enzyme chemistry Pyrazines Molecular Medicine Heterologous expression Oxidoreductases |
| Zdroj: | Chembiochem : a European journal of chemical biology. 21(3) |
| ISSN: | 1439-7633 |
| Popis: | Pyrazines are widespread chemical compounds that include pheromones and odors. Herein, a novel mechanism used by Pseudomonas fluorescens SBW25 to biosynthesize monocyclic pyrazines is reported. Heterologous expression of the papABC genes that synthesize the natural α-amino acid 4-aminophenylalanine (4APhe), together with three adjacent papDEF genes of unknown function, in Escherichia coli resulted in the production of 2,5-dimethyl-3,6-bis(4-aminobenzyl)pyrazine (DMBAP), which comprised two symmetrical aminobenzyl moieties derived from 4APhe. It is found that PapD is a novel amino acid C-acetyltransferase, which decarboxylates and transfers acetyl residues to 4APhe, to generate an α-aminoketone, which spontaneously dehydrates and condenses to give dihydro DMBAP. PapF is a novel oxidase in the amine oxidase superfamily that oxidizes dihydro DMBAP to yield the pyrazine ring of DMBAP. These two enzymes constitute a unique mechanism for synthesizing monocyclic pyrazines and might serve as a novel strategy for the enzymatic synthesis of pyrazine derivatives from natural α-amino acids. |
| Databáze: | OpenAIRE |
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