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A revised mechanism for the alkaline phosphatase reaction involving three metal ions.
Here, X-ray crystallography has been used to investigate the proposed double in-line displacement mechanism of Escherichia coli alkaline phosphatase in which two of the three active-site metal ionsExpand
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Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase.
Escherichia coli alkaline phosphatase exhibits maximal activity when Zn(2+) fills the M1 and M2 metal sites and Mg(2+) fills the M3 metal site. When other metals replace the zinc and magnesium, theExpand
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A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase.
The active sites of aminopeptidase A (PepA) from Escherichia coli and leucine aminopeptidase from bovine lens are isostructural, as shown by x-ray structures at 2.5 A and 1.6 A resolution,Expand
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A Model of the Transition State in the Alkaline Phosphatase Reaction*
A high resolution crystal structure ofEscherichia coli alkaline phosphatase in the presence of vanadate has been refined to 1.9 Å resolution. The vanadate ion takes on a trigonal bipyramidal geometryExpand
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Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme.
One of the best-studied examples of a class A beta-lactamase is Escherichia coli TEM-1 beta-lactamase. In this class of enzymes, the active-site serine residue takes on the role of a nucleophile andExpand
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Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis.
Site-specific mutagenesis was used to explore the roles of the side chains of residues Lys-328 and Asp-153 in Escherichia coli alkaline phosphatase. The D153H enzyme exhibits a 3.5-fold decrease inExpand
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Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis.
Crystal structures are known for aspartate carbamoyltransferase (ATCase) in the T and R states, with and without the allosteric activator adenosine triphosphate (ATP) or inhibitor cytidineExpand
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Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
In order to understand some of the differences between human placental, human, Saccharomyces cerevisiae and Escherichia coli alkaline phosphatases in specific activity, activation by magnesium, andExpand
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Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementation.
Escherichia coli alkaline phosphatase (EC 3.1.3.1) belongs to a rare group of enzymes that exhibit intragenic complementation. When certain mutant versions of alkaline phosphatase are combined, theExpand
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The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site‐specific mutagenesis
The proposed double in‐line displacement mechanism of Escherichia coli alkaline phosphatase (AP) involving two‐metal ion catalysis is based on NMR spectroscopic and X‐ray crystallographic studies.Expand
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