PMID:8476416

Citation	Zhang, HY, Zhang, J, Lin, L, Du, WY and Lu, J (1993) Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis. Biochem. Biophys. Res. Commun. 192:15-21
Abstract	Enzymatic generation of mutant libraries for random mutagenesis of aspartase gene from E. coli J2 was made. A mutant enzyme with 4-fold increase in aspartase activity was found. It is stable at pH7.5-9.0 (wild-type: pH7.0-8.0); heat stability and alpha-helicity are higher than those of the wild-type. By using site directed mutagenesis, the aspartase was activated by replacement of Lys-126 with an arginine residue. The mutation produced functional alterations without appreciable structure changes. The optimum pH for the mutant enzyme is 8.5. The stable pH range is 7.0-9.0. Heat stability is higher than that of the wild-type one. Activity of the mutant enzyme is about 5-fold as much as that of wild-type one.
Links	PubMed Online version:10.1006/bbrc.1993.1375
Keywords	Amino Acid Sequence; Aspartate Ammonia-Lyase/genetics; Aspartate Ammonia-Lyase/metabolism; Circular Dichroism; Enzyme Stability; Escherichia coli/enzymology; Hot Temperature; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis; Mutagenesis, Site-Directed
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.