title: Studies on lysine:N6-hydroxylation by cell-free systems of Aerobacter aerogenes 62-1.
abstract: Electron microscopic examination has revealed the vesicular nature of the membrane component, of the cell-free system of Aerobacter aerogenes 62-1, which catalyses lysine: N6-hydroxylation. Regardless of the orientation of the vesicles, N-hydroxylation process is still stimulated by pyruvate. Both pyruvate oxidation and lysine: N6-hydroxylation were inhibited by protonophores and Gramicidin S.
authors.affiliation: Guelph-Waterloo Centre for Graduate Work in Chemistry, University of Waterloo, Canada.
authors.forename: C J
authors.initials: CJ
authors.lastname: Goh
authors.forename: E W
authors.initials: EW
authors.lastname: Szczepan
authors.forename: N
authors.initials: N
authors.lastname: Menhart
authors.forename: T
authors.initials: T
authors.lastname: Viswanatha
mesh_terms: D001433:Bacteriolysis; D002384:Catalysis; D002462:Cell Membrane / Q000502:physiology; D002474:Cell-Free System; D004754:Enterobacter / Q000201:enzymology / Q000502:physiology* / Q000648:ultrastructure; D004755:Enterobacteriaceae / Q000502:physiology*; D006900:Hydroxylation; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D011773:Pyruvates / Q000502:physiology; D013347:Subcellular Fractions
chemical_list: D011773:Pyruvates; C049468:N(6)-acetyl-N(6)-hydroxylysine; D008239:Lysine