Substrate specificity of a ketosynthase domain involved in bacillaene biosynthesis

• Zhiyong Yin and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2024, 20, 734–740, doi:10.3762/bjoc.20.67

• -labelled carbons. Biosynthetic model for bacillaene (1). M1–M17 indicate modules 1–17. A = adenylation domain, ACP = acyl carrier protein, AT = acyltransferase, C = condensation domain, DH = dehydratase, KR = ketoreductase, KS = ketosynthase, MT = methyltransferase, PCP = peptidyl carrier protein, TE

New variochelins from soil-isolated Variovorax sp. H002

• Jabal Rahmat Haedar,
• Aya Yoshimura and
• Toshiyuki Wakimoto

Beilstein J. Org. Chem. 2024, 20, 692–700, doi:10.3762/bjoc.20.63

• by diamonds. EIMS of DMOX derivatized free fatty acids derived from variochelins C–E (3–5). (a) 3, (b) 4, and (c) 5. (a) Plausible biosynthetic pathway of variochelin A–E (1–5). The circles represent domains: A: adenylation domain, C: condensation domain, PCP: peptide carrier protein, E

Development of a chemical scaffold for inhibiting nonribosomal peptide synthetases in live bacterial cells

• Fumihiro Ishikawa,
• Sho Konno,
• Hideaki Kakeya and
• Genzoh Tanabe

Beilstein J. Org. Chem. 2024, 20, 445–451, doi:10.3762/bjoc.20.39

• synthetase A (GrsA) in the gramicidin S-producer Aneurinibacillus migulanus ATCC 9999, providing an alternative scaffold to develop novel A-domain inhibitors. Keywords: adenylation domain inhibitor; gramicidin S synthetase; natural product; nonribosomal peptide; nonribosomal peptide synthetase

Discovery of unguisin J, a new cyclic peptide from Aspergillus heteromorphus CBS 117.55, and phylogeny-based bioinformatic analysis of UngA NRPS domains

• Sharmila Neupane,
• Marcelo Rodrigues de Amorim and
• Elizabeth Skellam

Beilstein J. Org. Chem. 2024, 20, 321–330, doi:10.3762/bjoc.20.32

• of the UngA NRPS were analyzed in an attempt to understand the lack of substrate specificity observed. Keywords: adenylation domain; condensation domain; fungal non-ribosomal peptide synthetase; heptapeptide; unguisin biosynthesis; Introduction Unguisins are a small family of fungal cyclic

Genomics-inspired discovery of massiliachelin, an agrochelin epimer from Massilia sp. NR 4-1

• Jan Diettrich,
• Hirokazu Kage and
• Markus Nett

Beilstein J. Org. Chem. 2019, 15, 1298–1303, doi:10.3762/bjoc.15.128

• stereochemistry at the C2 position derived from L-cysteine. This is because the MicC homolog from Massilia sp. NR 4-1 features only a single adenylation domain for the activation of L-cysteine, which corresponds to the micacocidin and yersiniabactin assembly lines [13][16]. An inspection of the ketoreductase (KR

A non-canonical peptide synthetase adenylates 3-methyl-2-oxovaleric acid for auriculamide biosynthesis

• Daniel Braga,
• Dirk Hoffmeister and
• Markus Nett

Beilstein J. Org. Chem. 2016, 12, 2766–2770, doi:10.3762/bjoc.12.274

• acid by the enzyme supports the hypothesis that it participates in the biosynthesis of auriculamide. An artificially truncated version of AulA that lacks the first adenylation domain activated this substrate like the full-length enzyme which shows that the first adenylation domain is dispensable

• -2-oxovaleric acid by its second adenylation domain. Our results also contribute to hone algorithms used to predict substrates from nonribosomal codes. Moreover, we describe how this enzyme is pliant to minor structural variations of that molecule, enabling future attempts to generate auriculamide

Biosynthesis of oxygen and nitrogen-containing heterocycles in polyketides

• Franziska Hemmerling and
• Frank Hahn

Beilstein J. Org. Chem. 2016, 12, 1512–1550, doi:10.3762/bjoc.12.148

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• [27], the exact roles of AerE and AerF remain to be elucidated (Figure 4B). The succeeding NRPS adenylation domain is then directly activating Choi as a substrate. The aeruginoside assembly line does not contain a thioesterase or reductase domain [26]. It is thus currently unclear how the final

• between the condensation and adenylation domain. This sequence stretch does not show homology to any of the anabaenopeptin (Apt) biosynthesis proteins, suggesting a different mechanism of ureido bond formation for anabaenopeptins and syringolin [33]. Anatoxin Anatoxin-a (6) and homoanatoxin-a are potent

• cyanobacteria living in corraloid roots of Cycas circinalis. Schematic representation of enzymatic domains in A) nonribosomal peptide synthetases (NRPS); B) polyketide synthases (PKS) and C) the typical organisation of a ribosomal biosynthetic gene cluster. Abbreviations: C: Condensation domain; A: Adenylation