title: Purification and Properties of Glycine Oxidase from Pseudomonas putida KT2440.
abstract: Glycine oxidase, encoded by the thiO gene, participates in the biosynthesis of thiamin by providing glyoxyl imine to form the thiazole moiety of thiamin. We have purified and characterized ThiO from Pseudomonas putida KT2440. It has a monomeric structure that is distinct from the homotetrameric ThiOs from Bacillus subtilis and Geobacillus kaustophilus. The P. putida ThiO is unique in that glycine is its preferred substrate, which differs markedly from the B. subtilis and G. kaustophilus enzymes that use D-proline as the preferred substrate.
authors.affiliation: College of Life Sciences, Ritsumeikan University.
authors.forename: Messele Yohannes
authors.initials: MY
authors.lastname: Equar
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Tani
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Mihara
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D001412:Bacillus subtilis / Q000201:enzymology; D056506:Geobacillus / Q000201:enzymology; D005998:Glycine / Q000378:metabolism*; D015394:Molecular Structure; D016958:Pseudomonas putida / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000594:Amino Acid Oxidoreductases; C115925:glycine oxidase; D005998:Glycine