User menu

Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation.

Bibliographic reference Gemayel, Rita ; Fortpied, Juliette ; Rzem, Rim ; Vertommen, Didier ; Veiga da Cunha, Maria ; et. al. Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation.. In: The FEBS journal, Vol. 274, no. 17, p. 4360-74 (2007)
Permanent URL http://hdl.handle.net/2078.1/11058
  1. Delpierre G., Rider M. H., Collard F., Stroobant V., Vanstapel F., Santos H., Van Schaftingen E., Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase, 10.2337/diabetes.49.10.1627
  2. DELPIERRE Ghislain, COLLARD François, FORTPIED Juliette, VAN SCHAFTINGEN Emile, Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes, 10.1042/bj20020325
  3. da-Cunha Maria VEIGA, Jacquemin Patrick, Delpierre Ghislain, Godfraind Catherine, Théate Ivan, Vertommen Didier, Clotman Frédéric, Lemaigre Frédéric, Devuyst Olivier, Van Schaftingen Emile, Increased protein glycation in fructosamine 3-kinase-deficient mice, 10.1042/bj20060684
  4. Collard F., Delpierre G., Stroobant V., Matthijs G., Van Schaftingen E., A Mammalian Protein Homologous to Fructosamine-3-Kinase Is a Ketosamine-3-Kinase Acting on Psicosamines and Ribulosamines but not on Fructosamines, 10.2337/diabetes.52.12.2888
  5. COLLARD François, WIAME Elsa, BERGANS Niki, FORTPIED Juliette, VERTOMMEN Didier, VANSTAPEL Florent, DELPIERRE Ghislain, VAN SCHAFTINGEN Emile, Fructosamine 3-kinase-related protein and deglycation in human erythrocytes, 10.1042/bj20040307
  6. FORTPIED Juliette, GEMAYEL Rita, STROOBANT Vincent, van SCHAFTINGEN Emile, Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme, 10.1042/bj20041976
  7. Fortpied Juliette, Gemayel Rita, Vertommen Didier, Van Schaftingen Emile, Identification of protein-ribulosamine-5-phosphatase as human low-molecular-mass protein tyrosine phosphatase-A, 10.1042/bj20061485
  8. Vincent, J Bacteriol, 181, 3472 (1999)
  9. Kuznetsova Ekaterina, Proudfoot Michael, Gonzalez Claudio F., Brown Greg, Omelchenko Marina V., Borozan Ivan, Carmel Liran, Wolf Yuri I., Mori Hirotada, Savchenko Alexei V., Arrowsmith Cheryl H., Koonin Eugene V., Edwards Aled M., Yakunin Alexander F., Genome-wide Analysis of Substrate Specificities of theEscherichia coliHaloacid Dehalogenase-like Phosphatase Family, 10.1074/jbc.m605449200
  10. Delplanque Jérôme, Delpierre Ghislain, Opperdoes Fred R., Van Schaftingen Emile, Tissue Distribution and Evolution of Fructosamine 3-Kinase and Fructosamine 3-Kinase-related Protein, 10.1074/jbc.m407678200
  11. Soulat D., Vaganay E., Duclos B., Genestier A.-L., Etienne J., Cozzone A. J., Staphylococcus aureus Contains Two Low-Molecular-Mass Phosphotyrosine Protein Phosphatases, 10.1128/jb.184.18.5194-5199.2002
  12. Delpierrre Ghislain, Vertommen Didier, Communi David, Rider Mark H., Van Schaftingen Emile, Identification of Fructosamine Residues Deglycated by Fructosamine-3-kinase in Human Hemoglobin, 10.1074/jbc.m402091200
  13. Wiame Elsa, Delpierre Ghislain, Collard François, Van Schaftingen Emile, Identification of a Pathway for the Utilization of the Amadori Product Fructoselysine inEscherichia coli, 10.1074/jbc.m200863200
  14. Wiame Elsa, Lamosa Pedro, Santos Helena, Van Schaftingen Emile, Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine, 10.1042/bj20051183
  15. McKay G. A., Thompson P. R., Wright G. D., Broad Spectrum Aminoglycoside Phosphotransferase Type III from Enterococcus: Overexpression, Purification, and Substrate Specificity, 10.1021/bi00188a024
  16. SANDWICK ROGER, JOHANSON MATTHEW, BREUER ELIZABETH, Maillard Reactions of Ribose 5-Phosphate and Amino Acids, 10.1196/annals.1333.011
  17. Veiga-da-Cunha M, Santos H, Van Schaftingen E, Pathway and regulation of erythritol formation in Leuconostoc oenos., 10.1128/jb.175.13.3941-3948.1993
  18. Li C., Clarke S., A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance., 10.1073/pnas.89.20.9885
  19. Moskovitz J, Rahman M A, Strassman J, Yancey S O, Kushner S R, Brot N, Weissbach H, Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage., 10.1128/jb.177.3.502-507.1995
  20. Collet Jean-Francois, D'Souza Jonathan Conrad, Jakob Ursula, Bardwell James C. A., Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site, 10.1074/jbc.m307818200
  21. Fortpied Juliette, Maliekal Pushpa, Vertommen Didier, Van Schaftingen Emile, Magnesium-dependent Phosphatase-1 Is a Protein-Fructosamine-6-phosphatase Potentially Involved in Glycation Repair, 10.1074/jbc.m513208200
  22. Park, J Biol Chem, 181, 149 (1949)
  23. 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
  24. Veiga-da-Cunha Maria, Courtois Stephane, Michel Alain, Gosselain Eric, Van Schaftingen Emile, Amino Acid Conservation in Animal Glucokinases : IDENTIFICATION OF RESIDUES IMPLICATED IN THE INTERACTION WITH THE REGULATORY PROTEIN, 10.1074/jbc.271.11.6292
  25. WIAME Elsa, VAN SCHAFTINGEN Emile, Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli, 10.1042/bj20031527
  26. 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
  27. Maliekal P., Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase, 10.1093/glycob/cwj050
  28. Itaya Koichi, Ui Michio, A new micromethod for the colorimetric determination of inorganic phosphate, 10.1016/0009-8981(66)90114-8
  29. Altschul S., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, 10.1093/nar/25.17.3389
  30. Thompson J., The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, 10.1093/nar/25.24.4876