title: Identification and characterization of 2-oxoglutarate-dependent dioxygenases catalyzing selective cis-hydroxylation of proline and pipecolinic acid from actinomycetes.
abstract: Microbial hydroxylases were screened for the capacity to effect direct hydroxylation of proline and pipecolinic acid, based on genomic information. Of the eight candidates screened, 2-oxoglutarate-dependent hydroxylase from Streptosporangium roseum NBRC 3776(T) and aspartyl/asparaginyl β-hydroxylase from Catenulispora acidiphila NBRC 102108(T) showed both proline and pipecolinic acid hydroxylation activities. In the case of l-proline hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-proline and cis-4-hydroxy-l-proline, and cis-4-hydroxy-l-proline was preferentially produced. In the case of l-pipecolinic acid hydroxylation, both enzymes catalyzed the simultaneous formation of cis-3-hydroxy-l-pipecolinic acid and cis-5-hydroxy-l-pipecolinic acid. While the former enzyme preferentially produced cis-3-hydroxy-l-pipecolinic acid, the latter enzyme preferentially produced cis-5-hydroxy-l-pipecolinic acid.
authors.affiliation: Research Institute for Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan.
authors.forename: Ryotaro
authors.initials: R
authors.lastname: Hara
authors.affiliation: Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan.
authors.forename: Naoko
authors.initials: N
authors.lastname: Uchiumi
authors.affiliation: Research Institute for Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan; Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, 3-4-1 Ohkubo, Shinjuku-ku, Tokyo 169-8555, Japan. Electronic address: kkino@waseda.jp.
authors.forename: Kuniki
authors.initials: K
authors.lastname: Kino
mesh_terms: D039903:Actinobacteria / Q000145:classification / Q000201:enzymology*; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology; D002264:Carboxylic Acids / Q000378:metabolism*; D049308:Dioxygenases / Q000235:genetics / Q000502:physiology*; D006900:Hydroxylation; D006909:Hydroxyproline / Q000378:metabolism*; D007656:Ketoglutaric Acids / Q000378:metabolism*; D008956:Models, Chemical
chemical_list: D001426:Bacterial Proteins; D002264:Carboxylic Acids; D007656:Ketoglutaric Acids; D049308:Dioxygenases; D006909:Hydroxyproline
keywords: Dioxygenase; Hydroxylase; Hydroxylation; Hydroxypipecolinic acid; Hydroxyproline