title: The N-terminal amino acid sequences of Brevibacterium sp. R312 nitrile hydratase.
abstract: Nitrile hydratase from Brevibacterium sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their N-terminal amino acid sequences were found to be identical to those of Rhodococcus sp. N-774 nitrile hydratase.
authors.affiliation: Chaire de Microbiologie Industrielle et de Génétique des Microorganismes, Ecole Nationale Supérieure Agronomique de Montpellier, France.
authors.forename: R
authors.initials: R
authors.lastname: Duran
authors.forename: C K
authors.initials: CK
authors.lastname: Chion
authors.forename: F
authors.initials: F
authors.lastname: Bigey
authors.forename: A
authors.initials: A
authors.lastname: Arnaud
authors.forename: P
authors.initials: P
authors.lastname: Galzy
mesh_terms: D000595:Amino Acid Sequence; D001951:Brevibacterium / Q000737:chemistry / Q000201:enzymology*; D003352:Corynebacterium / Q000201:enzymology; D006836:Hydro-Lyases / Q000737:chemistry* / Q000302:isolation & purification; D007218:Industrial Microbiology; D008969:Molecular Sequence Data; D011549:Pseudomonas / Q000201:enzymology
chemical_list: D006836:Hydro-Lyases; C048831:nitrile hydratase