NDLI: The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S

Content Provider	PubMed Central
Author	Yu, Guiyang Li, Li Liu, Xiangyang Liu, Guang Deng, Zixin Zabriskie, Mark T. Jiang, Ming He, Xinyi
Copyright Year	2015
Abstract	The peptidyl nucleoside blasticidin S (BS) isolated from Streptomyces griseochromogenes was the first non-mercurial fungicide used on a large scale to prevent rice blast. In the biosynthesis of BS, leucylblasticidin S (LBS) was suggested as the penultimate metabolite with 20-fold less inhibitory activity than the final product BS. Incomplete conversion of LBS to BS at a variable efficiency ranging from 10% to 90% was observed either in the native strain S. griseochromogenes or a heterologous producer Streptomyces lividans WJ2. In this study, we determined that maturation of BS from LBS is not a spontaneous process but is governed by a standalone peptidase PepN, which hydrolyzes LBS in a pH-sensitive way with most appropriate of pH 7~8 but is inactive when the pH is below 5 or above 10. PepN1 and PepN2, two neighboring PepN homologs from Streptomyces lividans were purified in E. coli but displayed ca.100-fold difference in LBS hydrolytic activity. Overexpression of pepN1 in WJ2 enhanced BS yield by 100% and lowered the ratio of LBS to BS from 2:1 to 2:3. This work presents the expansion of the biological role for PepN in antibiotic maturation and the first report of hydrolysis of beta amide linkage by this conserved enzyme.
Related Links	http://dx.doi.org/10.1038/srep17641
Starting Page	17641
File Format	PDF
ISSN	20452322
e-ISSN	20452322
Journal	Scientific Reports
Volume Number	5
Language	English
Publisher	Nature Publishing Group
Publisher Date	2015-12-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Science and technology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S

Guanidine N-methylation by BlsL Is Dependent on Acylation of Beta-amine Arginine in the Biosynthesis of Blasticidin S

PepN-like aminopeptidase from Lactohacillus curvatus DPC2024: purification and characterization

PepN-like aminopeptidase from Lactohacillus curvatus DPC2024: purification and characterization

Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome

Characterization and overexpression of the Lactococcus lactis pepN gene and localization of its product, aminopeptidase N.

S-acylation of the Insulin-Responsive Aminopeptidase (IRAP): Quantitative analysis and Identification of Modified Cysteines

Streptomyces lividans Blasticidin S Deaminase and Its Application in Engineering a Blasticidin S-Producing Strain for Ease of Genetic Manipulation

Functional characterization of aminopeptidase PepN from Mycobacterium tuberculosis

The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S

Similar Documents

The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S

Guanidine N-methylation by BlsL Is Dependent on Acylation of Beta-amine Arginine in the Biosynthesis of Blasticidin S

PepN-like aminopeptidase from Lactohacillus curvatus DPC2024: purification and characterization

PepN-like aminopeptidase from Lactohacillus curvatus DPC2024: purification and characterization

Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome

Characterization and overexpression of the Lactococcus lactis pepN gene and localization of its product, aminopeptidase N.

S-acylation of the Insulin-Responsive Aminopeptidase (IRAP): Quantitative analysis and Identification of Modified Cysteines

Streptomyces lividans Blasticidin S Deaminase and Its Application in Engineering a Blasticidin S-Producing Strain for Ease of Genetic Manipulation

Functional characterization of aminopeptidase PepN from Mycobacterium tuberculosis

The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S