title: Enniatin synthetases from different fusaria exhibiting distinct amino acid specificities.
abstract: Enniatin synthetases from the cyclodepsipeptide producers Fusarium lateritium and Fusarium sambucinum were purified to homogeneity and characterized. Like the previously described enniatin synthetase from Fusarium scirpi both enzymes consist of a single polypeptide chain and are very similar concerning their Mr (250 kdaltons) and reaction mechanism. Limited proteolytic digests show only slight differences in their patterns in SDS-gels. Interestingly the synthetases differ in their amino acids specificities. The enzyme from the enniatin A producer F. sambucinum exhibits a high affinity to the substrate amino acids L-Leu and L-Ile. In contrast the synthetase from the enniatin B producer F. lateritium preferably accepts L-Val, the constituent amino acid of enniatin B.
authors.affiliation: Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Pieper
authors.forename: H
authors.initials: H
authors.lastname: Kleinkauf
authors.forename: R
authors.initials: R
authors.lastname: Zocher
mesh_terms: D000911:Antibodies, Monoclonal; D005670:Fusarium / Q000201:enzymology*; D010453:Peptide Synthases / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D013379:Substrate Specificity
chemical_list: D000911:Antibodies, Monoclonal; D010453:Peptide Synthases; C023122:enniatin B synthetase