title: A bacterial homolog to the mitochondrial enoyl-CoA hydratase.
abstract: A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.
authors.affiliation: Department of Biology, Washington University, St. Louis, MO 63130.
authors.forename: D L
authors.initials: DL
authors.lastname: Beckman
authors.forename: R G
authors.initials: RG
authors.lastname: Kranz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004746:Enoyl-CoA Hydratase / Q000235:genetics*; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D051381:Rats; D016354:Rhodobacter capsulatus / Q000201:enzymology* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
chemical_list: D004746:Enoyl-CoA Hydratase