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Directed evolution of alpha-aspartyl dipeptidase from Salmonella typhimurium.

Abstract：

:Model-free approaches (error-prone PCR to introduce random mutations, DNA shuffling to combine positive mutations, and screening of the resultant mutant libraries) have been used to enhance the catalytic activity and thermostability of alpha-aspartyl dipeptidase from Salmonella typhimurium, which is uniquely able to hydrolyze Asp-X dipeptides (where X is any amino acid) and one tripeptide (Asp-Gly-Gly). Under double selective pressures of activity and thermostability, through two rounds of error-prone PCR and three sequential generations of DNA shuffling, coupled with screening, a mutant pepEM3074 with approximately 47-fold increased enzyme activity compared with its wild-type parent was obtained. Moreover, the stability of pepEM3074 is increased significantly. Three amino acid substitutions (Asn89His, Gln153Glu, and Leu205Arg), two of them are near the active site and substrate binding pocket, were identified by sequencing the genes encoding this evolved enzyme. The mechanism of the enhancement of activity and stability was analyzed in this paper.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kong X,Liu Y,Gou X,Zhu S,Zhang H,Wang X,Zhang J

doi

10.1006/bbrc.2001.5937

subject

Has Abstract

pub_date

2001-11-23 00:00:00

pages

137-42

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95937-6

journal_volume

289

pub_type

杂志文章

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