메뉴 건너뛰기




Volumn 50, Issue 26, 2011, Pages 5918-5924

Crystal structures of aspartate aminotransferase reconstituted with 1-deazapyridoxal 5′-phosphate: Internal aldimine and stable l -aspartate external aldimine

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALDIMINES; AMINO GROUP; ASPARTATE AMINOTRANSFERASE; ASPARTATES; CATALYTIC BASE; COCRYSTALLIZATION; MECHANISTIC DIFFERENCES; METHYL GROUP; PLANARITY; PYRIDINE RINGS; SCHIFF-BASE; STERIC BULK;

EID: 79959778389     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200436y     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 9744235147 scopus 로고    scopus 로고
    • Reaction specificity in pyridoxal phosphate enzymes
    • DOI 10.1016/j.abb.2004.09.037, PII S0003986104005338
    • Toney, M. D. (2005) Reaction specificity in pyridoxal phosphate enzymes Arch. Biochem. Biophys. 433, 279-287 (Pubitemid 39586598)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 279-287
    • Toney, M.D.1
  • 2
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • DOI 10.1146/annurev.biochem.73.011303.074021
    • Eliot, A. C. and Kirsch, J. F. (2004) Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations Annu. Rev. Biochem. 73, 383-415 (Pubitemid 39050374)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 3
    • 0029090374 scopus 로고
    • Pyridoxal enzymes: Mechanistic diversity and uniformity
    • Hayashi, H. (1995) Pyridoxal enzymes: Mechanistic diversity and uniformity J. Biochem. 118, 463-473
    • (1995) J. Biochem. , vol.118 , pp. 463-473
    • Hayashi, H.1
  • 4
    • 0024297340 scopus 로고
    • Three-dimensional structure of the trptophan synthase α2β2 multienzyme complex from Salmonella typhimurium
    • Hyde, C. C., Ahmed, S. A., Padlan, E. A., Miles, E. W., and Davies, D. R. (1988) Three-dimensional structure of the trptophan synthase α2β2 multienzyme complex from Salmonella typhimurium J. Biol. Chem. 263, 17857-17871
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1    Ahmed, S.A.2    Padlan, E.A.3    Miles, E.W.4    Davies, D.R.5
  • 5
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution
    • DOI 10.1021/bi961856c
    • Shaw, J. P., Petsko, G. A., and Ringe, D. (1997) Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution Biochemistry 36, 1329-1342 (Pubitemid 27074957)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, G.A.2    Ringe, D.3
  • 7
    • 0035900982 scopus 로고    scopus 로고
    • Metal ion inhibition of nonenzymatic pyridoxal phosphate catalyzed decarboxylation and transamination
    • DOI 10.1021/ja0026354
    • Zabinski, R. F. and Toney, M. D. (2001) Metal ion inhibition of nonenzymatic pyridoxal phosphate catalyzed decarboxylation and transamination J. Am. Chem. Soc. 123, 193-198 (Pubitemid 32062162)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.2 , pp. 193-198
    • Zabinski, R.F.1    Toney, M.D.2
  • 8
    • 0027954463 scopus 로고
    • Characterization of the apparent negative co-operativity induced m Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change
    • Onuffer, J. J. and Kirsch, J. F. (1994) Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change Protein Eng. 7, 413-424 (Pubitemid 24063141)
    • (1994) Protein Engineering , vol.7 , Issue.3 , pp. 413-424
    • Onuffer, J.J.1    Kirsch, J.F.2
  • 10
    • 0033591876 scopus 로고    scopus 로고
    • Influence of Electrostatic Effects on Activation Barriers in Enzymatic Reactions: Pyridoxal 5′-Phosphate-Dependent Decarboxylation of α-Amino Acids
    • Bach, R. D., Canepa, C., and Glukhovtsev, M. N. (1999) Influence of Electrostatic Effects on Activation Barriers in Enzymatic Reactions: Pyridoxal 5′-Phosphate-Dependent Decarboxylation of α-Amino Acids J. Am. Chem. Soc. 121, 6542-6555
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6542-6555
    • Bach, R.D.1    Canepa, C.2    Glukhovtsev, M.N.3
  • 11
    • 70349087290 scopus 로고    scopus 로고
    • Pyridoxal 5′-phosphate: Electrophilic catalyst extraordinaire
    • Richard, J. P., Amyes, T. L., Crugeiras, J., and Rios, A. (2009) Pyridoxal 5′-phosphate: Electrophilic catalyst extraordinaire Curr. Opin. Chem. Biol. 13, 475-483
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 475-483
    • Richard, J.P.1    Amyes, T.L.2    Crugeiras, J.3    Rios, A.4
  • 12
    • 33745656984 scopus 로고    scopus 로고
    • Transition state stabilization and α-amino carbon acidity in alanine racemase
    • DOI 10.1021/ja062272t
    • Major, D. T., Nam, K., and Gao, J. (2006) Transition state stabilization and α-amino carbon acidity in alanine racemase J. Am. Chem. Soc. 128, 8114-8115 (Pubitemid 43967737)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.25 , pp. 8114-8115
    • Major, D.T.1    Nam, K.2    Gao, J.3
  • 13
    • 58249145025 scopus 로고    scopus 로고
    • Theoretical study on the distribution of atomic charges in the Schiff bases of 3-hydroxypyridine-4-aldehyde and alanine. the effect of the protonation state of the pyridine and imine nitrogen atoms
    • Casasnovas, R., Salva, A., Frau, J., Donoso, J., and Munoz, F. (2009) Theoretical study on the distribution of atomic charges in the Schiff bases of 3-hydroxypyridine-4-aldehyde and alanine. The effect of the protonation state of the pyridine and imine nitrogen atoms Chem. Phys. 355, 149-156
    • (2009) Chem. Phys. , vol.355 , pp. 149-156
    • Casasnovas, R.1    Salva, A.2    Frau, J.3    Donoso, J.4    Munoz, F.5
  • 14
    • 75449092895 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of 1-deaza-pyridoxal 5′-phosphate
    • Griswold, W. R. and Toney, M. D. (2010) Chemoenzymatic synthesis of 1-deaza-pyridoxal 5′-phosphate Bioorg. Med. Chem. Lett. 20, 1352-1354
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1352-1354
    • Griswold, W.R.1    Toney, M.D.2
  • 15
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J. and Messing, J. (1987) Production of single-stranded plasmid DNA Methods Enzymol. 153, 3-11
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 16
    • 0027405984 scopus 로고
    • Lysine 258 in aspartate aminotransferase: Enforcer of the circle effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift
    • Toney, M. D. and Kirsch, J. F. (1993) Lysine 258 in aspartate aminotransferase: Enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift Biochemistry 32, 1471-1479 (Pubitemid 23077553)
    • (1993) Biochemistry , vol.32 , Issue.6 , pp. 1471-1479
    • Toney, M.D.1    Kirsch, J.F.2
  • 17
    • 0028103275 scopus 로고
    • The ccp4 suite: Programs for protein crystallography
    • Collaborative Computational Project Numer 4 ()
    • Collaborative Computational Project Numer 4 (1994) The ccp4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 23
    • 0028167665 scopus 로고
    • X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form
    • Okamoto, A., Higuchi, T., Hirotsu, K., Kuramitsu, S., and Kagamiyama, H. (1994) X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form J. Biochem. 116, 95-107
    • (1994) J. Biochem. , vol.116 , pp. 95-107
    • Okamoto, A.1    Higuchi, T.2    Hirotsu, K.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 24
    • 0032573119 scopus 로고    scopus 로고
    • The imine-pyridine torsion of the pyridoxal 5'-phosphate schiff base of aspartate aminotransferase lowers its pK(a) in the unliganded enzyme and is crucial for the successive increase in the pK(a) during catalysis
    • DOI 10.1021/bi981517e
    • Hayashi, H., Mizuguchi, H., and Kagamiyama, H. (1998) The imine-pyridine torsion of the pyridoxal 5′-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis Biochemistry 37, 15076-15085 (Pubitemid 28503235)
    • (1998) Biochemistry , vol.37 , Issue.43 , pp. 15076-15085
    • Hayashi, H.1    Mizuguchi, H.2    Kagamiyama, H.3
  • 26
    • 0026664513 scopus 로고
    • Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate
    • Yano, T., Kuramitsu, S., Tanase, S., Morino, Y., and Kagamiyama, H. (1992) Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5′-phosphate Biochemistry 31, 5878-5887
    • (1992) Biochemistry , vol.31 , pp. 5878-5887
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Kagamiyama, H.5
  • 27
    • 0021634693 scopus 로고
    • Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure
    • DOI 10.1016/0022-2836(84)90333-4
    • Kirsch, J. F., Eichele, G., Ford, G. C., Vincent, M. G., Jansonius, J. N., Gehring, H., and Christen, P. (1984) Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure J. Mol. Biol. 174, 497-525 (Pubitemid 15011750)
    • (1984) Journal of Molecular Biology , vol.174 , Issue.3 , pp. 497-525
    • Kirsch, J.F.1    Eichele, G.2    Ford, G.C.3
  • 28
    • 0037657606 scopus 로고    scopus 로고
    • Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: Application to alanine racemase
    • DOI 10.1021/bi0274064
    • Spies, M. A. and Toney, M. D. (2003) Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: Application to alanine racemase Biochemistry 42, 5099-5107 (Pubitemid 36532064)
    • (2003) Biochemistry , vol.42 , Issue.17 , pp. 5099-5107
    • Spies, M.A.1    Toney, M.D.2
  • 29
    • 1242273640 scopus 로고    scopus 로고
    • α,β-Elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required?
    • DOI 10.1016/S1570-9639(03)00052-9
    • Cook, P. F. (2003) α,β-Elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? Biochim. Biophys. Acta 1647, 66-69 (Pubitemid 38234634)
    • (2003) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1647 , Issue.1-2 , pp. 66-69
    • Cook, P.F.1
  • 30
    • 79952254697 scopus 로고    scopus 로고
    • Substituent Effects on Electrophillic Catalysis by the Carbonyl Group: Anatomy of the Rate Acceleration for PLP-Catalyzed Deprotonation of Glycine
    • Crugeiras, J., Rios, A., Riveiros, E., and Richard, J. P. (2011) Substituent Effects on Electrophillic Catalysis by the Carbonyl Group: Anatomy of the Rate Acceleration for PLP-Catalyzed Deprotonation of Glycine J. Am. Chem. Soc. 133, 3173-3183
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3173-3183
    • Crugeiras, J.1    Rios, A.2    Riveiros, E.3    Richard, J.P.4
  • 31
    • 75449097725 scopus 로고
    • Catalytic Activities of Salicylaldehyde Derivatives. II. Kinetic Studies of the Racemization of Amino Acids
    • Ando, M. (1969) Catalytic Activities of Salicylaldehyde Derivatives. II. Kinetic Studies of the Racemization of Amino Acids Bull. Chem. Soc. Jpn. 42, 2628-2631
    • (1969) Bull. Chem. Soc. Jpn. , vol.42 , pp. 2628-2631
    • Ando, M.1
  • 32
    • 79959785241 scopus 로고
    • Catalytic Activities of Salicylaldehdye Derivatives. VIII. Kinetic Studies of the Catalytic Racemization of l -Glutamic Acid at 25 °c
    • Ando, M. (1978) Catalytic Activities of Salicylaldehdye Derivatives. VIII. Kinetic Studies of the Catalytic Racemization of l -Glutamic Acid at 25 °C Bull. Chem. Soc. Jpn. 51, 2366-2368
    • (1978) Bull. Chem. Soc. Jpn. , vol.51 , pp. 2366-2368
    • Ando, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.