{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,10]],"date-time":"2023-10-10T22:09:07Z","timestamp":1696975747046},"reference-count":23,"publisher":"Springer Science and Business Media LLC","issue":"1","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Microbiol"],"published-print":{"date-parts":[[2011,12]]},"abstract":"<jats:title>Abstract<\/jats:title>\n          <jats:sec>\n            <jats:title>Background<\/jats:title>\n            <jats:p>The aim of this study was to analyze the significance of leucine to proline substitution at position 138(Leu138Pro) on the hydrolysis of penicillin and ampicillin that we identified in the <jats:italic>bla<\/jats:italic>\n              <jats:sub>SHV<\/jats:sub> gene of clinical <jats:italic>Escherichia coli<\/jats:italic> swine isolate.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>Kinetic analysis of the mutant proteins showed that <jats:italic>K<\/jats:italic>\n              <jats:sub>\n                <jats:italic>m<\/jats:italic>\n              <\/jats:sub>value of the purified L138P mutant was comparatively higher than SHV-1, SHV-33 and SHV-33(L138P) enzyme for penicillin and ampicillin. Docking simulation of the SHV-1 and SHV-(L138P) enzymes also confirmed that \u03b2-lactamases preferred penicillin to ampicillin and the SHV-1 had a higher binding affinity for antibiotics compared to the SHV-(L138P) and other mutants.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>Our result demonstrated that L138P has a reduced role in penicillin and ampicillin hydrolyzing properties of SHV \u03b2-lactamases. These naturally occurring mutations rendering reduced function of the existing protein could trigger the emergence or acquisition of more effective alternative mechanisms for \u03b2-lactam hydrolysis.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2180-11-29","type":"journal-article","created":{"date-parts":[[2013,3,2]],"date-time":"2013-03-02T00:58:19Z","timestamp":1362185899000},"update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Enzymatic analysis of the effect of naturally occurring Leu138Pro mutation identified in SHV \u03b2-lactamase on hydrolysis of penicillin and ampicillin"],"prefix":"10.1186","volume":"11","author":[{"given":"Nabin","family":"Rayamajhi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeong Chan","family":"Joo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seung Bin","family":"Cha","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Subarna","family":"Pokherl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Min Kyung","family":"Shin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Young Je","family":"Yoo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Han Sang","family":"Yoo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2011,2,4]]},"reference":[{"key":"1316_CR1","doi-asserted-by":"publisher","first-page":"933","DOI":"10.1128\/CMR.14.4.933-951.2001","volume":"14","author":"PA Bradford","year":"2001","unstructured":"Bradford PA: Extended-spectrum \u03b2-lactamases in the 21st century: characterization, epidemiology and detection of this important resistance threat. 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