<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>6</volume><submitter>Leal AR</submitter><pubmed_abstract>The widespread presence of pepsin-like enzymes in eukaryotes together with their relevance in the control of multiple biological processes is reflected in the large number of studies published so far for this family of enzymes. By contrast, pepsin homologs from bacteria have only recently started to be characterized. The work with recombinant shewasin A from Shewanella amazonensis provided the first documentation of this activity in prokaryotes. Here we extend our studies to shewasin D, the pepsin homolog from Shewanella denitrificans, to gain further insight into this group of bacterial peptidases that likely represent ancestral versions of modern eukaryotic pepsin-like enzymes. We demonstrate that the enzymatic properties of recombinant shewasin D are strongly reminiscent of eukaryotic p</pubmed_abstract><journal>Scientific reports</journal><pagination>23869</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4814920</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Enzymatic properties, evidence for in vivo expression, and intracellular localization of shewasin D, the pepsin homolog from Shewanella denitrificans.</pubmed_title><pmcid>PMC4814920</pmcid><pubmed_authors>Cruz R</pubmed_authors><pubmed_authors>Faro C</pubmed_authors><pubmed_authors>Simoes I</pubmed_authors><pubmed_authors>Faro R</pubmed_authors><pubmed_authors>Leal AR</pubmed_authors><pubmed_authors>Wlodawer A</pubmed_authors><pubmed_authors>Huesgen PF</pubmed_authors><pubmed_authors>Manadas B</pubmed_authors><pubmed_authors>Bur D</pubmed_authors></additional><is_claimable>false</is_claimable><name>Enzymatic properties, evidence for in vivo expression, and intracellular localization of shewasin D, the pepsin homolog from Shewanella denitrificans.</name><description>The widespread presence of pepsin-like enzymes in eukaryotes together with their relevance in the control of multiple biological processes is reflected in the large number of studies published so far for this family of enzymes. By contrast, pepsin homologs from bacteria have only recently started to be characterized. The work with recombinant shewasin A from Shewanella amazonensis provided the first documentation of this activity in prokaryotes. Here we extend our studies to shewasin D, the pepsin homolog from Shewanella denitrificans, to gain further insight into this group of bacterial peptidases that likely represent ancestral versions of modern eukaryotic pepsin-like enzymes. We demonstrate that the enzymatic properties of recombinant shewasin D are strongly reminiscent of eukaryotic p</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Mar</publication><modification>2026-04-14T21:21:25.069Z</modification><creation>2019-03-27T03:10:44Z</creation></dates><accession>S-EPMC4814920</accession><cross_references><pubmed>27029611</pubmed><doi>10.1038/srep23869</doi></cross_references></HashMap>