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Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP

The dihydrochalcomycin (GERI) synthetic gene cluster from Streptomyces sp. KCTC 0041BP has been isolated. Two open reading frames (ORFs), designated gerT1 and gerT2 as glycosyltransferase genes, has been identified by sequence analysis. GerT1 encodes for the protein function as dTDP-deoxyallosyltran...

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Autores principales: Thuy, Ta Thi Thu, Sohng, Jae Kyung, Pfeifer, Blaine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Communications and Publications Division (CPD) of the IFCC 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4975237/
https://www.ncbi.nlm.nih.gov/pubmed/27683346
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author Thuy, Ta Thi Thu
Sohng, Jae Kyung
Pfeifer, Blaine
author_facet Thuy, Ta Thi Thu
Sohng, Jae Kyung
Pfeifer, Blaine
author_sort Thuy, Ta Thi Thu
collection PubMed
description The dihydrochalcomycin (GERI) synthetic gene cluster from Streptomyces sp. KCTC 0041BP has been isolated. Two open reading frames (ORFs), designated gerT1 and gerT2 as glycosyltransferase genes, has been identified by sequence analysis. GerT1 encodes for the protein function as dTDP-deoxyallosyltransferase and it is responsible to the attachment of dTDP-allose to the macrolide ring. Similarly, gerT2 encodes for peptide named as dTDP-chacosyltransferase which can transfers the dTDP-4,6-dideoxyglucose to macrolactone core. During process of compound isolation, a new compound has been isolated with molecular weight m/z 755 [M+Na+]. This compound could be the dihydrochalcomycin derivative. The compound has been shown the same antibacterial activity as GERI compound.
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spelling pubmed-49752372016-09-28 Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP Thuy, Ta Thi Thu Sohng, Jae Kyung Pfeifer, Blaine EJIFCC Research Article The dihydrochalcomycin (GERI) synthetic gene cluster from Streptomyces sp. KCTC 0041BP has been isolated. Two open reading frames (ORFs), designated gerT1 and gerT2 as glycosyltransferase genes, has been identified by sequence analysis. GerT1 encodes for the protein function as dTDP-deoxyallosyltransferase and it is responsible to the attachment of dTDP-allose to the macrolide ring. Similarly, gerT2 encodes for peptide named as dTDP-chacosyltransferase which can transfers the dTDP-4,6-dideoxyglucose to macrolactone core. During process of compound isolation, a new compound has been isolated with molecular weight m/z 755 [M+Na+]. This compound could be the dihydrochalcomycin derivative. The compound has been shown the same antibacterial activity as GERI compound. The Communications and Publications Division (CPD) of the IFCC 2010-01-26 /pmc/articles/PMC4975237/ /pubmed/27683346 Text en Copyright © 2009 International Federation of Clinical Chemistry and Laboratory Medicine (IFCC). All rights reserved. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Thuy, Ta Thi Thu
Sohng, Jae Kyung
Pfeifer, Blaine
Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title_full Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title_fullStr Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title_full_unstemmed Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title_short Dihydrochalcomycin Production and Glycosyltransferase from Streptomyces SP. KCTC 0041BP
title_sort dihydrochalcomycin production and glycosyltransferase from streptomyces sp. kctc 0041bp
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4975237/
https://www.ncbi.nlm.nih.gov/pubmed/27683346
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