Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains  被引量:2

在线阅读下载全文

作  者:Joshua C.Corpuz Javier O.Sanlley Michael D.Burkart 

机构地区:[1]Department of Chemistry and Biochemistry,University of California-San Diego,9500 Gilman Drive,La Jolla,CA,92093-0358,USA

出  处:《Synthetic and Systems Biotechnology》2022年第2期671-682,共12页合成和系统生物技术(英文)

基  金:J.C.C.was supported by the National Institute of General Medical Science(NIGMS)of the National Institutes of Health(NIH)under award number 1F31GM13761601A1;J.O.S.was supported by the ACS Bridge Program and The Genentech Foundation;This work was supported by the NIGMS of the NIH under award number R01GM095970.

摘  要:Non-ribosomal peptide synthetases(NRPSs)are attractive targets for biosynthetic pathway engineering due to their modular architecture and the therapeutic relevance of their products.With catalysis mediated by specific protein-protein interactions formed between the peptidyl carrier protein(PCP)and its partner enzymes,NRPS enzymology and control remains fertile ground for discovery.This review focuses on the recent efforts within structural biology by compiling high-resolution structural data that shed light into the various protein-protein interfaces formed between the PCP and its partner enzymes,including the phosphopantetheinyl transferase(PPTase),adenylation(A)domain,condensation(C)domain,thioesterase(TE)domain and other tailoring enzymes within the synthetase.Integrating our understanding of how the PCP recognizes partner proteins with the potential to use directed evolution and combinatorial biosynthetic methods will enhance future efforts in discovery and production of new bioactive compounds.

关 键 词:Natural products Protein-protein interactions Non-ribosomal peptide synthetase Peptidyl carrier protein Combinatorial biosynthesis Synthetic biology 

分 类 号:O62[理学—有机化学]

 

参考文献:

正在载入数据...

 

二级参考文献:

正在载入数据...

 

耦合文献:

正在载入数据...

 

引证文献:

正在载入数据...

 

二级引证文献:

正在载入数据...

 

同被引文献:

正在载入数据...

 

相关期刊文献:

正在载入数据...

相关的主题
相关的作者对象
相关的机构对象