Nitrile hydratase of Rhodococcus sp. N‐774 Purification and amino acid sequences

FEBS Letters

Endo, Takakazu¹  Watanabe, Ichiro¹ 

[1] Central Research Laboratory, Nitto Chemical Industry Co., 10-1, Daikoku-cho, Tsurumi-ku, Yokohama 230, Japan

关键词: Nitrile hydratase;    Bacteria;    Amino acid sequence;    NHase;    nitrile hydratase;    HPLC;    high-performance liquid chromatography;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(89)81218-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nitrile hydratase of Rhodococcus sp. N-774 was purified and crystallized. The enzyme is composed of two different subunits (molecular masses: subunit α, 28 500 Da; subunit β, 29 000 Da). The amino-terminal amino acid sequence of each subunit was determined. There is no sequence homology between the two subunits, suggesting that the peptides originate from different cistrons. The activity of the purified enzyme did not decrease during incubation in the dark, whereas it gradually decreased in intact cells.

【 授权许可】

Unknown