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Posttranslational Modifications during Natural Product Biosynthesis

项目来源

美国卫生和人类服务部基金(HHS)

项目主持人

BOND, MICHELLE RUEFFER

项目受资助机构

UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN

项目编号

5R37GM058822-20

立项年度

2019

立项时间

未公开

研究期限

未知 / 未知

项目级别

国家级

受资助金额

275729.00美元

学科

Antimicrobial Resistance;Biotechnology;Emerging Infectious Diseases;Genetics;Infectious Diseases

学科代码

未公开

基金类别

Non-SBIR/STTR RPGs

关键词

未公开

参与者

VAN DER DONK, WILFRED A.

参与机构

NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

项目标书摘要：DESCRIPTION (provided by applicant): Lanthipeptides are post-translationally modified peptide with a variety of biological activities. Nisin, its best known member, has been used for decades in the food industry without significant development of resistance. Other lanthipeptides are under investigation or in clinical trials for the treatment of cystic fibrosis and for the treament of multi-drug resistant bacteria. In this grant application we seek to extend our past success towards the use of the biosynthetic machinery as tools for biotechnology and to better understand their mechanism of substrate recognition and catalysis. Our goals are: 1. Understand the enzymes involved in lanthipeptide biosynthesis. 2. Engineer efficient processes to use posttranslationally modified peptide natural products for various applications. 3. Investigate new posttranslationally modified peptide natural products.

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  • 2.The Enzymology of Prochlorosin Biosynthesis

    • 关键词：
    • LANTHIPEPTIDE SYNTHETASE PROCM; MALTOSE-BINDING PROTEIN; PRECURSOR LIPID-II; LANTIBIOTIC MERSACIDIN; ESCHERICHIA-COLI; SECONDARY METABOLITES; MARINE CYANOBACTERIA; MODIFICATION ENZYME; ABC TRANSPORTERS; NATURAL-PRODUCTS
    • Bobeica, Silvia C.;van der Donk, Wilfred A.
    • 《MARINE ENZYMES AND SPECIALIZED METABOLISM, PT A》
    • 2018年
    • 会议

    Lanthipeptides are ribosomally synthesized and posttranslationally modified peptides containing thioether cross-links formed through addition of a cysteine to a dehydroalanine (to form lanthionine) or to a dehydrobutyrine (to form 3-methyllanthionine). Genome sequencing of marine cyanobacteria lead to the discovery of 1.6 million open reading frames encoding lanthipeptides. In many cases, a genome encodes a single lanthipeptide synthetase, but a large number of substrates. The enzymatic modification process in Prochlorococcus MIT9313 has been reconstituted in vitro, and a variety of experimental approaches have been used to try and understand how one enzyme is capable of modifying 30 different substrates. The methods used to characterize this system will be described along with a brief genomic description of the lanthipeptide landscape found in Prochlorococcus and Synechococcus.

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