Origins of peptidases

Abstract

a b s t r a c tThe distribution of all peptidase homologues across all phyla of organisms was analysed to determine within which kingdom each of the 271 families originated. No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methionyl aminopeptides are missing from some clades. There are 33 peptidase families common to archaea, bacteria and eukaryotes and are assumed to have originated in the last universal common ancestor (LUCA). These include peptidases with different catalytic types, exo-and endopeptidases, peptidases with different tertiary structures and peptidases from different families but with similar structures. This implies that the different catalytic types and structures pre-date LUCA. Other families have had their origins in the ancestors of viruses, archaea, bacteria, fungi, plants and animals, and a number of families have had their origins in the ancestors of particular phyla. The evolution of peptidases is compared to recent hypotheses about the evolution of organisms.

Disruption of a C69-Family Cysteine Dipeptidase Gene Enhances Heat Shock and UV-B Tolerances in Metarhizium acridum

“…Function reports of dipeptidases are mostly limited to virulence and growth in microorganisms, while there is little information regarding the effect of dipeptidases on stress tolerance in microorganisms. Family C69 dipeptidase is strictly distributed in fungi to ascomycetes (Rawlings and Bateman, 2019). Few studies were reported on PepDA in microorganisms and no functional analysis has been reported in fungi.…”

“…Peptidases (EC 3.4) are a class of enzymes to hydrolyze peptide chain to oligopeptides and single amino acids (Barrett, 1994). Peptidases can be classified into 261 families by catalytic mechanism as serine, cysteine, aspartyl, threonine, glutamic, or metallopeptidases (Rawlings and Bateman, 2019). For example, peptidases in which the nucleophile that attacks the scissile peptide bond is the sulfhydryl group of a cysteine residue are designated as cysteine-type peptidases (Rawlings et al, 2011;Barrett and Rawlingsm, 2013).…”

“…For example, peptidases in which the nucleophile that attacks the scissile peptide bond is the sulfhydryl group of a cysteine residue are designated as cysteine-type peptidases (Rawlings et al, 2011;Barrett and Rawlingsm, 2013). The clans and families of cysteine peptidases were summarized in the review (Rawlings and Bateman, 2019).…”

“…Dipeptidase A (PepDA) belongs to the cysteine peptidase family C69, which was evolutionarily conserved and found in 14 bacterial phyla and some eukaryotes. In fungi, the PepDA only existed in ascomycetes (Rawlings and Bateman, 2019). Family C69 dipeptidase was first characterized in Lactobacillus farciminis, showing an extremely strict substrate specificity (Sakamoto et al, 2013).…”

Digestive Hydrolases of Wheat Bugs: Properties, Significance and Possible Ways to Limit Their Activity

“…Протеазы играют ряд важнейших функций во всех живых организмах, и на долю кодирующих их генов приходится около 2 % от общего числа генов (Barrett et al, 2001;Rawlings et al,2004;Rawlings and Bateman, 2019). Пищеварительные протеазы, осуществляющие гидролиз пептидных связей в белках пищи, обеспечивают насекомых, как и другие организмы, аминокислотами -мономерами для построения собственных белков, а дефицит необходимых аминокислот ведет к негативным последствиям, вплоть до летального исхода.…”