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pubmed:abstractText |
Many pharmacologically important peptides are synthesized nonribosomally by multimodular peptide synthetases (NRPSs). These enzyme templates consist of iterated modules that, in their number and organization, determine the primary structure of the corresponding peptide products. At the core of each module is an adenylation domain that recognizes the cognate substrate and activates it as its aminoacyl adenylate. Recently, the crystal structure of the phenylalanine-activating adenylation domain PheA was solved with phenylalanine and AMP, illustrating the structural basis for substrate recognition.
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pubmed:affiliation |
Biochemie/Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Strasse, D-35032, Marburg, Germany.
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