Article
A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase.
The Journal of biological chemistry - 25 Dec 1993
Tschantz W R, Sung M, Delgado-Partin V M, Dalbey R E
Abstract excerpt
We report that a thiol leader peptidase, produced by replacing the critical serine at position 90 with a cysteine residue, is enzymatically active. In contrast to the wild-type leader peptidase, the thiol enzyme can be inactivated with N-ethylmaleimide, a cysteine-specific reagent. This strongly suggests that the serine 90 is involved in catalysis and is located at the active site. Of the three conserved basic...
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