{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:07:56Z","timestamp":1791266876404,"version":"4.1.0"},"reference-count":62,"publisher":"Microbiology Society","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2003,12,1]]},"abstract":"<jats:p>\n                    PepN and its homologues are involved in the ATP-independent steps (downstream processing) during cytosolic protein degradation. To obtain insights into the contribution of PepN to the peptidase activity in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    , the hydrolysis of a selection of endopeptidase and exopeptidase substrates was studied in extracts of wild-type strains and two\n                    <jats:italic>pepN<\/jats:italic>\n                    mutants, 9218 and DH5\n                    <jats:italic>\u03b1<\/jats:italic>\n                    \u0394\n                    <jats:italic>pepN<\/jats:italic>\n                    . Hydrolysis of three of the seven endopeptidase substrates tested was reduced in both\n                    <jats:italic>pepN<\/jats:italic>\n                    mutants. Similar studies revealed that hydrolysis of 10 of 14 exopeptidase substrates studied was greatly reduced in both\n                    <jats:italic>pepN<\/jats:italic>\n                    mutants. This decreased ability to cleave these substrates is\n                    <jats:italic>pepN<\/jats:italic>\n                    -specific as there is no reduction in the ability to hydrolyse exopeptidase substrates in\n                    <jats:italic>E. coli<\/jats:italic>\n                    mutants lacking other peptidases,\n                    <jats:italic>pepA<\/jats:italic>\n                    ,\n                    <jats:italic>pepB<\/jats:italic>\n                    or\n                    <jats:italic>pepE<\/jats:italic>\n                    . PepN overexpression complemented the hydrolysis of the affected exopeptidase substrates. These results suggest that PepN is responsible for the majority of aminopeptidase activity in\n                    <jats:italic>E. coli<\/jats:italic>\n                    . Further\n                    <jats:italic>in vitro<\/jats:italic>\n                    studies with purified PepN revealed a preference to cleave basic and small amino acids as aminopeptidase substrates. Kinetic characterization revealed the aminopeptidase cleavage preference of\n                    <jats:italic>E. coli<\/jats:italic>\n                    PepN to be Arg&gt;Ala&gt;Lys&gt;Gly. Finally, it was shown that PepN is a negative regulator of the sodium-salicylate-induced stress in\n                    <jats:italic>E. coli<\/jats:italic>\n                    , demonstrating a physiological role for this aminoendopeptidase under some stress conditions.\n                  <\/jats:p>","DOI":"10.1099\/mic.0.26518-0","type":"journal-article","created":{"date-parts":[[2003,12,8]],"date-time":"2003-12-08T16:38:53Z","timestamp":1070901533000},"page":"3437-3447","source":"Crossref","is-referenced-by-count":64,"title":["PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress"],"prefix":"10.1099","volume":"149","author":[{"given":"Dilip","family":"Chandu","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dipankar","family":"Nandi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1111\/j.1574-6968.1983.tb00554.x","article-title":"Molecular cloning and amplification of the gene for aminopeptidase N of Escherichia coli","volume":"19","author":"Bally","year":"1983","journal-title":"FEMS Microbiol Lett"},{"key":"R2","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/BF00341454","article-title":"Cloning and orientation of the gene encoding aminopeptidase N in Escherichia coli","volume":"195","author":"Bally","year":"1984","journal-title":"Mol Gen Genet"},{"key":"R3","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1099\/00221287-147-8-2045","article-title":"Lysine aminopeptidase of Aspergillus niger","volume":"147","author":"Basten","year":"2001","journal-title":"Microbiology"},{"key":"R4","doi-asserted-by":"crossref","first-page":"18734","DOI":"10.1074\/jbc.273.30.18734","article-title":"Interferon- \u03b3 can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase","volume":"273","author":"Beninga","year":"1998","journal-title":"J Biol Chem"},{"key":"R5","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0968-0004(98)01227-4","article-title":"N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families","volume":"23","author":"Bradshaw","year":"1998","journal-title":"Trends Biochem Sci"},{"key":"R6","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1038\/35106609","article-title":"Crystal structure of the tricorn protease reveals a protein disassembly line","volume":"414","author":"Brandstetter","year":"2001","journal-title":"Nature"},{"key":"R7","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1128\/JB.156.1.308-315.1983","article-title":"Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium","volume":"156","author":"Braun","year":"1983","journal-title":"J Bacteriol"},{"key":"R8","doi-asserted-by":"crossref","first-page":"14310","DOI":"10.1016\/S0021-9258(19)85242-0","article-title":"Isolation and characterization of AAP1 . 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