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Nitrile hydratase of Rhodococcus sp. N‐774 Purification and amino acid sequences
Author(s) -
Endo Takakazu,
Watanabe Ichiro
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81218-9
Subject(s) - nitrile hydratase , rhodococcus , nitrile , chemistry , rhodococcus equi , amino acid , biochemistry , organic chemistry , enzyme , gene , virulence
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.