1993
DOI: 10.1021/bi00091a019
View full text
|
|

Abstract: To investigate the role of magnesium at the M3 site in Escherichia coli alkaline phosphatase, site-specific mutagenesis was used to substitute Glu-322, a ligand of the Mg2+ with either aspartic acid (E322D) or alanine (E322A). The residual Mg2+ content of the E322D enzyme is about 16-fold lower than that of the wild-type enzyme, and both mutant enzymes exhibit extremely poor catalytic activity compared to the wild-type enzyme. Mg2+ is a strong activator of the E322D enzyme. The hydrolysis activity of the E322D… Show more

Help me understand this page

Search citation statements

Order By: Relevance

Paper Sections

0
0
0
0
0

Citation Types

1
8
0

Publication Types

Select...

Relationship

0
0

Authors

Journals