3-D structure of a mutant (Asp101→Ser) of E. coli alkaline phosphatase with higher catalytic activity

Mutagenesis of the absolutely conserved residue Asp101 of the non-specific monoesterase alkaline phosphatase (E.C. 3.1.3.1) from E. coli has produced an enzyme with increased k sub(cat). The carboxyl group of the Asp101 residue has been proposed to be involved in the positioning of Arg166 and the fo...

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Veröffentlicht in:	Protein engineering 1992, Vol.5 (7), p.605-610
Hauptverfasser:	LIQING CHEN, NEIDHART, D, KOHLBRENNER, W. M, MANDECKI, W, BELL, S, SOWADSKI, J, ABAD-ZAPATERO, C
Format:	Artikel
Sprache:	eng
Schlagworte:	alkaline phosphatase Biological and medical sciences Biotechnology crystal structure effects on Escherichia coli Fundamental and applied biological sciences. Psychology Methods. Procedures. Technologies Protein engineering site-directed mutagenesis X-ray diffraction
Online-Zugang:	Volltext
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