Exploring the impact of different thioesterase domains for the design of hybrid peptide synthetases-Reference-Cited by-同舟云学术

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Exploring the impact of different thioesterase domains for the design of hybrid peptide synthetases

Published:2001-10 Issue:10 Volume:8 Page:997-1010
ISSN:1074-5521
Container-title:Chemistry & Biology
language:en
Short-container-title:Chemistry & Biology

Author:

Schwarzer Dirk,Mootz Henning D,Marahiel Mohamed A

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry

Reference36 articles.

1. Modular peptide synthetases involved in non-ribosomal peptide synthesis;Marahiel;Chem. Rev.,1997

2. Harnessing the biosynthetic code: combinations, permutations, and mutations;Cane;Science,1998

3. The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains;Mootz;J. Bacteriol.,1997

4. Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S;Conti;EMBO J.,1997

5. Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases;Weber;Struct. Fold Des.,2000

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1. Chemoenzymatic synthesis of macrocyclic peptides and polyketides via thioesterase-catalyzed macrocyclization;Beilstein Journal of Organic Chemistry;2024-04-04

2. Effects of the deletion and substitution of thioesterase on bacillomycin D synthesis;Biotechnology Letters;2023-06-02

3. A machine learning-based method for prediction of macrocyclization patterns of polyketides and non-ribosomal peptides;Bioinformatics;2020-11-22

4. Efficient rational modification of non-ribosomal peptides by adenylation domain substitution;Nature Communications;2020-09-11

5. Efficient rational modification of non-ribosomal peptides by adenylation domain substitution;2020-03-02

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