A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase.

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...

Topics

Binding Sites
Catalysis
Endopeptidases
Enzyme Inhibitors
Escherichia coli
Ethylmaleimide
Lysine
Membrane Proteins
Mutation
Serine
Serine Endopeptidases

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