The N-terminal amino acid sequences of Brevibacterium sp. R312 nitrile hydratase.
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.
Duran
R
R
Chaire de Microbiologie Industrielle et de Génétique des Microorganismes, Ecole Nationale Supérieure Agronomique de Montpellier, France.
Chion
C K
CK
Bigey
F
F
Arnaud
A
A
Galzy
P
P
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
D006836:Hydro-Lyases; C048831:nitrile hydratase