메뉴 건너뛰기




Volumn 22, Issue 10, 2013, Pages 1417-1424

Crystal structure of Saccharomyces cerevisiae Aro8, a putative α-aminoadipate aminotransferase

Author keywords

Aminotransferase; Aromatic aminotransferase I; Lysine biosynthesis; Multi substrate enzyme; Pyridoxal 50 phosphate; X ray crystallography

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; ARO8 PROTEIN; KYNURENINE AMINOTRANSFERASE; KYNURENINE AMINOTRANSFERASE II; LYSINE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAMINE PHOSPHATE; SACCHAROMYCES CEREVISIAE PROTEIN; UNCLASSIFIED DRUG;

EID: 84892920495     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2315     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 33748290014 scopus 로고    scopus 로고
    • The alpha-Aminoadipate pathway for lysine biosynthesis in fungi
    • Xu H, Andi B, Qian J, West AH, Cook PF (2006) The alpha-Aminoadipate pathway for lysine biosynthesis in fungi. Cell Biochem Biophys 46:43-64.
    • (2006) Cell Biochem Biophys , vol.46 , pp. 43-64
    • Xu, H.1    Andi, B.2    Qian, J.3    West, A.H.4    Cook, P.F.5
  • 2
    • 0014670717 scopus 로고
    • Enzymatic and physiological properties of the yeast glutamate-Alpha- Ketoadipate transaminase
    • Matsuda M, Ogur M (1969) Enzymatic and physiological properties of the yeast glutamate-Alpha-Ketoadipate transaminase. J Biol Chem 244:5153-5158.
    • (1969) J Biol Chem , vol.244 , pp. 5153-5158
    • Matsuda, M.1    Ogur, M.2
  • 3
    • 0014690579 scopus 로고
    • Separation and specificity of the yeast glutamate-Alpha-Ketoadipate transaminase
    • Matsuda M, Ogur M (1969) Separation and specificity of the yeast glutamate-Alpha-Ketoadipate transaminase. J Biol Chem 244:3352-3358.
    • (1969) J Biol Chem , vol.244 , pp. 3352-3358
    • Matsuda, M.1    Ogur, M.2
  • 5
    • 0031884617 scopus 로고    scopus 로고
    • Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases i and II reveals a new aminotransferase subfamily
    • Iraqui I, Vissers S, Cartiaux M, Urrestarazu A (1998) Characterisation of Saccharomyces cerevisiae ARO8 and ARO9 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily. Mol Gen Genet 257:238-248.
    • (1998) Mol Gen Genet , vol.257 , pp. 238-248
    • Iraqui, I.1    Vissers, S.2    Cartiaux, M.3    Urrestarazu, A.4
  • 6
    • 0031908994 scopus 로고    scopus 로고
    • Phenylalanine- and tyrosine-Auxotrophic mutants of Saccharomyces cerevisiae impaired in transamination
    • Urrestarazu A, Vissers S, Iraqui I, Grenson M (1998) Phenylalanine- and tyrosine-Auxotrophic mutants of Saccharomyces cerevisiae impaired in transamination. Mol Gen Genet 257:230-237.
    • (1998) Mol Gen Genet , vol.257 , pp. 230-237
    • Urrestarazu, A.1    Vissers, S.2    Iraqui, I.3    Grenson, M.4
  • 7
    • 41249085863 scopus 로고    scopus 로고
    • Crystal structure of human kynurenine aminotransferase II
    • Han Q, Robinson H, Li J (2008) Crystal structure of human kynurenine aminotransferase II. J Biol Chem 283:3567-3573.
    • (2008) J Biol Chem , vol.283 , pp. 3567-3573
    • Han, Q.1    Robinson, H.2    Li, J.3
  • 8
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of Family i within the protein superfamily of aminotransferases
    • Jensen RA, Gu W (1996) Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases. J Bacteriol 178:2161-2171.
    • (1996) J Bacteriol , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 9
    • 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
  • 10
    • 41249087474 scopus 로고    scopus 로고
    • Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia
    • Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M (2008) Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia. J Biol Chem 283:3559-3566.
    • (2008) J Biol Chem , vol.283 , pp. 3559-3566
    • Rossi, F.1    Garavaglia, S.2    Montalbano, V.3    Walsh, M.A.4    Rizzi, M.5
  • 11
    • 66149104738 scopus 로고    scopus 로고
    • Mechanism for multiple-Substrates recognition of alpha-Aminoadipate aminotransferase from Thermus thermophilus
    • Tomita T, Miyagawa T, Miyazaki T, Fushinobu S, Kuzuyama T, Nishiyama M (2009) Mechanism for multiple-Substrates recognition of alpha-Aminoadipate aminotransferase from Thermus thermophilus. Proteins 75:348-359.
    • (2009) Proteins , vol.75 , pp. 348-359
    • Tomita, T.1    Miyagawa, T.2    Miyazaki, T.3    Fushinobu, S.4    Kuzuyama, T.5    Nishiyama, M.6
  • 12
    • 81355127345 scopus 로고    scopus 로고
    • Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae
    • Karsten WE, Reyes ZL, Bobyk KD, Cook PF, Chooback L (2011) Mechanism of the aromatic aminotransferase encoded by the Aro8 gene from Saccharomyces cerevisiae. Arch Biochem Biophys 516:67-74.
    • (2011) Arch Biochem Biophys , vol.516 , pp. 67-74
    • Karsten, W.E.1    Reyes, Z.L.2    Bobyk, K.D.3    Cook, P.F.4    Chooback, L.5
  • 13
    • 0020355644 scopus 로고
    • Tryptophan degradation in Saccharomyces cerevisiae: Characterization of two aromatic aminotransferases
    • Kradolfer P, Niederberger P, Hutter R (1982) Tryptophan degradation in Saccharomyces cerevisiae: Characterization of two aromatic aminotransferases. Arch Microbiol 133:242-248.
    • (1982) Arch Microbiol , vol.133 , pp. 242-248
    • Kradolfer, P.1    Niederberger, P.2    Hutter, R.3
  • 14
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin NV, Phillips MA, Goldsmith EJ (1995) Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci 4:1291-1304.
    • (1995) Protein Sci , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 15
    • 0036303304 scopus 로고    scopus 로고
    • Functional attributes of the phosphate group binding cup of pyridoxal phosphate-Dependent enzymes
    • Denesyuk AI, Denessiouk KA, Korpela T, Johnson MS (2002) Functional attributes of the phosphate group binding cup of pyridoxal phosphate-Dependent enzymes. J Mol Biol 316:155-172.
    • (2002) J Mol Biol , vol.316 , pp. 155-172
    • Denesyuk, A.I.1    Denessiouk, K.A.2    Korpela, T.3    Johnson, M.S.4
  • 16
    • 68949162019 scopus 로고    scopus 로고
    • Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-Aminoadipate aminotransferase from Thermus thermophilus
    • Ouchi T, Tomita T, Miyagawa T, Kuzuyama T, Nishiyama M (2009) Dual roles of a conserved pair, Arg23 and Ser20, in recognition of multiple substrates in alpha-Aminoadipate aminotransferase from Thermus thermophilus. Biochem Biophys Res Commun 388:21-27.
    • (2009) Biochem Biophys Res Commun , vol.388 , pp. 21-27
    • Ouchi, T.1    Tomita, T.2    Miyagawa, T.3    Kuzuyama, T.4    Nishiyama, M.5
  • 17
    • 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, Grimm 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 U.S.A. , vol.94 , pp. 4866-4871
    • Hennig, M.1    Grimm, B.2    Contestabile, R.3    John, R.A.4    Jansonius, J.N.5
  • 18
    • 78149468408 scopus 로고    scopus 로고
    • Crystal structure of glutamate-1-Semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine- 50-Phosphate
    • Ge H, Lv X, Fan J, Gao Y, Teng M, Niu L (2010) Crystal structure of glutamate-1-Semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine- 50-Phosphate. Biochem Biophys Res Commun 402:356-360.
    • (2010) Biochem Biophys Res Commun , vol.402 , pp. 356-360
    • Ge, H.1    Lv, X.2    Fan, J.3    Gao, Y.4    Teng, M.5    Niu, L.6
  • 19
    • 0016427366 scopus 로고
    • The binding of 8- anilinonaphthalene-1-Sulphonate to cytoplasmic aspartate aminotransferase from pig heart
    • Harris HE, Bayley PM (1975) The binding of 8- anilinonaphthalene-1- Sulphonate to cytoplasmic aspartate aminotransferase from pig heart. Biochem J 145: 125-128.
    • (1975) Biochem J , vol.145 , pp. 125-128
    • Harris, H.E.1    Bayley, P.M.2
  • 20
    • 0019332441 scopus 로고
    • Mechanismbased inactivation of pig heart L-Alanine transaminase by L-Propargylglycine. Half-Site reactivity
    • Burnett G, Marcotte P, Walsh C (1980) Mechanismbased inactivation of pig heart L-Alanine transaminase by L-Propargylglycine. Half-Site reactivity. J Biol Chem 255:3487-3491.
    • (1980) J Biol Chem , vol.255 , pp. 3487-3491
    • Burnett, G.1    Marcotte, P.2    Walsh, C.3
  • 21
    • 57049172633 scopus 로고    scopus 로고
    • Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
    • Han Q, Cai T, Tagle DA, Robinson H, Li J (2008) Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep 28:205-215.
    • (2008) Biosci Rep , vol.28 , pp. 205-215
    • Han, Q.1    Cai, T.2    Tagle, D.A.3    Robinson, H.4    Li, J.5
  • 22
    • 57049176460 scopus 로고    scopus 로고
    • Curiosity to kill the KAT (kynurenine aminotransferase): Structural insights into brain kynurenic acid synthesis
    • Rossi F, Schwarcz R, Rizzi M (2008) Curiosity to kill the KAT (kynurenine aminotransferase): Structural insights into brain kynurenic acid synthesis. Curr Opin Struct Biol 18:748-755.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 748-755
    • Rossi, F.1    Schwarcz, R.2    Rizzi, M.3
  • 23
    • 72149126110 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis
    • Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC (2009) Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. J Biol Chem 284:35769-35780.
    • (2009) J Biol Chem , vol.284 , pp. 35769-35780
    • Bulfer, S.L.1    Scott, E.M.2    Couture, J.F.3    Pillus, L.4    Trievel, R.C.5
  • 25
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doubli-E S (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276: 523-530.
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doubli-E, S.1
  • 26
    • 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. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
  • 32
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin AA, Teplyakov, A. (1997) MOLREP: An automated program for molecular replacement. J Appl Crystallogr 30:1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 34
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol 374:300-321.
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.