title: Aminoacyl-S-enzyme intermediates in beta-hydroxylations and alpha,beta-desaturations of amino acids in peptide antibiotics.
abstract: Many of the alpha-amino acids found in proteins are shunted into microbial secondary metabolism to form peptide antibiotics by specific oxidation, including hydroxylation, at the beta carbon. Examples for the enzymatic hydroxylation of tyrosine and histidine and for desaturation of proline during covalent attachment as aminoacyl-S-pantetheinyl enzyme intermediates suggest a general strategy in peptide antibiotic biosynthesis.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
authors.forename: H
authors.initials: H
authors.lastname: Chen
authors.forename: M G
authors.initials: MG
authors.lastname: Thomas
authors.forename: S E
authors.initials: SE
authors.lastname: O'Connor
authors.forename: B K
authors.initials: BK
authors.lastname: Hubbard
authors.forename: M D
authors.initials: MD
authors.lastname: Burkart
authors.forename: C T
authors.initials: CT
authors.lastname: Walsh
mesh_terms: D000596:Amino Acids / Q000378:metabolism*; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D004798:Enzymes / Q000378:metabolism*; D006900:Hydroxylation; D010455:Peptides; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D000900:Anti-Bacterial Agents; D004798:Enzymes; D010455:Peptides