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Volumn 281, Issue 14, 2014, Pages 3228-3242

Structural and biochemical characterization of the folyl-poly-γ- l -glutamate hydrolyzing activity of human glutamate carboxypeptidase II

Author keywords

arene binding site; crystal structure; folate hydrolase 1; H475Y(1561C T) polymorphism; zinc metalloprotease

Indexed keywords

FOLYL POLY GAMMA LEVO GLUTAMIC ACID; GLUTAMATE CARBOXYPEPTIDASE II; PTEROPTIN; UNCLASSIFIED DRUG;

EID: 84904732507     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12857     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0027500319 scopus 로고
    • Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen
    • Israeli RS, Powell CT, Fair WR, &, Heston WD, (1993) Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen. Cancer Res 53, 227-230.
    • (1993) Cancer Res , vol.53 , pp. 227-230
    • Israeli, R.S.1    Powell, C.T.2    Fair, W.R.3    Heston, W.D.4
  • 2
    • 0023232412 scopus 로고
    • Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate. Identification and characterization of a novel N-acetylated alpha-linked acidic dipeptidase activity from rat brain
    • Robinson MB, Blakely RD, Couto R, &, Coyle JT, (1987) Hydrolysis of the brain dipeptide N-acetyl-L-aspartyl-L-glutamate. Identification and characterization of a novel N-acetylated alpha-linked acidic dipeptidase activity from rat brain. J Biol Chem 262, 14498-14506.
    • (1987) J Biol Chem , vol.262 , pp. 14498-14506
    • Robinson, M.B.1    Blakely, R.D.2    Couto, R.3    Coyle, J.T.4
  • 4
    • 66049093465 scopus 로고    scopus 로고
    • Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods
    • Klusak V, Barinka C, Plechanovova A, Mlcochova P, Konvalinka J, Rulisek L, &, Lubkowski J, (2009) Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods. Biochemistry 48, 4126-4138.
    • (2009) Biochemistry , vol.48 , pp. 4126-4138
    • Klusak, V.1    Barinka, C.2    Plechanovova, A.3    Mlcochova, P.4    Konvalinka, J.5    Rulisek, L.6    Lubkowski, J.7
  • 5
    • 84857589525 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II in diagnosis and treatment of neurologic disorders and prostate cancer
    • Barinka C, Rojas C, Slusher B, &, Pomper M, (2012) Glutamate carboxypeptidase II in diagnosis and treatment of neurologic disorders and prostate cancer. Curr Med Chem 19, 856-870.
    • (2012) Curr Med Chem , vol.19 , pp. 856-870
    • Barinka, C.1    Rojas, C.2    Slusher, B.3    Pomper, M.4
  • 6
    • 84858136101 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II: An overview of structural studies and their importance for structure-based drug design and deciphering the reaction mechanism of the enzyme
    • Pavlicek J, Ptacek J, &, Barinka C, (2012) Glutamate carboxypeptidase II: an overview of structural studies and their importance for structure-based drug design and deciphering the reaction mechanism of the enzyme. Curr Med Chem 19, 1300-1309.
    • (2012) Curr Med Chem , vol.19 , pp. 1300-1309
    • Pavlicek, J.1    Ptacek, J.2    Barinka, C.3
  • 8
    • 34547869292 scopus 로고    scopus 로고
    • Relations of glutamate carboxypeptidase II (GCPII) polymorphisms to folate and homocysteine concentrations and to scores of cognition, anxiety, and depression in a homogeneous Norwegian population: The Hordaland Homocysteine Study
    • Halsted CH, Wong DH, Peerson JM, Warden CH, Refsum H, Smith AD, Nygard OK, Ueland PM, Vollset SE, &, Tell GS, (2007) Relations of glutamate carboxypeptidase II (GCPII) polymorphisms to folate and homocysteine concentrations and to scores of cognition, anxiety, and depression in a homogeneous Norwegian population: the Hordaland Homocysteine Study. Am J Clin Nutr 86, 514-521.
    • (2007) Am J Clin Nutr , vol.86 , pp. 514-521
    • Halsted, C.H.1    Wong, D.H.2    Peerson, J.M.3    Warden, C.H.4    Refsum, H.5    Smith, A.D.6    Nygard, O.K.7    Ueland, P.M.8    Vollset, S.E.9    Tell, G.S.10
  • 9
    • 0036276029 scopus 로고    scopus 로고
    • The glutamate carboxypeptidase gene II (C>T) polymorphism does not affect folate status in the Framingham Offspring cohort
    • Vargas-Martinez C, Ordovas JM, Wilson PW, &, Selhub J, (2002) The glutamate carboxypeptidase gene II (C>T) polymorphism does not affect folate status in the Framingham Offspring cohort. J Nutr 132, 1176-1179.
    • (2002) J Nutr , vol.132 , pp. 1176-1179
    • Vargas-Martinez, C.1    Ordovas, J.M.2    Wilson, P.W.3    Selhub, J.4
  • 10
    • 2442681816 scopus 로고    scopus 로고
    • Polymorphisms in the one-carbon metabolic pathway, plasma folate levels and colorectal cancer in a prospective study
    • Chen J, Kyte C, Valcin M, Chan W, Wetmur JG, Selhub J, Hunter DJ, &, Ma J, (2004) Polymorphisms in the one-carbon metabolic pathway, plasma folate levels and colorectal cancer in a prospective study. Int J Cancer 110, 617-620.
    • (2004) Int J Cancer , vol.110 , pp. 617-620
    • Chen, J.1    Kyte, C.2    Valcin, M.3    Chan, W.4    Wetmur, J.G.5    Selhub, J.6    Hunter, D.J.7    Ma, J.8
  • 11
    • 33645635701 scopus 로고    scopus 로고
    • Interactions among polymorphisms in folate-metabolizing genes and serum total homocysteine concentrations in a healthy elderly population
    • Devlin AM, Clarke R, Birks J, Evans JG, &, Halsted CH, (2006) Interactions among polymorphisms in folate-metabolizing genes and serum total homocysteine concentrations in a healthy elderly population. Am J Clin Nutr 83, 708-713.
    • (2006) Am J Clin Nutr , vol.83 , pp. 708-713
    • Devlin, A.M.1    Clarke, R.2    Birks, J.3    Evans, J.G.4    Halsted, C.H.5
  • 12
    • 84904756746 scopus 로고    scopus 로고
    • Combined impact of polymorphism of folate metabolism genes; Glutamate carboxypeptidase, methylene tetrahydrofolate reductase and methionine synthase reductase on breast cancer susceptibility in Kashmiri women
    • Mir MM, (2008) Combined impact of polymorphism of folate metabolism genes; glutamate carboxypeptidase, methylene tetrahydrofolate reductase and methionine synthase reductase on breast cancer susceptibility in Kashmiri women. Clin Chem 54, A126.
    • (2008) Clin Chem , vol.54
    • Mir, M.M.1
  • 14
  • 16
    • 0034703861 scopus 로고    scopus 로고
    • Glutamate carboxypeptidase II: A polymorphism associated with lower levels of serum folate and hyperhomocysteinemia
    • Devlin AM, Ling EH, Peerson JM, Fernando S, Clarke R, Smith AD, &, Halsted CH, (2000) Glutamate carboxypeptidase II: a polymorphism associated with lower levels of serum folate and hyperhomocysteinemia. Hum Mol Genet 9, 2837-2844.
    • (2000) Hum Mol Genet , vol.9 , pp. 2837-2844
    • Devlin, A.M.1    Ling, E.H.2    Peerson, J.M.3    Fernando, S.4    Clarke, R.5    Smith, A.D.6    Halsted, C.H.7
  • 18
    • 3042849118 scopus 로고    scopus 로고
    • Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding
    • Barinka C, Mlcochova P, Sacha P, Hilgert I, Majer P, Slusher BS, Horejsi V, &, Konvalinka J, (2004) Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding. Eur J Biochem 271, 2782-2790.
    • (2004) Eur J Biochem , vol.271 , pp. 2782-2790
    • Barinka, C.1    Mlcochova, P.2    Sacha, P.3    Hilgert, I.4    Majer, P.5    Slusher, B.S.6    Horejsi, V.7    Konvalinka, J.8
  • 19
    • 0032496731 scopus 로고    scopus 로고
    • Hydrolysis of the neuropeptide N-acetylaspartylglutamate (NAAG) by cloned human glutamate carboxypeptidase II
    • Luthi-Carter R, Barczak AK, Speno H, &, Coyle JT, (1998) Hydrolysis of the neuropeptide N-acetylaspartylglutamate (NAAG) by cloned human glutamate carboxypeptidase II. Brain Res 795, 341-348.
    • (1998) Brain Res , vol.795 , pp. 341-348
    • Luthi-Carter, R.1    Barczak, A.K.2    Speno, H.3    Coyle, J.T.4
  • 21
    • 77954516516 scopus 로고    scopus 로고
    • Folic acid and L-5-methyltetrahydrofolate comparison of clinical pharmacokinetics and pharmacodynamics
    • Pietrzik K, Bailey L, &, Shane B, (2010) Folic acid and L-5-methyltetrahydrofolate comparison of clinical pharmacokinetics and pharmacodynamics. Clin Pharmacokinet 49, 535-548.
    • (2010) Clin Pharmacokinet , vol.49 , pp. 535-548
    • Pietrzik, K.1    Bailey, L.2    Shane, B.3
  • 25
    • 68749087539 scopus 로고    scopus 로고
    • Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III
    • Hlouchova K, Barinka C, Konvalinka J, &, Lubkowski J, (2009) Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III. FEBS J 276, 4448-4462.
    • (2009) FEBS J , vol.276 , pp. 4448-4462
    • Hlouchova, K.1    Barinka, C.2    Konvalinka, J.3    Lubkowski, J.4
  • 26
    • 80055081130 scopus 로고    scopus 로고
    • Molecular identification of beta-citrylglutamate hydrolase as glutamate carboxypeptidase 3
    • Collard F, Vertommen D, Constantinescu S, Buts L, &, Van Schaftingen E, (2011) Molecular identification of beta-citrylglutamate hydrolase as glutamate carboxypeptidase 3. J Biol Chem 286, 38220-38230.
    • (2011) J Biol Chem , vol.286 , pp. 38220-38230
    • Collard, F.1    Vertommen, D.2    Constantinescu, S.3    Buts, L.4    Van Schaftingen, E.5
  • 27
    • 0036488137 scopus 로고    scopus 로고
    • Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II
    • Barinka C, Rinnova M, Sacha P, Rojas C, Majer P, Slusher BS, &, Konvalinka J, (2002) Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. J Neurochem 80, 477-487.
    • (2002) J Neurochem , vol.80 , pp. 477-487
    • Barinka, C.1    Rinnova, M.2    Sacha, P.3    Rojas, C.4    Majer, P.5    Slusher, B.S.6    Konvalinka, J.7
  • 28
    • 84855464771 scopus 로고    scopus 로고
    • Efficient and versatile one-step affinity purification of in vivo biotinylated proteins: Expression, characterization and structure analysis of recombinant human glutamate carboxypeptidase II
    • Tykvart J, Sacha P, Barinka C, Knedlik T, Starkova J, Lubkowski J, &, Konvalinka J, (2012) Efficient and versatile one-step affinity purification of in vivo biotinylated proteins: expression, characterization and structure analysis of recombinant human glutamate carboxypeptidase II. Protein Expr Purif 82, 106-115.
    • (2012) Protein Expr Purif , vol.82 , pp. 106-115
    • Tykvart, J.1    Sacha, P.2    Barinka, C.3    Knedlik, T.4    Starkova, J.5    Lubkowski, J.6    Konvalinka, J.7
  • 29
    • 34547567980 scopus 로고    scopus 로고
    • OligoCalc: An online oligonucleotide properties calculator
    • Kibbe WA, (2007) OligoCalc: an online oligonucleotide properties calculator. Nucleic Acids Res 35, W43-W46.
    • (2007) Nucleic Acids Res , vol.35
    • Kibbe, W.A.1
  • 30
    • 33947319738 scopus 로고    scopus 로고
    • A high-resolution structure of ligand-free human glutamate carboxypeptidase II
    • Barinka C, Starkova J, Konvalinka J, &, Lubkowski J, (2007) A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr F 63, 150-153.
    • (2007) Acta Crystallogr F , vol.63 , pp. 150-153
    • Barinka, C.1    Starkova, J.2    Konvalinka, J.3    Lubkowski, J.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Meth Enzymol 276, 307-326.
    • (1997) Meth Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 84861486823 scopus 로고    scopus 로고
    • XDSAPP: A graphical user interface for the convenient processing of diffraction data using XDS
    • Krug M, Weiss MS, Heinemann U, &, Mueller U, (2012) XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS. J Appl Crystallogr 45, 568-572.
    • (2012) J Appl Crystallogr , vol.45 , pp. 568-572
    • Krug, M.1    Weiss, M.S.2    Heinemann, U.3    Mueller, U.4
  • 35
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, &, van Aalten DM, (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60, 1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 38
    • 0015072056 scopus 로고
    • Fluorescence reaction for amino acids
    • Roth M, (1971) Fluorescence reaction for amino acids. Anal Chem 43, 880.
    • (1971) Anal Chem , vol.43 , pp. 880
    • Roth, M.1
  • 39
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, DeTitta GT, Dekker N, &, Nordlund P, (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357, 289-298.
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5


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