Nature communications biology radar - feb 2021

Abstract: Black pepper (Piper nigrum L.) is the world’s most popular spice and is also used as an ingredient in traditional medicine. Its pungent perception is due to the interaction of its major compound, 1-piperoyl-piperidine (piperine) with the human TRPV-1 or vanilloid receptor. We now identified the hitherto concealed enzymatic formation of piperine from piperoyl coenzyme A and piperidine based on a differential RNA-Seq approach from developing black pepper fruits. This enzyme is described as piperine synthase (piperoyl-CoA:piperidine piperoyl transferase) and is a member of the BAHD-type of acyltransferases encoded by a gene that is preferentially expressed in immature fruits. A second BAHD-type enzyme, also highly expressed in immature black pepper fruits has a rather promiscuous substrate specificity combining diverse CoA-esters with aliphatic and aromatic amines with similar efficiencies, and was termed piperamide synthase. Recombinant piperine and piperamide synthases are members of a small BAHD-gene family in black pepper. They can be used to facilitate the microbial production of a broad range of medicinally relevant aliphatic and aromatic amides piperamides based on a wide array CoA-donors and amine-derived acceptors offering widespread applications.

Cite this as

Schnabel, Arianne, Athmer, Benedikt, Manke, Kerstin, Schumacher, Frank, Cotinguiba, Fernando, Vogt, Thomas (2021). Dataset: Nature communications biology radar - feb 2021. https://doi.org/10.22000/400

DOI retrieved: 2021

Additional Info

Field Value
Imported on January 12, 2023
Last update November 28, 2024
License CC BY-SA 4.0 Attribution-ShareAlike
Source https://doi.org/10.22000/400
Author Schnabel, Arianne
Given Name Arianne
Family Name Schnabel
More Authors
Athmer, Benedikt
Manke, Kerstin
Schumacher, Frank
Cotinguiba, Fernando
Vogt, Thomas
Source Creation 2021
Publishers
Vogt, Thomas
Production Year 2021
Publication Year 2021
Resource Type Dataset - chromatograms, Excel files, raw data
Subject Areas
Name: Biochemistry