Glutamic acid residues as metal ligands in the active site of Escherichia coli alkaline phosphatase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1649, Issue 1, 2003, Pages 68-73

  Wojciechowski, Cheryl L ^a   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

Atomic absorption; Enzyme kinetics; Hydrolysis; Metalloenzyme; Transphosphorylation

Indexed keywords

ALKALINE PHOSPHATASE; GLUTAMIC ACID; ASPARTIC ACID; ESCHERICHIA COLI PROTEIN; HISTIDINE; LIGAND; MAGNESIUM; METAL; ZINC;

ARTICLE; BINDING SITE; CHEMICAL INTERACTION; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; AMINO ACID SUBSTITUTION; ENZYMOLOGY; GENETICS; HYDROLYSIS; KINETICS; METABOLISM; PH; PHOSPHORYLATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI;

ALKALINE PHOSPHATASE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BINDING SITES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HISTIDINE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LIGANDS; MAGNESIUM; METALS; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; STRUCTURE-ACTIVITY RELATIONSHIP; ZINC;

EID: 1242318675     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00156-0     Document Type: Article

References (26)

1. Kim E.E., Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures: two-metal ion catalysis. J. Mol. Biol. 218:1991;449-464.
2. Janeway C.M.L., Xu X., Murphy J.E., Chaidaroglou A., Kantrowitz E.R. Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis. Biochemistry. 32:1993;1601-1609.
3. Murphy J.E., Xu X., Kantrowitz E.R. Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution Escherichia coli alkaline phosphatase. J. Biol. Chem. 268:1993;21497-21500.
4. Murphy J.E., Tibbitts T.T., Kantrowitz E.R. Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases. J. Mol. Biol. 253:1995;604-617.
5. Tibbitts T.T., Murphy J.E., Kantrowitz E.R. Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. J. Mol. Biol. 257:1996;700-715.
6. Burley S.K., David P.R., Sweet R.M., Taylor A., Lipscomb W.N. Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 224:1992;113-140.
7. Ollis D.L., Kline C., Steitz T.A. Domain of E. coli DNA polymerase I showing sequence homology to T7 DNA polymerase. Nature. 313:1985;818-819.
8. Pelltier H., Sawaya M.R., Kumar A., Wilson S.H., Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer and ddCTP. Science. 264:1994;2022-2025.
9. Holtz K.M., Kantrowitz E.R. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. FEBS Lett. 462:1999;7-11.
10. Stec B., Holtz K.M., Kantrowitz E.R. A revised mechanism of the alkaline phosphatase reaction involving three metal ions. J. Mol. Biol. 299:2000;1303-1311.
11. Dudev T., Cowan J.A., Lim C. Competitive binding in magnesium coordination chemistry: water versus ligands of biological interest. J. Am. Chem. Soc. 121:1999;7665-7673.
12. Dudev T., Lim C. Metal binding in proteins: the effect of the dielectric medium. J. Phys. Chem., B. 104:2000;3692-3694.
13. Kunkel T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. U. S. A. 82:1985;488-492.
14. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U. S. A. 74:1977;5463-5467.
15. Chaidaroglou A., Brezinski J.D., Middleton S.A., Kantrowitz E.R. Function of arginine in the active site of Escherichia coli alkaline phosphatase. Biochemistry. 27:1988;8338-8343.
16. Garen A., Levinthal C. A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli: 1. Purification and characterization of alkaline phosphatase. Biochim. Biophys. Acta. 38:1960;470-483.
17. Alberts I.L., Nadassy K., Wodak S.J. Analysis of zinc binding sites in protein crystal structures. Protein Sci. 7:1998;1700-1716.
18. Hay R.W. Bio-Inorganic Chemistry. 1984;Wiley, New York.
19. Black C.B., Cowan J.A. Cowan J.A. The Biological Chemistry of Magnesium. 1995;159 VCH Publisher, New York.
20. Dudev T., Lim C. Tetrahedral vs. octahedral zinc complexes with ligands of biological interest: a DFT/CDM study. J. Am. Chem. Soc. 122:2000;11146-11153.
21. Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C. Crystallographic analysis of reversible metal binding observed in a mutant (Asp153→Gly) of Escherichia coli alkaline phosphatase. Biochemistry. 34:1995;13967-13973.
22. Dealwis C.G., Chen L., Brennan C., Mandecki W., Abad-Zapatero C. 3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity. Protein Eng. 8:1995;865-871.
23. Matlin A.R., Kendall D.A., Carano K.S., Banzon J.A., Klecka S.B., Solomon N.M. Enhanced catalysis by active-site mutagenesis at aspartic acid 153 in Escherichia coli alkaline phosphatase. Biochemistry. 31:1992;8196-8200.
24. 2+. J. Phys. Chem., B. 105:2001;4446-4452.
25. Ma L., Kantrowitz E.R. Mutations at histidine-412 alter zinc binding and eliminate transferase activity in Escherichia coli alkaline phosphatase. J. Biol. Chem. 269:1994;31614-31619.
26. Evans S.V. SETOR: hardware-lighted three-dimensional solid representations of macromolecules. J. Mol. Graph. 11:1993;134-138.