title: Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms.
abstract: The aromatic amino acids phenylalanine and tyrosine represent essential sources of high value natural aromatic compounds for human health and industry. Depending on the organism, alternative routes exist for their synthesis. Phenylalanine and tyrosine are synthesized either via phenylpyruvate/4-hydroxyphenylpyruvate or via arogenate. In arogenate-competent microorganisms, an aminotransferase is required for the transamination of prephenate into arogenate, but the identity of the genes is still unknown. We present here the first identification of prephenate aminotransferases (PATs) in seven arogenate-competent microorganisms and the discovery that PAT activity is provided by three different classes of aminotransferase, which belong to two different fold types of pyridoxal phosphate enzymes: an aspartate aminotransferase subgroup 1β in tested α- and β-proteobacteria, a branched-chain aminotransferase in tested cyanobacteria, and an N-succinyldiaminopimelate aminotransferase in tested actinobacteria and in the β-proteobacterium Nitrosomonas europaea. Recombinant PAT enzymes exhibit high activity toward prephenate, indicating that the corresponding genes encode bona fide PAT. PAT functionality was acquired without other modification of substrate specificity and is not a general catalytic property of the three classes of aminotransferases.
authors.affiliation: From the Commissariat à l'Energie Atomique, Direction des Sciences du Vivant, institut de Recherches en Technologies et en Sciences pour le Vivant, Laboratoire de Physiologie Cellulaire et Végétale, F-38054 Grenoble, France.
authors.forename: Matthieu
authors.initials: M
authors.lastname: Graindorge
authors.forename: Cécile
authors.initials: C
authors.lastname: Giustini
authors.forename: Alexandra
authors.initials: A
authors.lastname: Kraut
authors.forename: Lucas
authors.initials: L
authors.lastname: Moyet
authors.forename: Gilles
authors.initials: G
authors.lastname: Curien
authors.forename: Michel
authors.initials: M
authors.lastname: Matringe
mesh_terms: D000600:Amino Acids, Dicarboxylic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D053138:Cyclohexenes / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D006801:Humans; D011732:Pyridoxal Phosphate / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000637:Transaminases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D000600:Amino Acids, Dicarboxylic; D001426:Bacterial Proteins; D053138:Cyclohexenes; D014443:Tyrosine; C015478:pretyrosine; D011732:Pyridoxal Phosphate; D000637:Transaminases; C044954:prephenate aminotransferase
keywords: Amination; Amino Acid; Bacterial Metabolism; Enzymes; Tyrosine