Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase

Site-directed mutagenesis was used to examine the catalytic importance of 2 histidine and 4 arginine residues in Escherichia coli periplasmic acid phosphatase (EcAP). The residues that were selected as targets for mutagenesis were those that were also conserved in a number of high molecular weight a...

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Veröffentlicht in:	The Journal of biological chemistry 1992-11, Vol.267 (32), p.22830-22836
Hauptverfasser:	Ostanin, K, Harms, E H, Stevis, P E, Kuciel, R, Zhou, M M, Van Etten, R L
Format:	Artikel
Sprache:	eng
Schlagworte:	acid phosphatase Acid Phosphatase - genetics Acid Phosphatase - isolation & purification Acid Phosphatase - metabolism Base Sequence C.D Circular Dichroism Cloning, Molecular DNA, Bacterial - genetics DNA, Bacterial - isolation & purification Electrophoresis, Polyacrylamide Gel Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics expression Genes, Bacterial Kinetics Molecular Sequence Data Mutagenesis, Site-Directed N.M.R Oligodeoxyribonucleotides Plasmids Protein Conformation Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping site-directed mutagenesis Substrate Specificity
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