Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A
Corallopyronin A is a promising in vivo active antibiotic, currently undergoing preclinical evaluation. This myxobacterial compound interferes with a newly identified drug target site, i.e., the switch region of the bacterial DNA-dependent RNA-polymerase (RNAP). Since this target site differs from t...
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Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3910853 http://www.ncbi.nlm.nih.gov/pubmed/24277032 https://doi.org/10.1128/AAC.01894-13 |
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ftpubmed:oai:pubmedcentral.nih.gov:3910853 2023-05-15T15:52:24+02:00 Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A Schäberle, Till F. Mir Mohseni, Mahsa Lohr, Friederike Schmitz, Alexander König, Gabriele M. 2014-02 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3910853 http://www.ncbi.nlm.nih.gov/pubmed/24277032 https://doi.org/10.1128/AAC.01894-13 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/24277032 http://dx.doi.org/10.1128/AAC.01894-13 Copyright © 2014, American Society for Microbiology. All Rights Reserved. Chemistry Biosynthesis Text 2014 ftpubmed https://doi.org/10.1128/AAC.01894-13 2014-08-03T00:57:50Z Corallopyronin A is a promising in vivo active antibiotic, currently undergoing preclinical evaluation. This myxobacterial compound interferes with a newly identified drug target site, i.e., the switch region of the bacterial DNA-dependent RNA-polymerase (RNAP). Since this target site differs from that of known RNAP inhibitors such as the rifamycins, corallopyronin A shows no cross-resistance with other antibacterial agents. Corallopyronin A is a polyketide synthase- and nonribosomal peptide synthetase-derived molecule whose structure and biosynthesis is distinguished by several peculiarities, such as the unusual vinyl carbamate functionality whose formation involves carbonic acid as an unprecedented C1-starter unit. Using in vitro experiments the nature of this starter molecule was revealed to be the methyl ester of carbonic acid. Biochemical investigations showed that methylation of carbonic acid is performed by the O-methyltransferase CorH. These experiments shed light on the biosynthesis of the Eastern chain of α-pyrone antibiotics such as corallopyronin A. Text Carbonic acid PubMed Central (PMC) Antimicrobial Agents and Chemotherapy 58 2 950 956 |
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Chemistry Biosynthesis |
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Chemistry Biosynthesis Schäberle, Till F. Mir Mohseni, Mahsa Lohr, Friederike Schmitz, Alexander König, Gabriele M. Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
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Chemistry Biosynthesis |
description |
Corallopyronin A is a promising in vivo active antibiotic, currently undergoing preclinical evaluation. This myxobacterial compound interferes with a newly identified drug target site, i.e., the switch region of the bacterial DNA-dependent RNA-polymerase (RNAP). Since this target site differs from that of known RNAP inhibitors such as the rifamycins, corallopyronin A shows no cross-resistance with other antibacterial agents. Corallopyronin A is a polyketide synthase- and nonribosomal peptide synthetase-derived molecule whose structure and biosynthesis is distinguished by several peculiarities, such as the unusual vinyl carbamate functionality whose formation involves carbonic acid as an unprecedented C1-starter unit. Using in vitro experiments the nature of this starter molecule was revealed to be the methyl ester of carbonic acid. Biochemical investigations showed that methylation of carbonic acid is performed by the O-methyltransferase CorH. These experiments shed light on the biosynthesis of the Eastern chain of α-pyrone antibiotics such as corallopyronin A. |
format |
Text |
author |
Schäberle, Till F. Mir Mohseni, Mahsa Lohr, Friederike Schmitz, Alexander König, Gabriele M. |
author_facet |
Schäberle, Till F. Mir Mohseni, Mahsa Lohr, Friederike Schmitz, Alexander König, Gabriele M. |
author_sort |
Schäberle, Till F. |
title |
Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
title_short |
Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
title_full |
Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
title_fullStr |
Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
title_full_unstemmed |
Function of the Loading Module in CorI and of the O-Methyltransferase CorH in Vinyl Carbamate Biosynthesis of the Antibiotic Corallopyronin A |
title_sort |
function of the loading module in cori and of the o-methyltransferase corh in vinyl carbamate biosynthesis of the antibiotic corallopyronin a |
publisher |
American Society for Microbiology |
publishDate |
2014 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3910853 http://www.ncbi.nlm.nih.gov/pubmed/24277032 https://doi.org/10.1128/AAC.01894-13 |
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Carbonic acid |
genre_facet |
Carbonic acid |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC http://www.ncbi.nlm.nih.gov/pubmed/24277032 http://dx.doi.org/10.1128/AAC.01894-13 |
op_rights |
Copyright © 2014, American Society for Microbiology. All Rights Reserved. |
op_doi |
https://doi.org/10.1128/AAC.01894-13 |
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Antimicrobial Agents and Chemotherapy |
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58 |
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2 |
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950 |
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956 |
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1766387593408151552 |