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Volumn 7, Issue 5, 1998, Pages 1092-1105

Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase

Author keywords

Bayesian statistics; Gibbs sampling; Human glutamate decarboxylase; Multiple sequence alignment; Structural prediction by homology

Indexed keywords

APOENZYME; ASPARTATE AMINOTRANSFERASE; BINDING PROTEIN; GLUTAMATE DECARBOXYLASE; ISOENZYME; ORNITHINE DECARBOXYLASE; PYRIDOXAL 5 PHOSPHATE; TYROSINE PHENOL LYASE;

EID: 0031863617     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070503     Document Type: Article
Times cited : (31)

References (42)
  • 1
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes Regio-specific α, β and γ families
    • Alexander FW, Sandmeier E, Mehta PK, Christen P. 1994. Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes Regio-specific α, β and γ families. Eur J Biochem 219:953-960.
    • (1994) Eur J Biochem , vol.219 , pp. 953-960
    • Alexander, F.W.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 3
    • 0028341371 scopus 로고
    • The Exon-Intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylase (GAD67 and GAD65) suggests that they derive from a common ancestral GAD
    • Bu DF, Tohin AJ. 1994. The Exon-Intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylase (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics 21:222-228.
    • (1994) Genomics , vol.21 , pp. 222-228
    • Bu, D.F.1    Tohin, A.J.2
  • 5
    • 0030595364 scopus 로고    scopus 로고
    • Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 Å
    • Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. 1996. Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 Å. J Mol Biol 262:202-224.
    • (1996) J Mol Biol , vol.262 , pp. 202-224
    • Clausen, T.1    Huber, R.2    Laber, B.3    Pohlenz, H.D.4    Messerschmidt, A.5
  • 9
    • 0030995422 scopus 로고    scopus 로고
    • Crystal structure of glutamate-1-semialdehyde aminomutase: An alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity
    • Hennig M, Grim B, Contestabile R, John RA, Jansonius JN. 1997. Crystal structure of glutamate-1-semialdehyde aminomutase: An alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Proc Natl Acad Sci USA 94:4866-4871.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4866-4871
    • Hennig, M.1    Grim, B.2    Contestabile, R.3    John, R.A.4    Jansonius, J.N.5
  • 10
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol WGJ, van Duijnen PT, Berendsen HJC. 1978. The α-helix dipole and the properties of proteins. Nature 273:443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 11
    • 0028914569 scopus 로고
    • Pyridoxal phosphate-dependent enzymes
    • John RA. 1995. Pyridoxal phosphate-dependent enzymes. Biochim Biophys Acta 1248:81-96.
    • (1995) Biochim Biophys Acta , vol.1248 , pp. 81-96
    • John, R.A.1
  • 14
    • 0026754015 scopus 로고
    • Accurate modeling of protein conformation by automatic segment matching
    • Levitt M. 1992. Accurate modeling of protein conformation by automatic segment matching. J Mol Biol 226:507-533.
    • (1992) J Mol Biol , vol.226 , pp. 507-533
    • Levitt, M.1
  • 15
    • 0021095856 scopus 로고
    • Protein folding by constrained energy minimization and molecular dynamics
    • Levitt M. 1983. Protein folding by constrained energy minimization and molecular dynamics. J Mol Biol 170:723-764.
    • (1983) J Mol Biol , vol.170 , pp. 723-764
    • Levitt, M.1
  • 16
    • 0345234230 scopus 로고    scopus 로고
    • Statistical models for multiple sequence alignment: Unifications and generalizations
    • Liu JS, Lawrence CE. 1996. Statistical models for multiple sequence alignment: Unifications and generalizations. Proc Am Stat Assoc Stat Comput Sect:1-8.
    • (1996) Proc Am Stat Assoc Stat Comput Sect , pp. 1-8
    • Liu, J.S.1    Lawrence, C.E.2
  • 17
    • 84950424966 scopus 로고
    • Bayesian models for multiple local sequence alignment and Gibbs sampling strategies
    • Liu JS, Neuwald A, Lawrence CE. 1995. Bayesian models for multiple local sequence alignment and Gibbs sampling strategies. JASA 90:1156-1170.
    • (1995) JASA , vol.90 , pp. 1156-1170
    • Liu, J.S.1    Neuwald, A.2    Lawrence, C.E.3
  • 18
    • 2642685838 scopus 로고    scopus 로고
    • Markovian structures in biological sequence alignments
    • Forthcoming
    • Liu JS, Neuwald A, Lawrence CE. 1998. Markovian structures in biological sequence alignments. JASA Forthcoming.
    • (1998) JASA
    • Liu, J.S.1    Neuwald, A.2    Lawrence, C.E.3
  • 19
    • 8044253810 scopus 로고    scopus 로고
    • 67 associated with specific pools of GABA in brain?
    • Forthcoming
    • 67 associated with specific pools of GABA in brain? Perspect Dev Biol. Forthcoming.
    • (1997) Perspect Dev Biol.
    • Martin, D.L.1    Barke, K.2
  • 20
    • 0025838324 scopus 로고
    • Regulatory properties of brain glutamate decarboxylase (GAD): The apoenzyme of GAD is present principally as the smaller of two molecular forms of GAD in brain
    • Martin DL, Martin SB, Wu SJ, Espina N. 1991. Regulatory properties of brain glutamate decarboxylase (GAD): The apoenzyme of GAD is present principally as the smaller of two molecular forms of GAD in brain. J Neurosci 11:2725-2731.
    • (1991) J Neurosci , vol.11 , pp. 2725-2731
    • Martin, D.L.1    Martin, S.B.2    Wu, S.J.3    Espina, N.4
  • 21
    • 0027395911 scopus 로고
    • Regulation of γ-aminobutyric acid synthesis in the brain
    • Martin DL, Rimvall K. 1993. Regulation of γ-aminobutyric acid synthesis in the brain. J Neurochem 60:395-407.
    • (1993) J Neurochem , vol.60 , pp. 395-407
    • Martin, D.L.1    Rimvall, K.2
  • 22
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen C, Vincent MG, Jansonius JN. 1992a. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J Mol Biol 225:495-517.
    • (1992) J Mol Biol , vol.225 , pp. 495-517
    • McPhalen, C.1    Vincent, M.G.2    Jansonius, J.N.3
  • 24
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta PK, Hale TI, Christen P. 1993. Aminotransferases: Demonstration of homology and division into evolutionary subgroups. Eur J Biochem 214:549-561.
    • (1993) Eur J Biochem , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 25
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine dearboxylase from Lactobacillus 30a to 3.0 Å resolution
    • Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML. 1995b. Crystallographic structure of a PLP-dependent ornithine dearboxylase from Lactobacillus 30a to 3.0 Å resolution. J Mol Biol 252:643-655.
    • (1995) J Mol Biol , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.L.4    Hackert, M.L.5
  • 26
    • 0028921425 scopus 로고
    • Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase
    • Momany C, Ghosh R, Hackert ML. 1995a. Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Protein Sci 4:849-854.
    • (1995) Protein Sci , vol.4 , pp. 849-854
    • Momany, C.1    Ghosh, R.2    Hackert, M.L.3
  • 27
    • 0031038166 scopus 로고    scopus 로고
    • Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha
    • Namchuk M, Lindsay L, Turek CW, Kanaani J, Baekkeskov S. 1997. Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem 272:1548-1557.
    • (1997) J Biol Chem , vol.272 , pp. 1548-1557
    • Namchuk, M.1    Lindsay, L.2    Turek, C.W.3    Kanaani, J.4    Baekkeskov, S.5
  • 28
    • 0029144601 scopus 로고
    • Gibbs motif sampling: Detection of bacterial outer membrane protein repeats
    • Neuwald A, Liu JS, Lawrence CE. 1995. Gibbs motif sampling: Detection of bacterial outer membrane protein repeats. Protein Sci 4:1618-1632.
    • (1995) Protein Sci , vol.4 , pp. 1618-1632
    • Neuwald, A.1    Liu, J.S.2    Lawrence, C.E.3
  • 29
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • Neuwald A, Liu JS, Lipman DJ, Lawrence CE. 1997. Extracting protein alignment models from the sequence database. Nucleic Acids Res 25:1665-1677.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1665-1677
    • Neuwald, A.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 30
    • 0027366667 scopus 로고
    • Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzyme
    • Pascarella S, Schirch V, Bossa F. 1993. Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzyme. FEBS 331:145-149.
    • (1993) FEBS , vol.331 , pp. 145-149
    • Pascarella, S.1    Schirch, V.2    Bossa, F.3
  • 31
    • 0026029016 scopus 로고
    • The open/closed conformational equilibrium of aspartate aminotransferase studies in the crystalline state and with a fluorescent probe in solution
    • Picot D, Sandmeier E, Thaller C, Vincent MG, Christen P, Jansonius JN. 1991. The open/closed conformational equilibrium of aspartate aminotransferase studies in the crystalline state and with a fluorescent probe in solution. Eur J Biochem 196:329-341.
    • (1991) Eur J Biochem , vol.196 , pp. 329-341
    • Picot, D.1    Sandmeier, E.2    Thaller, C.3    Vincent, M.G.4    Christen, P.5    Jansonius, J.N.6
  • 32
    • 0024255896 scopus 로고
    • Stability and activation of glutamate apodecarboxylase from pig brain
    • Porter TG, Martin DL. 1988. Stability and activation of glutamate apodecarboxylase from pig brain. J Neurochem 51:1886-1891.
    • (1988) J Neurochem , vol.51 , pp. 1886-1891
    • Porter, T.G.1    Martin, D.L.2
  • 33
    • 0022382871 scopus 로고
    • Transaminations catalysed by brain glutamate decarboxylase
    • Porter TG, Spink DC, Martin SB, Martin DL. 1985. Transaminations catalysed by brain glutamate decarboxylase. Biochem J 231:705-712.
    • (1985) Biochem J , vol.231 , pp. 705-712
    • Porter, T.G.1    Spink, D.C.2    Martin, S.B.3    Martin, D.L.4
  • 34
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider TD, Stephens RM. 1990. Sequence logos: A new way to display consensus sequences. Nucleic Acids Res 18:6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 35
    • 0029920293 scopus 로고    scopus 로고
    • Heteromers of glutamate decarboxylase isoforms occur in rat cerebellum
    • Sheikh SN, Martin DL. 1996. Heteromers of glutamate decarboxylase isoforms occur in rat cerebellum. J Neurochem 66:2082-2090.
    • (1996) J Neurochem , vol.66 , pp. 2082-2090
    • Sheikh, S.N.1    Martin, D.L.2
  • 36
    • 0027409043 scopus 로고
    • Association of GAD-65, but not of GAD-67, with the Golgi complex of transfected Chinese hamster ovary cells mediated by the N-terminal region
    • Solimena M, Aggujaro D, Muntzel C, Dirkx R, Butler M, DeCamilli P, Mayday A. 1993. Association of GAD-65, but not of GAD-67, with the Golgi complex of transfected Chinese hamster ovary cells mediated by the N-terminal region. Proc Natl Acad Sci USA 90:3073-3077.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3073-3077
    • Solimena, M.1    Aggujaro, D.2    Muntzel, C.3    Dirkx, R.4    Butler, M.5    DeCamilli, P.6    Mayday, A.7
  • 37
    • 0028200659 scopus 로고
    • A signal located within amino acids 1-27 of GAD65 is required for its targeting to the Golgi complex region
    • Solimena M, Dirkx R Jr, Radzynski M, Mundigl O, De Camilli P. 1994. A signal located within amino acids 1-27 of GAD65 is required for its targeting to the Golgi complex region. J Cell Biol 126:331-341.
    • (1994) J Cell Biol , vol.126 , pp. 331-341
    • Solimena, M.1    Dirkx Jr., R.2    Radzynski, M.3    Mundigl, O.4    De Camilli, P.5
  • 39
    • 0028885266 scopus 로고
    • Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase
    • Toney MD, Hohenester E, Keller JW, Jansonius JN. 1995. Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase. J Mol Biol 245:151-179.
    • (1995) J Mol Biol , vol.245 , pp. 151-179
    • Toney, M.D.1    Hohenester, E.2    Keller, J.W.3    Jansonius, J.N.4
  • 42
    • 0030629565 scopus 로고    scopus 로고
    • Bayesian alignment and inference
    • Zhu J, Liu JS, Lawrence CE. 1997. Bayesian alignment and inference. ISMB-97 5:358-368.
    • (1997) ISMB-97 , vol.5 , pp. 358-368
    • Zhu, J.1    Liu, J.S.2    Lawrence, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.