Product alkaline phosphatase
alkaline phosphatase |
homodimer |
metalloenzyme, Zn, Mn |
NULL
- Gentschev, I., J. Hess, W. Goebel 1990. Change in the cellular localization of alkaline phosphatase by alteration of its carboxy-terminal sequence. Mol.Gen.Genet. 222:211-216
- Freimuth, P.I., J.W. Taylor, E.T. Kaiser 1990. Introduction of guest peptides into Escherichia coli alkaline phosphatase. Excision and purification of a dynorphin analogue from an active chimeric protein. J.Biol.Chem. 265:896-901
- Dealwis, C.G., L. Chen, C. Brennan, W. Mandecki, C. Abad-Zapatero 1995. 3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity. Protein Eng 8:865-871
- Murphy, J.E., T.T. Tibbitts, E.R. Kantrowitz 1995. 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. 253:604-0
- Ma, L., T.T. Tibbitts, E.R. Kantrowitz 1995. Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites. Protein Sci. 4:1498-0
- Tibbitts, T.T., J.E. Murphy, E.R. Kantrowitz 1996. Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. J.Mol.Biol. 257:700-715
- Sarkar, S.N., N. Ghosh 1996. Reversible unfolding of Escherichia coli alkaline phosphatase: active site can be reconstituted by a number of pathways. Arch.Biochem. Biophys. 330:174-180
- Tibbitts, T.T., J.E. Murphy, E.R. Kantrowitz 1996. Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase. J.Mol.Biol. 257:700-715
- Karamyshev, A.L., Z.N. Karamysheva, A.V. Kajava, V.N. Ksenzenko, M.A. Nesmeyanova 1998. Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. J.Mol.Biol. 277:859-870
- Kajava, A.V., S.N. Zolov, A.E. Kalinin, M.A. Nesmeyanova 2000. The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria. J.Bacteriol. 182:2163-2169
- O'Brien, P.J., D. Herschlag 2001. Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase. Biochemistry 40:5691-5699
- Muller, BH, C Lamoure, MH Le Du, L Cattolico, E Lajeunesse, F Lemaître, A Pearson, F Ducancel, A Ménez, JC Boulain 2001. Improving Escherichia coli alkaline phosphatase efficacy by additional mutations inside and outside the catalytic pocket. Chembiochem 2(7-8):517-23.