Significant progress has been made in the past four decades toward understanding the
structures and synthesis of bioactive peptides produced by microorganisms through the …

SUMMARY Coronatine, syringomycin, syringopeptin, tabtoxin, and phaseolotoxin are the
most intensively studied phytotoxins of Pseudomonas syringae, and each contributes …

Background Many pharmacologically important peptides are synthesized nonribosomally by
multimodular peptide synthetases (NRPSs). These enzyme templates consist of iterated …

▪ Abstract Bacteria and fungi use large multifunctional enzymes, the so-called nonribosomal
peptide synthetases (NRPSs), to produce peptides of broad structural and biological activity …

Abstract Background: Nonribosomal peptide synthetases (NRPSs) are large modular
proteins that selectively bind, activate and condense amino acids in an ordered manner …

Covering: 1994 to 2002 The ability to synthesize nonribosomally small bioactive peptides
that find application in modern medicine is widely spread among microorganisms. As broad …

Background: Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the
presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin …

The ANL superfamily of adenylating enzymes contains acyl-and aryl-CoA synthetases, firefly
luciferase, and the adenylation domains of the modular non-ribosomal peptide synthetases …

Research into bioactive natural products began when A. Fleming discovered the antibiotic
activity of the peptide derivative penicillin produced by the fungal host organism Penicillium …

Covering up to the end of 2011 Many pharmaceuticals on the market today belong to a large
class of natural products called nonribosomal peptides (NRPs). Originating from bacteria …