{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86749"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86749","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"A Comparative Study of the Substrate Specificities of Peptidases A, B, and N From Salmonella Typhimurium","abstract":"To understand the function of Peptidase B (PepB) we have sequenced the pepB gene and purified its product. Two other peptidases, PepA and PepN, have also been purified to compare their substrate specificities with PepB. PepB has been assigned to the M17 family of peptidases on the basis of similarities in amino acid sequence and biochemical properties. PepB is a broad specificity aminopeptidase with a unique ability to remove Asp residues and a very efficient ability to remove Glu residues from the N-termini of peptides in than PepA and PepN. PepA, on the other hand, removes Pro residues, a function lacking in PepB and PepN. PepN has the unique ability of removing Gly residues from the N-terminus of peptides. The removal of amino acids from the N-terminus is also dependent on what kind of amino acid is present in the second position of the peptides. Neither PepA, PepB, nor PepN are processive in hydrolyzing their substrates. We have demonstrated the cooperation of PepA, PepB, and PepN in hydrolyzing some of their substrates.","abstract_html":"To understand the function of Peptidase B (PepB) we have sequenced the pepB gene and purified its product. Two other peptidases, PepA and PepN, have also been purified to compare their substrate specificities with PepB. PepB has been assigned to the M17 family of peptidases on the basis of similarities in amino acid sequence and biochemical properties. PepB is a broad specificity aminopeptidase with a unique ability to remove Asp residues and a very efficient ability to remove Glu residues from the N-termini of peptides in than PepA and PepN. PepA, on the other hand, removes Pro residues, a function lacking in PepB and PepN. PepN has the unique ability of removing Gly residues from the N-terminus of peptides. The removal of amino acids from the N-terminus is also dependent on what kind of amino acid is present in the second position of the peptides. Neither PepA, PepB, nor PepN are processive in hydrolyzing their substrates. We have demonstrated the cooperation of PepA, PepB, and PepN in hydrolyzing some of their substrates.","abstract_has_math":false,"creators":["Mathew, Zacharia"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Miller, Charles G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:48Z","date_published":"2015-09-28T15:17:48Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9953090"],"render_values":[{"text":"(MiAaPQ)AAI9953090","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86749","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Miller, Charles G."]},{"key":"dc:creator","label":"Author","values":["Mathew, Zacharia"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-28T15:17:48Z","10000-01-01","1999"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Microbiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/86749","(MiAaPQ)AAI9953090"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["To understand the function of Peptidase B (PepB) we have sequenced the pepB gene and purified its product. Two other peptidases, PepA and PepN, have also been purified to compare their substrate specificities with PepB. PepB has been assigned to the M17 family of peptidases on the basis of similarities in amino acid sequence and biochemical properties. PepB is a broad specificity aminopeptidase with a unique ability to remove Asp residues and a very efficient ability to remove Glu residues from the N-termini of peptides in than PepA and PepN. PepA, on the other hand, removes Pro residues, a function lacking in PepB and PepN. PepN has the unique ability of removing Gly residues from the N-terminus of peptides. The removal of amino acids from the N-terminus is also dependent on what kind of amino acid is present in the second position of the peptides. Neither PepA, PepB, nor PepN are processive in hydrolyzing their substrates. We have demonstrated the cooperation of PepA, PepB, and PepN in hydrolyzing some of their substrates.","Made available in DSpace on 2015-09-28T15:17:48Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9953090.pdf: 3604134 bytes, checksum: 76373711afa79163e6dd79d91c7f0197 (MD5) Previous issue date: 1999","Embargo set by: Seth Robbins for item 88030 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999."]},{"key":"dc:title","label":"Title","values":["A Comparative Study of the Substrate Specificities of Peptidases A, B, and N From Salmonella Typhimurium"]}]}],"canonical_facts":{"dc:contributor":["Miller, Charles G."],"dc:creator":["Mathew, Zacharia"],"dc:date":["2015-09-28T15:17:48Z","10000-01-01","1999"],"dc:description":["To understand the function of Peptidase B (PepB) we have sequenced the pepB gene and purified its product. Two other peptidases, PepA and PepN, have also been purified to compare their substrate specificities with PepB. PepB has been assigned to the M17 family of peptidases on the basis of similarities in amino acid sequence and biochemical properties. PepB is a broad specificity aminopeptidase with a unique ability to remove Asp residues and a very efficient ability to remove Glu residues from the N-termini of peptides in than PepA and PepN. PepA, on the other hand, removes Pro residues, a function lacking in PepB and PepN. PepN has the unique ability of removing Gly residues from the N-terminus of peptides. The removal of amino acids from the N-terminus is also dependent on what kind of amino acid is present in the second position of the peptides. Neither PepA, PepB, nor PepN are processive in hydrolyzing their substrates. We have demonstrated the cooperation of PepA, PepB, and PepN in hydrolyzing some of their substrates.","Made available in DSpace on 2015-09-28T15:17:48Z (GMT). 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