• Publications
  • Influence
Molecular characterization of the enniatin synthetase gene encoding a multifunctional enzyme catalysing N‐methyldepsipeptide formation in Fusarium scirpi
The gene encoding the multifunctional enzyme enniatin synthetase from Fusarium scirpi (esyn1) was isolated and characterized by transcriptional mapping and expression studies in Escherichia coli and seems to harbour the N‐methyl‐transferase function of the multienzyme. Expand
Enniatin production by fusarium strains and its effect on potato tuber tissue
Several Fusarium strains produce the cyclohexadepsipeptide enniatin, a host-nonspecific phytotoxin, aHost-nONSpecificPhytot toxin that may affect their pathogenicity. Expand
Multifunctional Peptide Synthetases.
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
Cyclosporin synthetase. The most complex peptide synthesizing multienzyme polypeptide so far described.
Cyclosporin Synthetase shows cross-reactions with monoclonal antibodies directed against enniatin synthetase, and is an integral entity of the enzyme; this could be shown by a photoaffinity labeling method. Expand
Synthesis of beauvericin by a multifunctional enzyme.
Beauvericin synthetase, a multifunctional enzyme catalyzing depsipeptide formation in Beauveria bassiana was purified to near homogeneity and revealed that phenylalanine could be replaced by a number of other aromatic or aliphatic amino acids like beta-phenylserine, ortho-, meta-, para-fluorophenylalanines, isoleucine, norleucine and leucine. Expand
Arrangement of catalytic sites in the multifunctional enzyme enniatin synthetase.
Localization of the methyltransferase function of enniatin synthetase in an amino acid portion integrated into region EB was achieved by N-terminal sequencing of a photolabelled S-[methyl-14C]adenosyl methionine 45-kDa fragment and the identification of a photographer-labelled peptide Asn-Leu-Asn-Pro-Gly- Leu-Ser-Tyr. Expand
Mutational Analysis of the N-Methyltransferase Domain of the Multifunctional Enzyme Enniatin Synthetase*
N-Methylcyclopeptides like cyclosporins and enniatins are synthesized by multifunctional enzymes representing hybrid systems of peptide synthetases andS-adenosyl-l-methionineExpand