Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions.
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[1] J. Vincent,et al. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. , 1991, The Journal of biological chemistry.
[2] E. E. Kim,et al. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. , 1991, Journal of molecular biology.
[3] Z. Zhang,et al. Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. , 1991, The Journal of biological chemistry.
[4] T. Steitz,et al. Structural basis for the 3′‐5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. , 1991, The EMBO journal.
[5] J. Vincent,et al. Proteins Containing Oxo-Bridged Dinuclear Iron Centers: A Bioinorganic Perspective , 1990 .
[6] J. Vincent,et al. An enzyme with a double identity: purple acid phosphatase and tartrate‐resistant acid phosphatase , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[7] L. Que,et al. Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active site and interaction with the hydroxo bridge , 1990 .
[8] J. Vincent,et al. Sequence homology between purple acid phosphatases and phosphoprotein phosphatases , 1990, FEBS letters.
[9] Edward Hough,et al. High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus , 1989, Nature.
[10] P. Aisen,et al. The binuclear iron centers of uteroferrin and the purple acid phosphatases , 1988 .
[11] D. Graves,et al. Mechanistic aspects of the low-molecular-weight phosphatase activity of the calmodulin-activated phosphatase, calcineurin. , 1986, The Journal of biological chemistry.
[12] S. Buchwald,et al. Stereochemistry of nucleophilic displacement on two phosphoric monoesters and a phosphoguanidine: the role of metaphosphate , 1984 .
[13] M. King,et al. The calmodulin-dependent activation and deactivation of the phosphoprotein phosphatase, calcineurin, and the effect of nucleotides, pyrophosphate, and divalent metal ions. Identification of calcineurin as a Zn and Fe metalloenzyme. , 1984, The Journal of biological chemistry.
[14] P. Gettins,et al. Alkaline phosphatase, solution structure, and mechanism. , 2006, Advances in enzymology and related areas of molecular biology.
[15] R. V. Etten,et al. HUMAN PROSTATIC ACID PHOSPHATASE: A HISTIDINE PHOSPHATASE * , 1982, Annals of the New York Academy of Sciences.
[16] R. V. Van Etten,et al. Human liver acid phosphatases: purification and properties of a low-molecular-weight isoenzyme. , 1982, Archives of biochemistry and biophysics.
[17] S. Buchwald,et al. Stereochemistry of phospho transfer catalyzed by bovine liver acid phosphatase. , 1981, The Journal of biological chemistry.
[18] C. Walsh,et al. Enzymatic Reaction Mechanisms , 1978 .
[19] Stephen R. Jones,et al. Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase , 1978, Nature.
[20] H. Chaimovich,et al. Steady state kinetics and effect of SH inhibitors on acid phosphatase from bovine brain. , 1975, Biochimica et biophysica acta.
[21] G. E. EDEN. Water as a Resource , 1972, Nature.
[22] H. N. Fernley,et al. Studies on alkaline phosphatase. Phosphorylation of calf-intestinal alkaline phosphatase by 32P-labelled pyrophosphate. , 1968, The Biochemical journal.
[23] L. G. Sillén. Quantitative studies of hydrolytic equilibria , 1959 .