메뉴 건너뛰기




Volumn 274, Issue 17, 2007, Pages 4360-4374

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

Author keywords

Deglycation; Erythrose 4 phosphate; Fructosamine; Glycation; Ribose 5 phosphate

Indexed keywords

AMINO ACID; AMINOKETONE; CADAVERINE; ERYTHRULOSELYSINE 4 PHOSPHATE; FRUCTOSAMINE; FRUCTOSAMINE 3 KINASE; LYSINE DERIVATIVE; PHOSPHOTRANSFERASE; PROTEIN TYROSINE PHOSPHATASE; RIBULOSAMINE 3 PHOSPHATASE; RIBULOSAMINE 5 PHOSPHATE; RIBULOSELYSINE 5 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 34548128354     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05948.x     Document Type: Article
Times cited : (32)

References (30)
  • 2
    • 0036683724 scopus 로고    scopus 로고
    • Fructosamine-3-kinase is involved in an intracellular deglycation pathway
    • Delpierre G, Collard F, Fortpied J Van Schaftingen E (2002) Fructosamine-3-kinase is involved in an intracellular deglycation pathway. Biochem J 365, 801 808.
    • (2002) Biochem J , vol.365 , pp. 801-808
    • Delpierre, G.1    Collard, F.2    Fortpied, J.3    Van Schaftingen, E.4
  • 4
    • 0345275810 scopus 로고    scopus 로고
    • A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines
    • Collard F, Delpierre G, Stroobant V, Matthijs G Van Schaftingen E (2003) A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes 12, 2888 2895.
    • (2003) Diabetes , vol.12 , pp. 2888-2895
    • Collard, F.1    Delpierre, G.2    Stroobant, V.3    Matthijs, G.4    Van Schaftingen, E.5
  • 6
    • 21744454994 scopus 로고    scopus 로고
    • Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme
    • Fortpied J, Gemayel R, Stroobant V Van Schaftingen E (2005) Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme. Biochem J 388, 795 802.
    • (2005) Biochem J , vol.388 , pp. 795-802
    • Fortpied, J.1    Gemayel, R.2    Stroobant, V.3    Van Schaftingen, E.4
  • 7
    • 34547829292 scopus 로고    scopus 로고
    • Identification of protein-ribulosamine-5-phosphatase as human low-molecular-weight protein-tyrosine-phosphatase-A
    • Fortpied J, Gemayel R, Vertommen D Van Schaftingen E (2007) Identification of protein-ribulosamine-5-phosphatase as human low-molecular-weight protein-tyrosine-phosphatase-A. Biochem J 406, 139 145.
    • (2007) Biochem J , vol.406 , pp. 139-145
    • Fortpied, J.1    Gemayel, R.2    Vertommen, D.3    Van Schaftingen, E.4
  • 8
    • 0033038516 scopus 로고    scopus 로고
    • Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, Wzb
    • Vincent C, Doublet P, Grangeasse C, Vaganay E, Cozzone AJ Duclos B (1999) Cells of Escherichia coli contain a protein-tyrosine kinase, Wzc, and a phosphotyrosine-protein phosphatase, Wzb. J Bacteriol 181, 3472 3477.
    • (1999) J Bacteriol , vol.181 , pp. 3472-3477
    • Vincent, C.1    Doublet, P.2    Grangeasse, C.3    Vaganay, E.4    Cozzone, A.J.5    Duclos, B.6
  • 10
    • 8744307268 scopus 로고    scopus 로고
    • Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
    • Delplanque J, Delpierre G, Opperdoes FR Van Schaftingen E (2004) Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein. J Biol Chem 279, 46606 46613.
    • (2004) J Biol Chem , vol.279 , pp. 46606-46613
    • Delplanque, J.1    Delpierre, G.2    Opperdoes, F.R.3    Van Schaftingen, E.4
  • 11
    • 0036723797 scopus 로고    scopus 로고
    • Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases
    • Soulat D, Vaganay E, Duclos B, Genestier A, Etienne J Cozzone AJ (2002) Staphylococcus aureus contains two low-molecular-mass phosphotyrosine protein phosphatases. J Bacteriol 184, 5194 5199.
    • (2002) J Bacteriol , vol.184 , pp. 5194-5199
    • Soulat, D.1    Vaganay, E.2    Duclos, B.3    Genestier, A.4    Etienne, J.5    Cozzone, A.J.6
  • 12
    • 3042644024 scopus 로고    scopus 로고
    • Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin
    • Delpierre G, Vertommen D, Communi D, Rider MH Van Schaftingen E (2004) Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin. J Biol Chem 279, 27613 27620.
    • (2004) J Biol Chem , vol.279 , pp. 27613-27620
    • Delpierre, G.1    Vertommen, D.2    Communi, D.3    Rider, M.H.4    Van Schaftingen, E.5
  • 13
    • 0037044736 scopus 로고    scopus 로고
    • Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli
    • Wiame E, Delpierre G, Collard F Van Schaftingen E (2002) Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli. J Biol Chem 277, 42523 42529.
    • (2002) J Biol Chem , vol.277 , pp. 42523-42529
    • Wiame, E.1    Delpierre, G.2    Collard, F.3    Van Schaftingen, E.4
  • 14
    • 29144503142 scopus 로고    scopus 로고
    • Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine
    • Wiame E, Lamosa P, Santos H Van Schaftingen E (2005) Identification of glucoselysine-6-phosphate deglycase, an enzyme involved in the metabolism of the fructation product glucoselysine. Biochem J 392, 263 269.
    • (2005) Biochem J , vol.392 , pp. 263-269
    • Wiame, E.1    Lamosa, P.2    Santos, H.3    Van Schaftingen, E.4
  • 15
    • 0028358078 scopus 로고
    • Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: Overexpression, purification, and substrate specificity
    • McKay GA, Thompson PR Wright GD (1994) Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity. Biochemistry 33, 6936 6944.
    • (1994) Biochemistry , vol.33 , pp. 6936-6944
    • McKay, G.A.1    Thompson, P.R.2    Wright, G.D.3
  • 16
    • 23744501806 scopus 로고    scopus 로고
    • Maillard reactions of ribose 5-phosphate and amino acids
    • Sandwick R, Johanson M Breuer E (2005) Maillard reactions of ribose 5-phosphate and amino acids. Ann N Y Acad Sci 1043, 85 96.
    • (2005) Ann N Y Acad Sci , vol.1043 , pp. 85-96
    • Sandwick, R.1    Johanson, M.2    Breuer, E.3
  • 17
    • 0027209897 scopus 로고
    • Pathway and regulation of erythritol formation in Leuconostoc oenos
    • Veiga-da-Cunha M, Santos H Van Schaftingen E (1993) Pathway and regulation of erythritol formation in Leuconostoc oenos. J Bacteriol 175, 3941 3948.
    • (1993) J Bacteriol , vol.175 , pp. 3941-3948
    • Veiga-Da-Cunha, M.1    Santos, H.2    Van Schaftingen, E.3
  • 18
    • 0026661893 scopus 로고
    • A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance
    • Li C Clarke S (1992) A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance. Proc Natl Acad Sci USA 89, 9885 9889.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9885-9889
    • Li, C.1    Clarke, S.2
  • 19
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
    • Moskovitz J, Rahman MA, Strassman J, Yancey SO, Kushner SR, Brot N Weissbach H (1995) Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol 177, 502 507.
    • (1995) J Bacteriol , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 20
    • 0242580976 scopus 로고    scopus 로고
    • Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site
    • Collet JF, D'Souza JC, Jakob U Bardwell JC (2003) Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J Biol Chem 278, 45325 45332.
    • (2003) J Biol Chem , vol.278 , pp. 45325-45332
    • Collet, J.F.1    D'Souza, J.C.2    Jakob, U.3    Bardwell, J.C.4
  • 21
    • 33745866585 scopus 로고    scopus 로고
    • Magnesium-dependent phosphatase-1 is a protein-fructosamine-6-phosphatase potentially involved in glycation repair
    • Fortpied J, Maliekal P, Vertommen D Van Schaftingen E (2006) Magnesium-dependent phosphatase-1 is a protein-fructosamine-6-phosphatase potentially involved in glycation repair. J Biol Chem 281, 18378 18385.
    • (2006) J Biol Chem , vol.281 , pp. 18378-18385
    • Fortpied, J.1    Maliekal, P.2    Vertommen, D.3    Van Schaftingen, E.4
  • 22
    • 76549203762 scopus 로고
    • A submicrodetermination of glucose
    • Park JT Johnson MJ (1949) A submicrodetermination of glucose. J Biol Chem 181, 149 151.
    • (1949) J Biol Chem , vol.181 , pp. 149-151
    • Park, J.T.1    Johnson, M.J.2
  • 23
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW Moffatt BA (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189, 113 130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 24
    • 0029918678 scopus 로고    scopus 로고
    • Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein
    • Veiga-da-Cunha M, Courtois S, Michel A, Gosselain E Van Schaftingen E (1996) Amino acid conservation in animal glucokinases. Identification of residues implicated in the interaction with the regulatory protein. J Biol Chem 271, 6292 6297.
    • (1996) J Biol Chem , vol.271 , pp. 6292-6297
    • Veiga-Da-Cunha, M.1    Courtois, S.2    Michel, A.3    Gosselain, E.4    Van Schaftingen, E.5
  • 25
    • 1642463960 scopus 로고    scopus 로고
    • Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli
    • Wiame E Van Schaftingen E (2004) Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli. Biochem J 378, 1047 1052.
    • (2004) Biochem J , vol.378 , pp. 1047-1052
    • Wiame, E.1    Van Schaftingen, E.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye-binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 31144464808 scopus 로고    scopus 로고
    • Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
    • Maliekal P, Vertommen D, Delpierre G Van Schaftingen E (2006) Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase. Glycobiology 16, 165 172.
    • (2006) Glycobiology , vol.16 , pp. 165-172
    • Maliekal, P.1    Vertommen, D.2    Delpierre, G.3    Van Schaftingen, E.4
  • 28
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya K Ui M (1966) A new micromethod for the colorimetric determination of inorganic phosphate. Clin Chim Acta 14, 361 366.
    • (1966) Clin Chim Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Ui, M.2
  • 30
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25, 4876 4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.