Details

Autor(en) / Beteiligte

• Bisquert, Ricardo
• Planells-Cárcel, Andrés
• Alonso-Del-Real, Javier
• Muñiz-Calvo, Sara
• Guillamón, José Manuel

Titel

The Role of the PAA1 Gene on Melatonin Biosynthesis in Saccharomyces cerevisiae : A Search of New Arylalkylamine N -Acetyltransferases

Ist Teil von

• Microorganisms (Basel), 2023-04, Vol.11 (5), p.1115

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2023

Link zum Volltext

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• Recently, the presence of melatonin in fermented beverages has been correlated with yeast metabolism during alcoholic fermentation. Melatonin, originally considered a unique product of the pineal gland of vertebrates, has been also identified in a wide range of invertebrates, plants, bacteria, and fungi in the last two decades. These findings bring the challenge of studying the function of melatonin in yeasts and the mechanisms underlying its synthesis. However, the necessary information to improve the selection and production of this interesting molecule in fermented beverages is to disclose the genes involved in the metabolic pathway. So far, only one gene has been proposed as involved in melatonin production in , , a polyamine acetyltransferase, a homolog of the vertebrate's aralkylamine -acetyltransferase (AANAT). In this study, we assessed the in vivo function of by evaluating the bioconversion of the different possible substrates, such as 5-methoxytryptamine, tryptamine, and serotonin, using different protein expression platforms. Moreover, we expanded the search for new -acetyltransferase candidates by combining a global transcriptome analysis and the use of powerful bioinformatic tools to predict similar domains to AANAT in . The AANAT activity of the candidate genes was validated by their overexpression in because, curiously, this system evidenced higher differences than the overexpression in their own host Our results confirm that possesses the ability to acetylate different aralkylamines, but AANAT activity does not seem to be the main acetylation activity. Moreover, we also prove that Paa1p is not the only enzyme with this AANAT activity. Our search of new genes detected as a new arylalkylamine -acetyltransferase in . This is the first report that clearly proves the involvement of this enzyme in AANAT activity.