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A nonribosomal system of peptide biosynthesis.
This review covers peptide structures originating from the concerted action of enzyme systems without the direct participation of nucleic acids. Biosynthesis proceeds by formation of linear peptidylExpand
Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis.
A specific alanine racemase, which is a key enzyme in the biosynthesis of the undecapeptide cyclosporin A, was purified to electrophoretic homogeneity from the fungus Tolypocladium niveum. This isExpand
A highly specific D-hydroxyisovalerate dehydrogenase from the enniatin producer Fusarium sambucinum.
A highly specific D-hydroxyisovalerate (D-HIV) dehydrogenase, which is a key enzyme in depsipeptide synthesis, was purified to near homogeneity from the enniatin-producing fungus Fusarium sambucinum.Expand
Characterization of two carnosine-degrading enzymes from rat brain. Partial purification and characterization of a carnosinase and a beta-alanyl-arginine hydrolase.
From rat brain extracts, two carnosine-degrading enzymes have been identified and partially purified by ion-exchange chromatography, hydrophobic interaction chromatography on phenyl-Sepharose CL-4BExpand
Nonribosomal biosynthesis of peptide antibiotics.
Peptide antibiotics are known to contain non-protein amino acids, D-amino acids, hydroxy acids, and other unusual constituents. In addition they may be modified by N-methylation and cyclizationExpand
Biosynthesis of carnosine and related peptides by glial cells in primary culture.
Synthesis of carnosine (beta-alanylhistidine) and related peptides by glial cells in primary culture could be demonstrated. After incubation with [3H]beta-alanine, the radiolabeled dipeptides couldExpand
Synthesis of beauvericin by a multifunctional enzyme.
Beauvericin synthetase, a multifunctional enzyme catalyzing depsipeptide formation in Beauveria bassiana was purified to near homogeneity. The enzyme consists of a single polypeptide chain with aExpand
Expression of an active adenylate‐forming domain of peptide synthetases corresponding to acyl‐CoA‐synthetases
Peptide synthetases and acyl‐CoA‐synthetases form acyl adenylates which are transferred to CoA or enzyme‐bound pantetheine. To verify the existence of an adenylate domain in peptide synthetases, aExpand
Biosynthesis of PF1022A and Related Cyclooctadepsipeptides*
PF1022A belongs to a recently identified class of N-methylated cyclooctadepsipeptides (CODPs) with strong anthelmintic properties. Described here is the cell-free synthesis of this CODP and relatedExpand
The activation of amino acids for biosynthesis of gramicidin S.