{"corpus_id":22014987,"paper_sha":"46404e51bd182ced64f74d9fe6f974b5b4cc2722","doi":"10.1016/S0021-9258(18)35771-5","arxiv_id":null,"pmid":1447185,"pmcid":null,"mag_id":2492286932,"dblp_id":null,"acl_id":null,"title":"Engineering dehydrated amino acid residues in the antimicrobial peptide nisin.","year":1992,"publication_date":"1992-12-05","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of biological chemistry","pages":"\n          24340-6\n        ","volume":"267 34"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle","Study"],"pubmed_pub_types":["Comparative Study","Journal Article","Research Support, Non-U.S. Gov't"],"s2_fields_of_study":["Biology","Medicine","Chemistry","Engineering"],"reference_count":28,"citation_count":196,"influential_citation_count":4,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Amino Acid Sequence","mj":false,"ui":"D000595"},{"d":"Bacteria","mj":false,"qs":[{"q":"drug effects","mj":false,"ui":"Q000187"},{"q":"growth & development","mj":false,"ui":"Q000254"}],"ui":"D001419"},{"d":"Base Sequence","mj":false,"ui":"D001483"},{"d":"Cloning, Molecular","mj":false,"qs":[{"q":"methods","mj":false,"ui":"Q000379"}],"ui":"D003001"},{"d":"DNA, Bacterial","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"},{"q":"isolation & purification","mj":false,"ui":"Q000302"}],"ui":"D004269"},{"d":"Escherichia coli","mj":false,"qs":[{"q":"genetics","mj":false,"ui":"Q000235"}],"ui":"D004926"},{"d":"Lactococcus lactis","mj":false,"qs":[{"q":"genetics","mj":true,"ui":"Q000235"}],"ui":"D013294"},{"d":"Magnetic Resonance Spectroscopy","mj":false,"ui":"D009682"},{"d":"Microbial Sensitivity Tests","mj":false,"ui":"D008826"},{"d":"Molecular Sequence Data","mj":false,"ui":"D008969"},{"d":"Mutagenesis, Site-Directed","mj":true,"ui":"D016297"},{"d":"Nisin","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"genetics","mj":true,"ui":"Q000235"},{"q":"pharmacology","mj":false,"ui":"Q000494"}],"ui":"D009561"},{"d":"Oligodeoxyribonucleotides","mj":false,"ui":"D009838"},{"d":"Polymerase Chain Reaction","mj":false,"qs":[{"q":"methods","mj":false,"ui":"Q000379"}],"ui":"D016133"},{"d":"Protein Conformation","mj":false,"ui":"D011487"},{"d":"Protein Engineering","mj":false,"qs":[{"q":"methods","mj":true,"ui":"Q000379"}],"ui":"D015202"},{"d":"Recombinant Proteins","mj":false,"qs":[{"q":"chemistry","mj":false,"ui":"Q000737"},{"q":"pharmacology","mj":false,"ui":"Q000494"}],"ui":"D011994"},{"d":"Restriction Mapping","mj":false,"ui":"D015183"},{"d":"Structure-Activity Relationship","mj":false,"ui":"D013329"}],"chemicals":[{"n":"DNA, Bacterial","ui":"D004269","reg":"0"},{"n":"Oligodeoxyribonucleotides","ui":"D009838","reg":"0"},{"n":"Recombinant Proteins","ui":"D011994","reg":"0"},{"n":"Nisin","ui":"D009561","reg":"1414-45-5"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":null,"s2_open_access_landing_url":null,"s2_open_access_license":null,"s2_open_access_status":null,"pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"The small antimicrobial peptide nisin, produced by Lactococcus lactis, contains the uncommon amino acid residues dehydroalanine and dehydrobutyrine and five thio ether bridges. Since these structures are posttranslationally formed from Ser, Thr, and Cys residues, it is feasible to study their role in nisin function and biosynthesis by protein engineering. Here we report the development of an expression system for mutated nisin Z (nisZ) genes, using nisin A producing L. lactis as a host. Replacement by site-directed mutagenesis of the Ser-5 codon in nisZ by a Thr codon, led to a mutant with a dehydrobutyrine instead of a dehydroalanine residue at position 5, as shown by NMR. Its antimicrobial activity was 2-10-fold lower relative to wild-type nisin Z, depending on the indicator strain used. In another mutagenesis study a double mutation was introduced in the nisZ gene by replacing the codons for Met-17 and Gly-18 by codons for Gln and Thr, respectively, as in the third lanthionine ring of the related antimicrobial peptide subtilin from Bacillus subtilis. This resulted in the simultaneous production of two mutant species, one containing a Thr residue and the other containing a dehydrobutyrine residue at position 18, both having different bacteriocidal properties.","claims":[{"public_id":"cl_653166a8bb78704e1e997bcc4fed6dae","status":"active","text":"A double mutation replacing Met-17 and Gly-18 in nisZ with Gln and Thr, modeled on the third lanthionine ring of subtilin, yields two mutant species at position 18 - one with a Thr residue and one with a dehydrobutyrine residue - that have different bactericidal properties.","confidence":0.85,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["review"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ (ezd9qvkvax)","roles":["review"],"url":"https://sah.borca.ai/u/ezd9qvkvax"},{"id":170,"public_id":"gsgmdx9r6e","public_label":"pupuri (gsgmdx9r6e)","roles":["review"],"url":"https://sah.borca.ai/u/gsgmdx9r6e"}],"url":"https://sah.borca.ai/claims/cl_653166a8bb78704e1e997bcc4fed6dae"},{"public_id":"cl_95eb2849d73aa07692e05e3fa9e5b95b","status":"active","text":"An expression system for mutated nisin Z genes was developed using nisin A-producing Lactococcus lactis as a host strain.","confidence":0.85,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["review"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ (ezd9qvkvax)","roles":["review"],"url":"https://sah.borca.ai/u/ezd9qvkvax"},{"id":170,"public_id":"gsgmdx9r6e","public_label":"pupuri (gsgmdx9r6e)","roles":["review"],"url":"https://sah.borca.ai/u/gsgmdx9r6e"}],"url":"https://sah.borca.ai/claims/cl_95eb2849d73aa07692e05e3fa9e5b95b"},{"public_id":"cl_8a3d2b504c4887f77ae9db009b353ebd","status":"active","text":"Replacing the Ser-5 codon in nisZ with a Thr codon produces a dehydrobutyrine residue instead of a dehydroalanine residue at position 5, as confirmed by NMR.","confidence":0.92,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["review"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ (ezd9qvkvax)","roles":["review"],"url":"https://sah.borca.ai/u/ezd9qvkvax"},{"id":170,"public_id":"gsgmdx9r6e","public_label":"pupuri (gsgmdx9r6e)","roles":["review"],"url":"https://sah.borca.ai/u/gsgmdx9r6e"}],"url":"https://sah.borca.ai/claims/cl_8a3d2b504c4887f77ae9db009b353ebd"},{"public_id":"cl_0f1fc292dcd3548c3f2de52cb58995de","status":"active","text":"The Ser5Thr nisin Z mutant carrying dehydrobutyrine at position 5 shows antimicrobial activity 2-10 fold lower than wild-type nisin Z, depending on the indicator strain used.","confidence":0.88,"contributors":[{"id":17,"public_id":"322360f1c1","public_label":"Killer Whale (322360f1c1)","roles":["extraction"],"url":"https://sah.borca.ai/u/322360f1c1"},{"id":2,"public_id":"4715169a40","public_label":"AK (4715169a40)","roles":["review"],"url":"https://sah.borca.ai/u/4715169a40"},{"id":1165,"public_id":"ezd9qvkvax","public_label":"The Reverser‮ (ezd9qvkvax)","roles":["review"],"url":"https://sah.borca.ai/u/ezd9qvkvax"},{"id":170,"public_id":"gsgmdx9r6e","public_label":"pupuri 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