메뉴 건너뛰기




Volumn 81, Issue 8, 2013, Pages 1457-1465

Crystal structure of the S187F variant of human liver alanine: Aminotransferase associated with primary hyperoxaluria type I and its functional implications

Author keywords

Alanine:glyoxylate aminotransferase; Crystal structure; Molecular modeling; Pathogenic variant; Primary Hyperoxaluria Type I; Pyridoxal 5 phosphate

Indexed keywords

ALANINE; ALANINE GLYOXYLATE AMINOTRANSFERASE;

EID: 84880700894     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24300     Document Type: Article
Times cited : (21)

References (41)
  • 1
    • 7544241975 scopus 로고    scopus 로고
    • Molecular aetiology of primary hyperoxaluria type 1
    • Danpure CJ. Molecular aetiology of primary hyperoxaluria type 1. Nephron Exp Nephrol 2004;98:e39-44.
    • (2004) Nephron Exp Nephrol , vol.98
    • Danpure, C.J.1
  • 2
    • 84857236273 scopus 로고    scopus 로고
    • The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase
    • Montioli R, Fargue S, Lewin J, Zamparelli C, Danpure CJ, Borri Voltattorni C, Cellini B. The N-terminal extension is essential for the formation of the active dimeric structure of liver peroxisomal alanine:glyoxylate aminotransferase. Int J Biochem Cell Biol 2012;44:536-546.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 536-546
    • Montioli, R.1    Fargue, S.2    Lewin, J.3    Zamparelli, C.4    Danpure, C.J.5    Borri Voltattorni, C.6    Cellini, B.7
  • 3
    • 84860004858 scopus 로고    scopus 로고
    • Molecular requirements for peroxisomal targeting of alanine-glyoxylate aminotransferase as an essential determinant in primary hyperoxaluria type 1
    • Fodor K, Wolf J, Erdmann R, Schliebs W, Wilmanns M. Molecular requirements for peroxisomal targeting of alanine-glyoxylate aminotransferase as an essential determinant in primary hyperoxaluria type 1. PLoS Biol 2012;10:e1001309.
    • (2012) PLoS Biol , vol.10
    • Fodor, K.1    Wolf, J.2    Erdmann, R.3    Schliebs, W.4    Wilmanns, M.5
  • 4
    • 0042242590 scopus 로고    scopus 로고
    • Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1
    • Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ. Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1. J Mol Biol 2003;331:643-652.
    • (2003) J Mol Biol , vol.331 , pp. 643-652
    • Zhang, X.1    Roe, S.M.2    Hou, Y.3    Bartlam, M.4    Rao, Z.5    Pearl, L.H.6    Danpure, C.J.7
  • 5
    • 0022516472 scopus 로고
    • Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I
    • Danpure CJ, Jennings PR. Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. FEBS Lett 1986;201:20-24.
    • (1986) FEBS Lett , vol.201 , pp. 20-24
    • Danpure, C.J.1    Jennings, P.R.2
  • 7
    • 84864038743 scopus 로고    scopus 로고
    • Primary hyperoxalurias: Disorders of glyoxylate detoxification
    • Salido E, Pey AL, Rodriguez R, Lorenzo V. Primary hyperoxalurias: Disorders of glyoxylate detoxification. Biochim Biophys Acta 2012;1822:1453-1464.
    • (2012) Biochim Biophys Acta , vol.1822 , pp. 1453-1464
    • Salido, E.1    Pey, A.L.2    Rodriguez, R.3    Lorenzo, V.4
  • 9
    • 36349021899 scopus 로고    scopus 로고
    • Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications
    • Cellini B, Bertoldi M, Montioli R, Paiardini A, Borri Voltattorni C. Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications. Biochem J 2007;408:39-50.
    • (2007) Biochem J , vol.408 , pp. 39-50
    • Cellini, B.1    Bertoldi, M.2    Montioli, R.3    Paiardini, A.4    Borri Voltattorni, C.5
  • 10
    • 78649899924 scopus 로고    scopus 로고
    • Human liver peroxisomal alanine:glyoxylate aminotransferase: Different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant
    • Cellini B, Lorenzetto A, Montioli R, Oppici E, Voltattorni CB. Human liver peroxisomal alanine:glyoxylate aminotransferase: Different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant. Biochimie 2010;92:1801-1811.
    • (2010) Biochimie , vol.92 , pp. 1801-1811
    • Cellini, B.1    Lorenzetto, A.2    Montioli, R.3    Oppici, E.4    Voltattorni, C.B.5
  • 12
    • 67649732393 scopus 로고    scopus 로고
    • Molecular insight into the synergism between the minor allele of human liver peroxisomal alanine:glyoxylate aminotransferase and the F152I mutation
    • Cellini B, Montioli R, Paiardini A, Lorenzetto A, Voltattorni CB. Molecular insight into the synergism between the minor allele of human liver peroxisomal alanine:glyoxylate aminotransferase and the F152I mutation. J Biol Chem 2009;284:8349-8358.
    • (2009) J Biol Chem , vol.284 , pp. 8349-8358
    • Cellini, B.1    Montioli, R.2    Paiardini, A.3    Lorenzetto, A.4    Voltattorni, C.B.5
  • 13
    • 84860351331 scopus 로고    scopus 로고
    • Molecular insights into primary hyperoxaluria type 1 pathogenesis
    • Cellini B, Oppici E, Paiardini A, Montioli R. Molecular insights into primary hyperoxaluria type 1 pathogenesis. Front Biosci 2012;17:621-634.
    • (2012) Front Biosci , vol.17 , pp. 621-634
    • Cellini, B.1    Oppici, E.2    Paiardini, A.3    Montioli, R.4
  • 14
    • 33750628757 scopus 로고    scopus 로고
    • Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations
    • Coulter-Mackie MB, Lian Q. Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations. Mol Genet Metab 2006;89:349-359.
    • (2006) Mol Genet Metab , vol.89 , pp. 349-359
    • Coulter-Mackie, M.B.1    Lian, Q.2
  • 15
    • 44649134535 scopus 로고    scopus 로고
    • Partial trypsin digestion as an indicator of mis-folding of mutant alanine:glyoxylate aminotransferase and chaperone effects of specific ligands. Study of a spectrum of missense mutants
    • Coulter-Mackie MB, Lian Q. Partial trypsin digestion as an indicator of mis-folding of mutant alanine:glyoxylate aminotransferase and chaperone effects of specific ligands. Study of a spectrum of missense mutants. Mol Genet Metab 2008;94:368-374.
    • (2008) Mol Genet Metab , vol.94 , pp. 368-374
    • Coulter-Mackie, M.B.1    Lian, Q.2
  • 16
    • 33845288635 scopus 로고    scopus 로고
    • Primary hyperoxaluria type 1: AGT mistargeting highlights the fundamental differences between the peroxisomal and mitochondrial protein import pathways
    • Danpure CJ. Primary hyperoxaluria type 1: AGT mistargeting highlights the fundamental differences between the peroxisomal and mitochondrial protein import pathways. Biochim Biophys Acta 2006;1763:1776-1784.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1776-1784
    • Danpure, C.J.1
  • 17
    • 57649183376 scopus 로고    scopus 로고
    • In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase
    • Hopper ED, Pittman AM, Fitzgerald MC, Tucker CL. In vivo and in vitro examination of stability of primary hyperoxaluria-associated human alanine:glyoxylate aminotransferase. J Biol Chem 2008;283:30493-30502.
    • (2008) J Biol Chem , vol.283 , pp. 30493-30502
    • Hopper, E.D.1    Pittman, A.M.2    Fitzgerald, M.C.3    Tucker, C.L.4
  • 18
    • 84855340861 scopus 로고    scopus 로고
    • Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with primary hyperoxaluria type I
    • Oppici E, Montioli R, Lorenzetto A, Bianconi S, Borri Voltattorni C, Cellini B. Biochemical analyses are instrumental in identifying the impact of mutations on holo and/or apo-forms and on the region(s) of alanine:glyoxylate aminotransferase variants associated with primary hyperoxaluria type I. Mol Genet Metab 2012;105:132-140.
    • (2012) Mol Genet Metab , vol.105 , pp. 132-140
    • Oppici, E.1    Montioli, R.2    Lorenzetto, A.3    Bianconi, S.4    Borri Voltattorni, C.5    Cellini, B.6
  • 19
    • 84855247358 scopus 로고    scopus 로고
    • Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria
    • Pey AL, Salido E, Sanchez-Ruiz JM. Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria. Amino Acids 2011;41:1233-1245.
    • (2011) Amino Acids , vol.41 , pp. 1233-1245
    • Pey, A.L.1    Salido, E.2    Sanchez-Ruiz, J.M.3
  • 21
    • 0038132253 scopus 로고    scopus 로고
    • Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase
    • Santana A, Salido E, Torres A, Shapiro LJ. Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase. Proc Natl Acad Sci U S A 2003;100:7277-7282.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7277-7282
    • Santana, A.1    Salido, E.2    Torres, A.3    Shapiro, L.J.4
  • 22
    • 80054681529 scopus 로고    scopus 로고
    • Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants
    • Cellini B, Montioli R, Voltattorni CB. Human liver peroxisomal alanine:glyoxylate aminotransferase: characterization of the two allelic forms and their pathogenic variants. Biochim Biophys Acta 2011;1814:1577-1584.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1577-1584
    • Cellini, B.1    Montioli, R.2    Voltattorni, C.B.3
  • 23
    • 0026953008 scopus 로고
    • A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1
    • Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R. A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet 1992;1:643-644.
    • (1992) Hum Mol Genet , vol.1 , pp. 643-644
    • Minatogawa, Y.1    Tone, S.2    Allsop, J.3    Purdue, P.E.4    Takada, Y.5    Danpur, C.J.6    Kido, R.7
  • 24
    • 40449128475 scopus 로고    scopus 로고
    • Construction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli
    • Cellini B, Montioli R, Bianconi S, Lopez-Alonso JP, Voltattorni CB. Construction, purification and characterization of untagged human liver alanine-glyoxylate aminotransferase expressed in Escherichia coli. Protein Pept Lett 2008;15:153-159.
    • (2008) Protein Pept Lett , vol.15 , pp. 153-159
    • Cellini, B.1    Montioli, R.2    Bianconi, S.3    Lopez-Alonso, J.P.4    Voltattorni, C.B.5
  • 27
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: space-group determination, scaling and intensity statistics
    • Evans PR. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr D Biol Crystallogr 2011;67(Pt 4):282-292.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.PART 4 , pp. 282-292
    • Evans, P.R.1
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53(Pt 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • COOT: model-building tools for molecular graphics
    • Pt 12 Pt 1
    • Emsley P, Cowtan K. COOT: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N.
    • Collaborative Computational Project N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 33
    • 0242626649 scopus 로고    scopus 로고
    • Treponema denticola cystalysin catalyzes beta-desulfination of L-cysteine sulfinic acid and beta-decarboxylation of L-aspartate and oxalacetate
    • Cellini B, Bertoldi M, Borri Voltattorni C. Treponema denticola cystalysin catalyzes beta-desulfination of L-cysteine sulfinic acid and beta-decarboxylation of L-aspartate and oxalacetate. FEBS Lett 2003;554:306-310.
    • (2003) FEBS Lett , vol.554 , pp. 306-310
    • Cellini, B.1    Bertoldi, M.2    Borri Voltattorni, C.3
  • 35
    • 84875801452 scopus 로고    scopus 로고
    • S250F variant associated with aromatic amino acid decarboxylase deficiency: molecular defects and intracellular rescue by pyridoxine
    • Montioli R, Oppici E, Cellini B, Roncador A, Dindo M, Voltattorni CB. S250F variant associated with aromatic amino acid decarboxylase deficiency: molecular defects and intracellular rescue by pyridoxine. Hum Mol Genet 2013.
    • (2013) Hum Mol Genet
    • Montioli, R.1    Oppici, E.2    Cellini, B.3    Roncador, A.4    Dindo, M.5    Voltattorni, C.B.6
  • 36
    • 0000051486 scopus 로고
    • Derivation of force fields for molecular mechanics and dynamics from ab initio energy surfaces
    • Maple JR, Dinur U, Hagler AT. Derivation of force fields for molecular mechanics and dynamics from ab initio energy surfaces. Proc Natl Acad Sci U S A 1988;85:5350-5354.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 5350-5354
    • Maple, J.R.1    Dinur, U.2    Hagler, A.T.3
  • 37
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins
    • 389.
    • Hendlich M, Rippmann F, Barnickel G. LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J Mol Graph Model 1997;15:359-363, 389.
    • (1997) J Mol Graph Model , vol.15 , pp. 359-363
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3
  • 38
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations
    • Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu Rev Biochem 2004;73:383-415.
    • (2004) Annu Rev Biochem , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 39
    • 0034680869 scopus 로고    scopus 로고
    • Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations
    • Lumb MJ, Danpure CJ. Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. J Biol Chem 2000;275:36415-36422.
    • (2000) J Biol Chem , vol.275 , pp. 36415-36422
    • Lumb, M.J.1    Danpure, C.J.2
  • 40
    • 44949211493 scopus 로고    scopus 로고
    • Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase
    • Zhu W, Lin A, Banerjee R. Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase. Biochemistry 2008;47:6226-6232.
    • (2008) Biochemistry , vol.47 , pp. 6226-6232
    • Zhu, W.1    Lin, A.2    Banerjee, R.3
  • 41
    • 84873872722 scopus 로고    scopus 로고
    • Biochemical and computational approaches to improve the clinical treatment of dopa decarboxylase-related diseases: an overview
    • Cellini B, Montioli R, Oppici E, Voltattorni CB. Biochemical and computational approaches to improve the clinical treatment of dopa decarboxylase-related diseases: an overview. Open Biochem J 2012;6:131-138.
    • (2012) Open Biochem J , vol.6 , pp. 131-138
    • Cellini, B.1    Montioli, R.2    Oppici, E.3    Voltattorni, C.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.