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Article

Recovery of catalytic activity from an inactive aggregated mutant of l-aspartase.

Biochemical and biophysical research communications - 22 Oct 1999

Jayasekera M M, Viola R E

Abstract excerpt

Two highly conserved lysyl residues have been replaced with an arginine to examine their role in the mechanism of l-aspartase from Escherichia coli. Replacement of an active-site lysine results in a significant loss of catalytic efficiency [A. S. Saribas, J. F. Schindler, and R. E. Viola (1994) J. Biol. Chem. 269, 6313-6319], while replacement of the second lysine leads to a completely inactive and insoluble...

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PMID: 10529408
DOI: 10.1006/bbrc.1999.1570

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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