Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractVOCCluster: Untargeted Metabolomics Feature Clustering Approach for Clinical Breath Gas Chromatography/Mass Spectrometry Data    Next AbstractSpecies recognition elicited by differences in composition of the genital sex pheromone in Dermacentor variabilis and D. andersoni (Acari: Ixodidae) »

J Fungi (Basel)


Title:Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi
Author(s):Alkin N; Dunaevsky Y; Elpidina E; Beljakova G; Tereshchenkova V; Filippova I; Belozersky M;
Address:"Biological Faculty, Lomonosov Moscow State University, 119991 Moscow, Russia. A.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia. Chemical Faculty, Lomonosov Moscow State University, 119991 Moscow, Russia"
Journal Title:J Fungi (Basel)
Year:2021
Volume:20210910
Issue:9
Page Number: -
DOI: 10.3390/jof7090744
ISSN/ISBN:2309-608X (Electronic) 2309-608X (Linking)
Abstract:"Proline-specific peptidases (PSP) play a crucial role in the processing of fungal toxins, pheromones, and intracellular signaling. They are of particular interest to biotechnology, as they are able to hydrolyze proline-rich oligopeptides that give a bitter taste to food and can also cause an autoimmune celiac disease. We performed in silico analysis of PSP homologs in the genomes of 42 species of higher fungi which showed the presence of PSP homologs characteristic of various kingdoms of living organisms and belonging to different families of peptidases, including homologs of dipeptidyl peptidase 4 (DPP4) and prolyl aminopeptidase 1 found in almost all the studied fungal species. Homologs of proliniminopeptidases from the S33 family absent in humans were also found. Several studied homologs are characteristic of certain taxonomic groups of fungi. Phylogenetic analysis suggests a duplication of ancestral DPP4 into transmembrane and secreted versions, which predate the split of ascomycete and basidiomycete lineages. Comparative biochemical analysis of DPP4 in alkaliphilic and alkali-tolerant strains of fungi showed that, notwithstanding some individual features of these enzymes, in both cases, the studied DPP4 are active and stable under alkaline conditions and at high salt concentrations, which makes them viable candidates for biotechnology and bioengineering"
Keywords:alkaliphilic and alkali-tolerant fungi ascomycetes basidiomycetes bioinformatic analysis proline-specific peptidases secretion;
Notes:"PubMed-not-MEDLINEAlkin, Nikita Dunaevsky, Yakov Elpidina, Elena Beljakova, Galina Tereshchenkova, Valeria Filippova, Irina Belozersky, Mikhail eng 19-04-00852-a/Russian Foundation for Fundamental Investigations/ Switzerland 2021/09/29 J Fungi (Basel). 2021 Sep 10; 7(9):744. doi: 10.3390/jof7090744"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 27-12-2024