메뉴 건너뛰기




Volumn 14, Issue 4, 2007, Pages 280-286

GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; AUTOANTIGEN; GLUTAMATE DECARBOXYLASE; GLUTAMATE DECARBOXYLASE 65; GLUTAMATE DECARBOXYLASE 67;

EID: 34247249781     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1228     Document Type: Article
Times cited : (194)

References (41)
  • 1
    • 0041465717 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase
    • Capitani, G. et al. Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase. EMBO J. 22, 4027-4037 (2003).
    • (2003) EMBO J , vol.22 , pp. 4027-4037
    • Capitani, G.1
  • 2
    • 33745752814 scopus 로고    scopus 로고
    • Escherichia coli acid resistance: PH-sensing, activation by chloride and autoinhibition in GadB
    • Gut, H. et al. Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB. EMBO J. 25, 2643-2651 (2006).
    • (2006) EMBO J , vol.25 , pp. 2643-2651
    • Gut, H.1
  • 3
    • 0032416442 scopus 로고    scopus 로고
    • Two isoforms of glutamate decarboxylase: Why?
    • Soghomonian, J.J. & Martin, D.L. Two isoforms of glutamate decarboxylase: why? Trends Pharmacol. Sci. 19, 500-505 (1998).
    • (1998) Trends Pharmacol. Sci , vol.19 , pp. 500-505
    • Soghomonian, J.J.1    Martin, D.L.2
  • 4
    • 1542408736 scopus 로고    scopus 로고
    • Specific GABAA circuits for visual cortical plasticity
    • Fagiolini, M. et al. Specific GABAA circuits for visual cortical plasticity. Science 303, 1681-1683 (2004).
    • (2004) Science , vol.303 , pp. 1681-1683
    • Fagiolini, M.1
  • 5
    • 31844447757 scopus 로고    scopus 로고
    • GABA regulates synaptic integration of newly generated neurons in the adult brain
    • Ge, S. et al. GABA regulates synaptic integration of newly generated neurons in the adult brain. Nature 439, 589-593 (2006).
    • (2006) Nature , vol.439 , pp. 589-593
    • Ge, S.1
  • 6
    • 0027338402 scopus 로고
    • A cluster of three GABAA receptor subunit genes is deleted in a neurological mutant of the mouse p locus
    • Nakatsu, Y. et al. A cluster of three GABAA receptor subunit genes is deleted in a neurological mutant of the mouse p locus. Nature 364, 448-450 (1993).
    • (1993) Nature , vol.364 , pp. 448-450
    • Nakatsu, Y.1
  • 7
    • 12644278303 scopus 로고    scopus 로고
    • Cleft palate and decreased brain gamma-aminobutyric acid in mice lacking the 67-kDa isoform of glutamic acid decarboxylase
    • Asada, H. et al. Cleft palate and decreased brain gamma-aminobutyric acid in mice lacking the 67-kDa isoform of glutamic acid decarboxylase. Proc. Natl. Acad. Sci. USA 94, 6496-6499 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6496-6499
    • Asada, H.1
  • 8
    • 0031443439 scopus 로고    scopus 로고
    • Epilepsy in mice deficient in the 65-kDa isoform of glutamic acid decarboxylase
    • Kash, S.F. et al. Epilepsy in mice deficient in the 65-kDa isoform of glutamic acid decarboxylase. Proc. Natl. Acad. Sci. USA 94, 14060-14065 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14060-14065
    • Kash, S.F.1
  • 9
    • 0030600546 scopus 로고    scopus 로고
    • Mice lacking the 65 kDa isoform of glutamic acid decarboxylase (GAD65) maintain normal levels of GAD67 and GABA in their brains but are susceptible to seizures
    • Asada, H. et al. Mice lacking the 65 kDa isoform of glutamic acid decarboxylase (GAD65) maintain normal levels of GAD67 and GABA in their brains but are susceptible to seizures. Biochem. Biophys. Res. Commun. 229, 891-895 (1996).
    • (1996) Biochem. Biophys. Res. Commun , vol.229 , pp. 891-895
    • Asada, H.1
  • 10
    • 12944281505 scopus 로고    scopus 로고
    • Homozygosity for a missense mutation in the 67 kDa isoform of glutamate decarboxylase in a family with autosomal recessive spastic cerebral palsy: Parallels with Stiff-Person Syndrome and other movement disorders
    • Lynex, C.N. et al. Homozygosity for a missense mutation in the 67 kDa isoform of glutamate decarboxylase in a family with autosomal recessive spastic cerebral palsy: parallels with Stiff-Person Syndrome and other movement disorders. BMC Neurol. 4, 20 (2004).
    • (2004) BMC Neurol , vol.4 , pp. 20
    • Lynex, C.N.1
  • 11
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius, J.N. Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8, 759-769 (1998).
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 12
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • 850-854
    • Percudani, R. & Peracchi, A. A genomic overview of pyridoxal-phosphate-dependent enzymes. EMBO Rep. 4, 850-854 (2003).
    • (2003) EMBO Rep , vol.4
    • Percudani, R.1    Peracchi, A.2
  • 13
    • 0022382871 scopus 로고
    • Transaminations catalysed by brain glutamate decarboxylase
    • Porter, T.G., Spink, D.C., Martin, S.B. & Martin, D.L. Transaminations catalysed by brain glutamate decarboxylase. Biochem. J. 231, 705-712 (1985).
    • (1985) Biochem. J , vol.231 , pp. 705-712
    • Porter, T.G.1    Spink, D.C.2    Martin, S.B.3    Martin, D.L.4
  • 14
    • 0041730409 scopus 로고    scopus 로고
    • Kinetic differences between the isoforms of glutamate decarboxylase: Implications for the regulation of GABA synthesis
    • Battaglioli, G., Liu, H. & Martin, D.L. Kinetic differences between the isoforms of glutamate decarboxylase: implications for the regulation of GABA synthesis. J. Neurochem. 86, 879-887 (2003).
    • (2003) J. Neurochem , vol.86 , pp. 879-887
    • Battaglioli, G.1    Liu, H.2    Martin, D.L.3
  • 15
    • 0029683483 scopus 로고    scopus 로고
    • Glutamic acid decarboxylase-gene to antigen to disease
    • Lernmark, A. Glutamic acid decarboxylase-gene to antigen to disease. J. Intern. Med. 240, 259-277 (1996).
    • (1996) J. Intern. Med , vol.240 , pp. 259-277
    • Lernmark, A.1
  • 16
    • 27644588663 scopus 로고    scopus 로고
    • Glutamate decarboxylase: Loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues
    • Battaglioli, G., Liu, H., Hauer, C.R. & Martin, D.L. Glutamate decarboxylase: loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues. Neurochem. Res. 30, 989-1001 (2005).
    • (2005) Neurochem. Res , vol.30 , pp. 989-1001
    • Battaglioli, G.1    Liu, H.2    Hauer, C.R.3    Martin, D.L.4
  • 17
    • 0034256926 scopus 로고    scopus 로고
    • Structural features and regulatory properties of the brain glutamate decarboxylases
    • Martin, D.L., Liu, H., Martin, S.B. & Wu, S.J. Structural features and regulatory properties of the brain glutamate decarboxylases. Neurochem. Int. 37, 111-119 (2000).
    • (2000) Neurochem. Int , vol.37 , pp. 111-119
    • Martin, D.L.1    Liu, H.2    Martin, S.B.3    Wu, S.J.4
  • 18
    • 0032568191 scopus 로고    scopus 로고
    • Expression in Saccharomyces cerevisiae of antigenically and enzymatically active recombinant glutamic acid decarboxylase
    • Law, R.H., Rowley, M.J., Mackay, I.R. & Corner, B. Expression in Saccharomyces cerevisiae of antigenically and enzymatically active recombinant glutamic acid decarboxylase. J. Biotechnol. 61, 57-68 (1998).
    • (1998) J. Biotechnol , vol.61 , pp. 57-68
    • Law, R.H.1    Rowley, M.J.2    Mackay, I.R.3    Corner, B.4
  • 19
    • 0031863617 scopus 로고    scopus 로고
    • Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
    • Qu, K., Martin, D.L. & Lawrence, C.E. Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. Protein Sci. 7, 1092-1105 (1998).
    • (1998) Protein Sci , vol.7 , pp. 1092-1105
    • Qu, K.1    Martin, D.L.2    Lawrence, C.E.3
  • 20
    • 0033574022 scopus 로고    scopus 로고
    • Increased anxiety and altered responses to anxiolytics in mice deficient in the 65-kDa isoform of glutamic acid decarboxylase
    • Kash, S.F., Tecott, L.H., Hodge, C. & Baekkeskov, S. Increased anxiety and altered responses to anxiolytics in mice deficient in the 65-kDa isoform of glutamic acid decarboxylase. Proc. Natl. Acad. Sci. USA 96, 1698-1703 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1698-1703
    • Kash, S.F.1    Tecott, L.H.2    Hodge, C.3    Baekkeskov, S.4
  • 21
    • 0025039679 scopus 로고
    • Identification of the 64K autoantigen in insulin-dependent diabetes as the GABA-synthesizing enzyme glutamic acid decarboxylase
    • Baekkeskov, S. et al. Identification of the 64K autoantigen in insulin-dependent diabetes as the GABA-synthesizing enzyme glutamic acid decarboxylase. Nature 347, 151-156 (1990).
    • (1990) Nature , vol.347 , pp. 151-156
    • Baekkeskov, S.1
  • 22
    • 10444225954 scopus 로고    scopus 로고
    • Glutamic acid decarboxylase autoimmunity in Batten disease and other disorders
    • Pearce, D.A., Atkinson, M. & Tagle, D.A. Glutamic acid decarboxylase autoimmunity in Batten disease and other disorders. Neurology 63, 2001-2005 (2004).
    • (2004) Neurology , vol.63 , pp. 2001-2005
    • Pearce, D.A.1    Atkinson, M.2    Tagle, D.A.3
  • 23
    • 28344449503 scopus 로고    scopus 로고
    • Analysis of GAD65 autoantibodies in Stiff-Person Syndrome patients
    • Raju, R. et al. Analysis of GAD65 autoantibodies in Stiff-Person Syndrome patients. J. Immunol. 175, 7755-7762 (2005).
    • (2005) J. Immunol , vol.175 , pp. 7755-7762
    • Raju, R.1
  • 25
    • 0037184097 scopus 로고    scopus 로고
    • Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase
    • Bertoldi, M., Gonsalvi, M., Contestabile, R. & Voltattorni, C.B. Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase. J. Biol. Chem. 277, 36357-36362 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 36357-36362
    • Bertoldi, M.1    Gonsalvi, M.2    Contestabile, R.3    Voltattorni, C.B.4
  • 26
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • Eliot, A.C. & Kirsch, J.F. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu. Rev. Biochem. 73, 383-415 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 27
    • 0034212493 scopus 로고    scopus 로고
    • Comparative expression and purification of human glutamic acid decarboxylase from Saccharomyces cerevisiae and Pichia pastoris
    • Papakonstantinou, T., Law, R.H., Gardiner, P., Rowley, M.J. & Mackay, I.R. Comparative expression and purification of human glutamic acid decarboxylase from Saccharomyces cerevisiae and Pichia pastoris. Enzyme Microb. Technol. 26, 645-652 (2000).
    • (2000) Enzyme Microb. Technol , vol.26 , pp. 645-652
    • Papakonstantinou, T.1    Law, R.H.2    Gardiner, P.3    Rowley, M.J.4    Mackay, I.R.5
  • 28
  • 31
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr , vol.50 , pp. 760-763
  • 34
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu, A.A., Shelenkov, A.A. & Dunbrack, R.L., Jr. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12, 2001-2014 (2003).
    • (2003) Protein Sci , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack Jr., R.L.3
  • 36
  • 37
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R.J., Perrakis, A. & Lamzin, V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374, 229-244 (2003).
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 38
    • 0004293491 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, California, USA
    • DeLano, W.L. The PyMOL User's Manual (DeLano Scientific, San Carlos, California, USA, 2002).
    • (2002) The PyMOL User's Manual
    • DeLano, W.L.1
  • 40
    • 0018583088 scopus 로고
    • Stimulation by phosphate on the activation of glutamate apodecarboxylase by pyridoxyl-5′-phosphate and its implications for the control of GABA synthesis
    • Martin, S.B. & Martin, D.L. Stimulation by phosphate on the activation of glutamate apodecarboxylase by pyridoxyl-5′-phosphate and its implications for the control of GABA synthesis. J. Neurochem. 33, 1275-1283 (1979).
    • (1979) J. Neurochem , vol.33 , pp. 1275-1283
    • Martin, S.B.1    Martin, D.L.2
  • 41
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40 (1993).
    • (1993) Protein Eng , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.