Identification and characterization of piperine synthase from black pepper, Piper nigrum L

Autor: Thomas Vogt, Arianne Schnabel, Benedikt Athmer, Fernando Cotinguiba, Kerstin Manke, Frank Schumacher
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Communications Biology
ISSN: 2399-3642
Popis: 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, piperine (1-piperoyl-piperidine) with the human TRPV-1 or vanilloid receptor. We now identify 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 gene family in black pepper. They can be used to facilitate the microbial production of a broad range of medicinally relevant aliphatic and aromatic piperamides based on a wide array of CoA-donors and amine-derived acceptors, offering widespread applications.
Schnabel et al. identify and characterize piperine synthase in developing black pepper fruits which catalyses the formation of piperine from piperoyl coenzyme A and piperidine. A member of BAHD-type acyltransferases, this enzyme can be useful for bio-production of a broad range of medicinally relevant piperamides.
Databáze: OpenAIRE