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Volumn 45, Issue 35, 2006, Pages 10412-10421

Crystal structure of α-amino-β-carboxymuconate-ε- semialdeliyde decarboxylase: Insight into the active site and catalytic mechanism of a novel decarboxylation reaction

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BIOSYNTHESIS; CATALYSIS; CONFORMATIONS; CRYSTAL STRUCTURE; ENZYMES; HYDROGEN BONDS; METABOLISM;

EID: 33748250307     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060903q     Document Type: Article
Times cited : (46)

References (39)
  • 3
    • 0034666543 scopus 로고    scopus 로고
    • A novel degradative pathway of 2-nitrobenzoate via 3-hydroxyanthranilate in Pseudomonas fluorescens strain KU-7
    • Hasegawa, Y., Muraki, T., Tokuyama, T., Iwaki, H., Tatsuno, M., and Lau, P. C. (2000) A novel degradative pathway of 2-nitrobenzoate via 3-hydroxyanthranilate in Pseudomonas fluorescens strain KU-7, FEMS Microbiol. Lett. 190, 185-90.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 185-190
    • Hasegawa, Y.1    Muraki, T.2    Tokuyama, T.3    Iwaki, H.4    Tatsuno, M.5    Lau, P.C.6
  • 4
    • 0037338581 scopus 로고    scopus 로고
    • Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7
    • Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H., and Lau, P. C. (2003) Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7, Appl. Environ. Microbiol. 69, 1564-72.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1564-1572
    • Muraki, T.1    Taki, M.2    Hasegawa, Y.3    Iwaki, H.4    Lau, P.C.5
  • 5
    • 12444320333 scopus 로고    scopus 로고
    • The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction
    • Colabroy, K. L., and Begley, T. P. (2005) The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction, J. Am. Chem. Soc. 127, 840-1.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 840-841
    • Colabroy, K.L.1    Begley, T.P.2
  • 6
    • 0000276819 scopus 로고
    • Metabolism of the benzene ring of tryptophan (mammals). II. Picolinic carboxylase (cat liver) (α-amino-β-carboxymuconic-ε-semialdehyde β-decarboxylase)
    • Nishizuka, Y., Ichiyama, A., and Hayaishi, O. (1970) Metabolism of the benzene ring of tryptophan (mammals). II. Picolinic carboxylase (cat liver) (α-amino-β-carboxymuconic-ε-semialdehyde β-decarboxylase), Methods Enzymol. 17, 471-6.
    • (1970) Methods Enzymol. , vol.17 , pp. 471-476
    • Nishizuka, Y.1    Ichiyama, A.2    Hayaishi, O.3
  • 7
    • 0348143569 scopus 로고
    • Tryptophan-niacin relationship in Xanthomonas pruni
    • Wilson, R., and Henderson, L. (1962) Tryptophan-niacin relationship in Xanthomonas pruni, J. Bacteriol. 85, 221-8.
    • (1962) J. Bacteriol. , vol.85 , pp. 221-228
    • Wilson, R.1    Henderson, L.2
  • 8
    • 0000936823 scopus 로고
    • Metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid
    • Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O., and Senoh, S. (1965) Metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid, J. Biol. Chem. 240, 740-9.
    • (1965) J. Biol. Chem. , vol.240 , pp. 740-749
    • Ichiyama, A.1    Nakamura, S.2    Kawai, H.3    Honjo, T.4    Nishizuka, Y.5    Hayaishi, O.6    Senoh, S.7
  • 9
    • 0036690151 scopus 로고    scopus 로고
    • Endogenous kynurenines as targets for drug discovery and development
    • Stone, T. W., and Darlington, L. G. (2002) Endogenous kynurenines as targets for drug discovery and development, Nat. Rev. Drug Discovery 1, 609-20.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 609-620
    • Stone, T.W.1    Darlington, L.G.2
  • 10
    • 0742323784 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a drug target
    • Schwarcz, R. (2004) The kynurenine pathway of tryptophan degradation as a drug target, Curr. Opin. Pharmacol. 4, 12-7.
    • (2004) Curr. Opin. Pharmacol. , vol.4 , pp. 12-17
    • Schwarcz, R.1
  • 11
    • 0020702374 scopus 로고
    • Quinolinic acid: An endogenous metabolite that produces axon-sparing lesions in rat brain
    • Schwarcz, R., Whetsell, W. O., Jr., and Mangano, R. M. (1983) Quinolinic acid: An endogenous metabolite that produces axon-sparing lesions in rat brain, Science 219, 316-8.
    • (1983) Science , vol.219 , pp. 316-318
    • Schwarcz, R.1    Whetsell Jr., W.O.2    Mangano, R.M.3
  • 13
    • 0000515044 scopus 로고
    • Studies with carboxyl-labeled 3-hydroxyanthranilic and picolinic acids in vivo and in vitro
    • May, E. L., and Mehler, A. H. (1956) Studies with carboxyl-labeled 3-hydroxyanthranilic and picolinic acids in vivo and in vitro, J. Biol. Chem. 223, 449-55.
    • (1956) J. Biol. Chem. , vol.223 , pp. 449-455
    • May, E.L.1    Mehler, A.H.2
  • 14
    • 0000070989 scopus 로고
    • Formation of picolinic and quinolinic acids following enzymatic oxidation of 3-hydroxyanthranilic acid
    • Mehler, A. H. (1956) Formation of picolinic and quinolinic acids following enzymatic oxidation of 3-hydroxyanthranilic acid, J. Biol. Chem. 218, 241-54.
    • (1956) J. Biol. Chem. , vol.218 , pp. 241-254
    • Mehler, A.H.1
  • 15
    • 24644500630 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor
    • Li, T., Walker, A. L., Iwaki, H., Hasegawa, Y., and Liu, A. (2005) Kinetic and spectroscopic characterization of ACMSD from Pseudomonas fluorescens reveals a pentacoordinate mononuclear metallocofactor, J. Am. Chem. Soc. 127, 12282-90.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12282-12290
    • Li, T.1    Walker, A.L.2    Iwaki, H.3    Hasegawa, Y.4    Liu, A.5
  • 16
    • 33744728709 scopus 로고    scopus 로고
    • α-amino-β-carboxymuconic-6-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily
    • Li, T., Iwaki, H., Fu, R., Hasegawa, Y., Zhang, H., and Liu, A. (2006) α-Amino-β-carboxymuconic-6-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily, Biochemistry 45, 6628-34.
    • (2006) Biochemistry , vol.45 , pp. 6628-6634
    • Li, T.1    Iwaki, H.2    Fu, R.3    Hasegawa, Y.4    Zhang, H.5    Liu, A.6
  • 17
    • 17844384785 scopus 로고    scopus 로고
    • Structural and catalytic diversity within the amidohydrolase superfamily
    • Seibert, C. M., and Raushel, F. M. (2005) Structural and catalytic diversity within the amidohydrolase superfamily, Biochemistry 44, 6383-91.
    • (2005) Biochemistry , vol.44 , pp. 6383-6391
    • Seibert, C.M.1    Raushel, F.M.2
  • 18
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm, L., and Sander, C. (1997) An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease, Proteins 28, 72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 19
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J. A., and Babbitt, P. C. (2001) Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies, Annu. Rev. Biochem. 70, 209-46.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 20
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie, S. (1997) Preparation of selenomethionyl proteins for phase determination, Methods Enzymol. 276, 523-30.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 21
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger, T. C. (2002) Automated structure solution, density modification and model building, Acta Crystallogr. D58, 1937-40.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-9.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin, A., and Teplyakov, A. (2000) An approach to multi-copy search in molecular replacement, Acta Crystallogr. D56, 1622-4.
    • (2000) Acta Crystallogr. , vol.D56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. D53, 240-55.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for protein crystallography, Acta Crystallogr. D50, 760-3.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 28
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm, L., and Sander, C. (1995) Dali: A network tool for protein structure comparison, Trends Biochem. Sci. 20, 478-80.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 29
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: A structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 247, 536-40.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 30
    • 0038671973 scopus 로고    scopus 로고
    • High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli
    • Thoden, J. B., Marti-Arbona, R., Raushel, F. M., and Holden, H. M. (2003) High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli, Biochemistry 42, 4874-82.
    • (2003) Biochemistry , vol.42 , pp. 4874-4882
    • Thoden, J.B.1    Marti-Arbona, R.2    Raushel, F.M.3    Holden, H.M.4
  • 31
    • 0032499630 scopus 로고    scopus 로고
    • Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity
    • Wang, Z., and Quiocho, F. A. (1998) Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity, Biochemistry 37, 8314-24.
    • (1998) Biochemistry , vol.37 , pp. 8314-8324
    • Wang, Z.1    Quiocho, F.A.2
  • 33
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • Benning, M. M., Kuo, J. M., Raushel, F. M., and Holden, H. M. (1995) Three-dimensional structure of the binuclear metal center of phosphotriesterase, Biochemistry 34, 7973-8.
    • (1995) Biochemistry , vol.34 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 34
    • 0030848288 scopus 로고    scopus 로고
    • Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease
    • Pearson, M. A., Michel, L. O., Hausinger, R. P., and Karplus, P. A. (1997) Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease, Biochemistry 36, 8164-72.
    • (1997) Biochemistry , vol.36 , pp. 8164-8172
    • Pearson, M.A.1    Michel, L.O.2    Hausinger, R.P.3    Karplus, P.A.4
  • 36
    • 0026434561 scopus 로고
    • Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson, D. K., Rudolph, F. B., and Quiocho, F. A. (1991) Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations, Science 252, 1278-84.
    • (1991) Science , vol.252 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 37
    • 0034622579 scopus 로고    scopus 로고
    • A closer look at the active site of γ-class carbonic anhydrases: High-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila
    • Iverson, T. M., Alber, B. E., Kisker, C., Ferry, J. G., and Rees, D. C. (2000) A closer look at the active site of γ-class carbonic anhydrases: High-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila, Biochemistry 39, 9222-31.
    • (2000) Biochemistry , vol.39 , pp. 9222-9231
    • Iverson, T.M.1    Alber, B.E.2    Kisker, C.3    Ferry, J.G.4    Rees, D.C.5
  • 38
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase: Evolution of the zinc binding site by nature and by design
    • Christianson, D. W., and Fierke, C. A. (1996) Carbonic Anhydrase: Evolution of the Zinc Binding Site by Nature and by Design, Acc. Chem. Res. 29, 331-9.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 331-339
    • Christianson, D.W.1    Fierke, C.A.2
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-50.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.