Enzymatic Reconstitution and Biosynthetic Investigation of the Bacterial Carbazole Neocarazostatin A.

Tricyclic carbazole is an important scaffold in many naturally occurring metabolites, as well as valuable building blocks. Here we report the reconstitution of the ring A formation of the bacterial neocarazostatin A carbazole metabolite. We provide evidence of the involvement of two unusual aromatic polyketide proteins.

Syntheses and structures of piperazin-1-ium Br ( = Cs or Rb): hybrid solids containing 'curtain wall' layers of face- and edge-sharing Br trigonal prisms.

The isostructural title compounds, poly[piperazin-1-ium [di-μ-bromido-caesium]], {(CHN)[CsBr]} , and poly[piperazin-1-ium [di-μ-bromido-rubidium]], {(CHN)[RbBr]} , contain singly-protonated piperazin-1-ium cations and unusual Br ( = Cs or Rb) trigonal prisms. The prisms are linked into a distinctive 'curtain wall' arrangement propagating in the (010) plane by face and edge sharing. In each case, a network of N-H⋯N, N-H⋯Br and N-H⋯(Br,Br) hydrogen bonds consolidates the structure.

Cyclic peptide production using a macrocyclase with enhanced substrate promiscuity and relaxed recognition determinants.

Macrocyclic peptides have promising therapeutic potential but the scaling up of their chemical synthesis is challenging. The cyanobactin macrocyclase PatG is an efficient tool for production but is limited to substrates containing 6-11 amino acids and at least one thiazoline or proline. Here we report a new cyanobactin macrocyclase that can cyclize longer peptide substrates and those not containing proline/thiazoline and thus allows exploring a wider chemical diversity.

A Blind Test of Computational Technique for Predicting the Likelihood of Peptide Sequences to Cyclize.

An in silico computational technique for predicting peptide sequences that can be cyclized by cyanobactin macrocyclases, e.g., PatG, is reported.