Article
Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidase.
Biochemistry - 20 Jun 2000
Carlos J L, Klenotic P A, Paetzel M, Strynadka N C, Dalbey R E
Abstract excerpt
Type I signal peptidase (SPase I) catalyzes the hydrolytic cleavage of the N-terminal signal peptide from translocated preproteins. SPase I belongs to a novel class of Ser proteases that utilize a Ser/Lys dyad catalytic mechanism instead of the classical Ser/His/Asp triad found in most Ser proteases. Recent X-ray crystallographic studies indicate that the backbone amide nitrogen of the catalytic Ser 90 and the...
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