scholarly journals Priming Type II Polyketide Synthases via a Type II Nonribosomal Peptide Synthetase Mechanism

2006 ◽  
Vol 128 (5) ◽  
pp. 1428-1429 ◽  
Author(s):  
Miho Izumikawa ◽  
Qian Cheng ◽  
Bradley S. Moore
Keyword(s):  
Nonribosomal Peptide Synthetase ◽  
Polyketide Synthases ◽  
Type Ii ◽  
Nonribosomal Peptide ◽  
Peptide Synthetase

scholarly journals Phosphinothricin Tripeptide Synthetases in Streptomyces viridochromogenes Tü494

2005 ◽  
Vol 49 (11) ◽  
pp. 4598-4607 ◽  
Author(s):  
Dirk Schwartz ◽  
Nicolas Grammel ◽  
Eva Heinzelmann ◽  
Ullrich Keller ◽  
Wolfgang Wohlleben
Keyword(s):  
Gene Cluster ◽  
Nonribosomal Peptide Synthetase ◽  
Herbicidal Activity ◽  
Type Ii ◽  
Biosynthesis Gene Cluster ◽  
Nonribosomal Peptide ◽  
Product Release ◽  
Peptide Synthetase ◽  
Biosynthesis Gene

ABSTRACT The tripeptide backbone of phosphinothricin (PT) tripeptide (PTT), a compound with herbicidal activity from Streptomyces viridochromogenes, is assembled by three stand-alone peptide synthetase modules. The enzyme PhsA (66 kDa) recruits the PT-precursor N-acetyl-demethylphosphinothricin (N-Ac-DMPT), whereas the two alanine residues of PTT are assembled by the enzymes PhsB and PhsC (129 and 119 kDa, respectively). During or after assembly, the N-Ac-DMPT residue in the peptide is converted to PT by methylation and deacetylation. Both phsB and phsC appear to be cotranscribed together with two other genes from a single promoter and they are located at a distance of 20 kb from the gene phsA, encoding PhsA, in the PTT biosynthesis gene cluster of S. viridochromogenes. PhsB and PhsC represent single nonribosomal peptide synthetase elongation modules lacking a thioesterase domain. Gene inactivations, genetic complementations, determinations of substrate specificity of the heterologously produced proteins, and comparison of PhsC sequence with the amino terminus of the alanine-activating nonribosomal peptide synthetase PTTSII from S. viridochromogenes confirmed the role of the two genes in the bialanylation of Ac-DMPT. The lack of an integral thioesterase domain in the PTT assembly system points to product release possibly involving two type II thioesterase genes (the1 and the2) located in the PTT gene cluster alone or in conjunction with an as yet unknown mechanism of product release.

scholarly journals Manipulating Protein–Protein Interactions in Nonribosomal Peptide Synthetase Type II Peptidyl Carrier Proteins

Biochemistry ◽  
2017 ◽  
Vol 56 (40) ◽  
pp. 5269-5273 ◽  
Author(s):  
Matt J. Jaremko ◽  
D. John Lee ◽  
Ashay Patel ◽  
Victoria Winslow ◽  
Stanley J. Opella ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Nonribosomal Peptide Synthetase ◽  
Type Ii ◽  
Carrier Proteins ◽  
Protein Protein Interactions ◽  
Nonribosomal Peptide ◽  
Peptide Synthetase

scholarly journals Draft Genome Sequence of Saccharomonospora sp. Strain LRS4.154, a Moderately Halophilic Actinobacterium with the Biotechnologically Relevant Polyketide Synthase and Nonribosomal Peptide Synthetase Systems

2017 ◽  
Vol 5 (21) ◽  
Author(s):  
Scarlett Alonso-Carmona ◽  
Blanca Vera-Gargallo ◽  
Rafael R. de la Haba ◽  
Antonio Ventosa ◽  
Horacio Sandoval-Trujillo ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Polyketide Synthase ◽  
Draft Genome ◽  
Nonribosomal Peptide Synthetase ◽  
Open Reading Frames ◽  
Draft Genome Sequence ◽  
Nonribosomal Peptide ◽  
Moderately Halophilic ◽  
Peptide Synthetase ◽  
Reading Frames

ABSTRACT The draft genome sequence of Saccharomonospora sp. strain LRS4.154, a moderately halophilic actinobacterium, has been determined. The genome has 4,860,108 bp, a G+C content of 71.0%, and 4,525 open reading frames (ORFs). The clusters of PKS and NRPS genes, responsible for the biosynthesis of a large number of biomolecules, were identified in the genome.

Engineered Nonribosomal Peptide Synthetase Shows Opposite Amino Acid Loading and Condensation Specificity

ACS Catalysis ◽  
2021 ◽  
pp. 8692-8700
Author(s):  
Aleksa Stanišić ◽  
Annika Hüsken ◽  
Philipp Stephan ◽  
David L. Niquille ◽  
Jochen Reinstein ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nonribosomal Peptide Synthetase ◽  
Nonribosomal Peptide ◽  
Peptide Synthetase ◽  
Acid Loading

scholarly journals Structural and Functional Insights into a Peptide Bond-Forming Bidomain from a Nonribosomal Peptide Synthetase

Structure ◽  
2007 ◽  
Vol 15 (7) ◽  
pp. 781-792 ◽  
Author(s):  
Stefan A. Samel ◽  
Georg Schoenafinger ◽  
Thomas A. Knappe ◽  
Mohamed A. Marahiel ◽  
Lars-Oliver Essen
Keyword(s):  
Peptide Bond ◽  
Nonribosomal Peptide Synthetase ◽  
Nonribosomal Peptide ◽  
Bond Forming ◽  
Peptide Synthetase
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