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Deacetoxycephalosporin C synthase (expandase): Research progress and application potential
Cephalosporins play an indispensable role against bacterial infections. Deacetyloxycephalosporin C synthase (DAOCS), also called expandase, is a key enzyme in cephalosporin biosynthesis that epoxides penicillin to form the hexavalent thiazide ring of cephalosporin. DAOCS in fungus Acremonium chrysog...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
KeAi Publishing
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8626558/ https://www.ncbi.nlm.nih.gov/pubmed/34901478 http://dx.doi.org/10.1016/j.synbio.2021.11.001 |
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author | Niu, Xiaofan Zhang, Jian Xue, Xianli Wang, Depei Wang, Lin Gao, Qiang |
author_facet | Niu, Xiaofan Zhang, Jian Xue, Xianli Wang, Depei Wang, Lin Gao, Qiang |
author_sort | Niu, Xiaofan |
collection | PubMed |
description | Cephalosporins play an indispensable role against bacterial infections. Deacetyloxycephalosporin C synthase (DAOCS), also called expandase, is a key enzyme in cephalosporin biosynthesis that epoxides penicillin to form the hexavalent thiazide ring of cephalosporin. DAOCS in fungus Acremonium chrysogenum was identified as a bifunctional enzyme with both ring expansion and hydroxylation, whereas two separate enzymes in bacteria catalyze these two reactions. In this review, we briefly summarize its source and function, improvement of the conversion rate of penicillin to deacetyloxycephalosporin C through enzyme modification, crystallography features, the prediction of the active site, and application perspective. |
format | Online Article Text |
id | pubmed-8626558 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | KeAi Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-86265582021-12-09 Deacetoxycephalosporin C synthase (expandase): Research progress and application potential Niu, Xiaofan Zhang, Jian Xue, Xianli Wang, Depei Wang, Lin Gao, Qiang Synth Syst Biotechnol Article Cephalosporins play an indispensable role against bacterial infections. Deacetyloxycephalosporin C synthase (DAOCS), also called expandase, is a key enzyme in cephalosporin biosynthesis that epoxides penicillin to form the hexavalent thiazide ring of cephalosporin. DAOCS in fungus Acremonium chrysogenum was identified as a bifunctional enzyme with both ring expansion and hydroxylation, whereas two separate enzymes in bacteria catalyze these two reactions. In this review, we briefly summarize its source and function, improvement of the conversion rate of penicillin to deacetyloxycephalosporin C through enzyme modification, crystallography features, the prediction of the active site, and application perspective. KeAi Publishing 2021-11-23 /pmc/articles/PMC8626558/ /pubmed/34901478 http://dx.doi.org/10.1016/j.synbio.2021.11.001 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Niu, Xiaofan Zhang, Jian Xue, Xianli Wang, Depei Wang, Lin Gao, Qiang Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title | Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title_full | Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title_fullStr | Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title_full_unstemmed | Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title_short | Deacetoxycephalosporin C synthase (expandase): Research progress and application potential |
title_sort | deacetoxycephalosporin c synthase (expandase): research progress and application potential |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8626558/ https://www.ncbi.nlm.nih.gov/pubmed/34901478 http://dx.doi.org/10.1016/j.synbio.2021.11.001 |
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