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Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate.

Bibliographic reference Collet, Jean-François ; Gerin, Isabelle ; Rider, Mark ; Veiga da Cunha, Maria ; Van Schaftingen, Emile. Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate.. In: FEBS letters, Vol. 408, no. 3, p. 281-4 (1997)
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  1. Borkenhagen Louise Fencil, Kennedy Eugene P., The enzymic equilibration of l-serine with O-phospho-serine, 10.1016/0006-3002(58)90463-3
  2. Neuhaus Francis C., Byrne William L., o-Phosphoserine phosphatase, 10.1016/0006-3002(58)90464-5
  3. Jaeken J., Detheux M., Van Maldergem L., Frijns J. P., Alliet P., Foulon M., Carchon H., Van Schaftingen E., 3-Phosphoglycerate dehydrogenase deficiency and 3-phosphoserine phosphatase deficiency: Inborn errors of serine biosynthesis, 10.1007/bf01799435
  4. Neuwald Andrew F., Stauffer George V., DNA sequence and characterization of theEscherichia coli serBgene, 10.1093/nar/13.19.7025
  5. Borkenhagen, J. Biol. Chem., 234, 849 (1959)
  6. Cagen, J. Biol. Chem., 247, 3382 (1972)
  7. Lennon Greg, Auffray Charles, Polymeropoulos Mihael, Soares Marcelo Bento, The I.M.A.G.E. Consortium: An Integrated Molecular Analysis of Genomes and Their Expression, 10.1006/geno.1996.0177
  8. Gaugler Béatrice, Brouwenstijn Nathalie, Vantomme Valérie, Szikora Jean-Pierre, Van der Spek Corry W., Patard Jean-Jacques, Boon Thierry, Schrier Peter, Van den Eynde Benoît J., A new gene coding for an antigen recognized by autologous cytolytic T lymphocytes on a human renal carcinoma, 10.1007/bf02602776
  9. Hérin M., Lemoine C., Weynants P., Vessière F., Van Pel A., Boon T., Knuth A., Devos R., Production of stable cytolytic T-cell clones directed against autologous human melanoma, 10.1002/ijc.2910390320
  10. Studier F.William, Moffatt Barbara A., Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes, 10.1016/0022-2836(86)90385-2
  11. Veiga-Da-Cunha Maria, Detheux Michel, Watelet Nathalie, Schaftingen Emile, Cloning and Expression of a Xenopus Liver cDNA Encoding a Fructose-Phosphate-Insensitive Regulatory Protein of Glucokinase, 10.1111/j.1432-1033.1994.00043.x
  12. Jaeken J, Detheux M, Van Maldergem L, Foulon M, Carchon H, Van Schaftingen E, 3-Phosphoglycerate dehydrogenase deficiency: an inborn error of serine biosynthesis., 10.1136/adc.74.6.542
  13. Hager Dayle A., Burgess Richard R., Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes, 10.1016/0003-2697(80)90013-5
  14. Rider Mark H., Puype Magda, Damme Jozef, Gevaert Kris, Boeck Stefan, D'Alayer Jacques, Rasmussen Hanna H., Celis Julio E., Vandekerckhove Joel, An Agarose-Based Gel-Concentration System for Microsequence and Mass Spectrometric Characterization of Proteins Previously Purified in Polyacrylamide Gels Starting at Low Picomole Levels, 10.1111/j.1432-1033.1995.0258i.x
  15. Fiske, J. Biol. Chem., 66, 375 (1925)
  16. McClard Ronald W., Synthesis and purification of [1-32P]fructose-1,6-bisphosphate with high specific radioactivity, 10.1016/0003-2697(79)90612-2
  17. Bradford Marion M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, 10.1016/0003-2697(76)90527-3
  18. Altschul Stephen F., Gish Warren, Miller Webb, Myers Eugene W., Lipman David J., Basic local alignment search tool, 10.1016/s0022-2836(05)80360-2
  19. Bridgers, J. Biol. Chem., 242, 2080 (1967)
  20. Corbin Jackie D., Reimann Erwin M., [41] Assay of cyclic AMP-dependent protein kinases, Hormone Action Part C: Cyclic Nucleotides (1974) ISBN:9780121819385 p.287-290, 10.1016/0076-6879(74)38044-5
  21. Witt Jonathan J., Roskoski Robert, Rapid protein kinase assay using phosphocellulose-paper absorption, 10.1016/0003-2697(75)90743-5
  22. LAEMMLI U. K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, 10.1038/227680a0
  23. Nechay, Fed. Proc., 45, 123 (1986)
  24. Veeranna, Shetty K. Taranath, Phosphoserine phosphatase of human brain: Partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs, 10.1007/bf01208581
  25. Engström Lorentz, Studies on calf-intestinal alkaline phosphatase II. Incorporation of inorganic phosphate into a highly purified enzyme preparation, 10.1016/0006-3002(61)90902-7
  26. Igarashi Mitsuo, Takahashi Hiroshi, Tsuyama Naoichi, Acid phosphatase from rat liver. Studies on the active center, 10.1016/0005-2744(70)90231-7
  27. Pilkis, J. Biol. Chem., 258, 6135 (1983)
  28. Rose Zelda B., Evidence for a phosphohistidine protein intermediate in the phosphoglycerate mutase reaction, 10.1016/0003-9861(70)90095-0
  29. Guan, J. Biol. Chem., 266, 17026 (1991)
  30. Hokin L. E., Sastry P. S., Galsworthy P. R., Yoda A., Evidence that a phosphorylated intermediate in a brain transport adenosine triphosphatase is an acyl phosphate., 10.1073/pnas.54.1.177
  31. Post, J. Biol. Chem., 248, 6993 (1973)