메뉴 건너뛰기




Volumn 464, Issue 3, 2014, Pages 387-399

Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins

Author keywords

2,5 dimethylpyrazine; Aminoacetone; Enzyme structure; Flavoprotein; X ray crystallography

Indexed keywords

AMINO ACID OXIDASE; AMINOACETONE OXIDASE; BACTERIAL ENZYME; FLAVOPROTEIN; OXIDOREDUCTASE; UNCLASSIFIED DRUG; 2,5-DIMETHYLPYRAZINE; ACETONE; AMINOACETONE; GLYCINE; GLYCINE METHYL ESTER; POLYAMINE OXIDASE; PYRAZINE DERIVATIVE;

EID: 84915733908     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140972     Document Type: Article
Times cited : (15)

References (47)
  • 1
    • 79953321262 scopus 로고    scopus 로고
    • Streptococcus mutans and oral streptococci in dental plaque
    • CrossRef PubMed
    • Nicolas, G. G. and Lavoie, M. C. (2011) Streptococcus mutans and oral streptococci in dental plaque. Can. J. Microbiol. 57, 1-20 CrossRef PubMed
    • (2011) Can. J. Microbiol. , vol.57 , pp. 1-20
    • Nicolas, G.G.1    Lavoie, M.C.2
  • 2
    • 0041810300 scopus 로고    scopus 로고
    • Streptococcus oligofermentans sp nov., a novel oral isolate from caries-free humans
    • CrossRef PubMed
    • Tong, H. C., Gao, X. J. and Dong, X. Z. (2003) Streptococcus oligofermentans sp nov., a novel oral isolate from caries-free humans. Int. J. Syst. Evol. Microbiol. 53, 1101-1104 CrossRef PubMed
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 1101-1104
    • Tong, H.C.1    Gao, X.J.2    Dong, X.Z.3
  • 3
    • 33846245425 scopus 로고    scopus 로고
    • Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H2O2: A possible counteroffensive strategy for interspecies competition
    • CrossRef PubMed
    • Tong, H., Chen, W., Merritt, J., Qi, F., Shi, W. and Dong, X. (2007) Streptococcus oligofermentans inhibits Streptococcus mutans through conversion of lactic acid into inhibitory H2O2: a possible counteroffensive strategy for interspecies competition. Mol. Microbiol. 63, 872-880 CrossRef PubMed
    • (2007) Mol. Microbiol. , vol.63 , pp. 872-880
    • Tong, H.1    Chen, W.2    Merritt, J.3    Qi, F.4    Shi, W.5    Dong, X.6
  • 4
    • 46049104610 scopus 로고    scopus 로고
    • SO-LAAO, a novel L-amino acid oxidase that enables Streptococcus oligofermentans to outcompete Streptococcus mutans by generating H2O2 from peptone
    • CrossRef PubMed
    • Tong, H. C., Chen, W., Shi, W. Y., Qi, F. X. and Dong, X. Z. (2008) SO-LAAO, a novel L-amino acid oxidase that enables Streptococcus oligofermentans to outcompete Streptococcus mutans by generating H2O2 from peptone. J. Bacteriol. 190, 4716-4721 CrossRef PubMed
    • (2008) J. Bacteriol. , vol.190 , pp. 4716-4721
    • Tong, H.C.1    Chen, W.2    Shi, W.Y.3    Qi, F.X.4    Dong, X.Z.5
  • 5
    • 84860375876 scopus 로고    scopus 로고
    • Phylogenetic analysis supports horizontal gene transfer of L-amino acid oxidase gene in Streptococcus oligofermentans
    • CrossRef PubMed
    • Boggs, J. M., South, A. H. and Hughes, A. L. (2012) Phylogenetic analysis supports horizontal gene transfer of L-amino acid oxidase gene in Streptococcus oligofermentans. Infect. Genet. Evol. 12, 1005-1009 CrossRef PubMed
    • (2012) Infect. Genet. Evol. , vol.12 , pp. 1005-1009
    • Boggs, J.M.1    South, A.H.2    Hughes, A.L.3
  • 6
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding β-α-β-fold in proteins, using an amino-acid-sequence fingerprint
    • CrossRef PubMed
    • Wierenga, R. K., Terpstra, P. and Hol, W. G. J. (1986) Prediction of the occurrence of the ADP-binding β-α-β-fold in proteins, using an amino-acid-sequence fingerprint. J. Mol. Biol. 187, 101-107 CrossRef PubMed
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 7
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • CrossRef PubMed
    • Pawelek, P. D., Cheah, J., Coulombe, R., Macheroux, P., Ghisla, S. and Vrielink, A. (2000) The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J. 19, 4204-4215 CrossRef PubMed
    • (2000) EMBO J. , vol.19 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 8
    • 0036644230 scopus 로고    scopus 로고
    • A new bacterial L-amino acid oxidase with a broad substrate specificity: Purification and characterization
    • Geueke, B. and Hummel, W. (2002) A new bacterial L-amino acid oxidase with a broad substrate specificity: purification and characterization. Enzyme Microb. Technol. 31, 77-87
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 77-87
    • Geueke, B.1    Hummel, W.2
  • 9
    • 84886883411 scopus 로고    scopus 로고
    • L-Amino acid oxidase as biocatalyst: A dream too far?
    • CrossRef PubMed
    • Pollegioni, L., Motta, P. and Molla, G. (2013) L-Amino acid oxidase as biocatalyst: a dream too far? Appl. Microbiol. Biotechnol. 97, 9323-9341 CrossRef PubMed
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 9323-9341
    • Pollegioni, L.1    Motta, P.2    Molla, G.3
  • 10
    • 0036234815 scopus 로고    scopus 로고
    • Snake venom L-amino acid oxidases
    • CrossRef PubMed
    • Du, X. Y. and Clemetson, K. J. (2002) Snake venom L-amino acid oxidases. Toxicon 40, 659-665 CrossRef PubMed
    • (2002) Toxicon , vol.40 , pp. 659-665
    • Du, X.Y.1    Clemetson, K.J.2
  • 11
    • 0033741877 scopus 로고    scopus 로고
    • The X-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation
    • CrossRef PubMed
    • Umhau, S., Pollegioni, L., Molla, G., Diederichs, K., Welte, W., Pilone, M. S. and Ghisla, S. (2000) The X-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. Proc. Natl. Acad. Sci. U.S.A. 97, 12463-12468 CrossRef PubMed
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12463-12468
    • Umhau, S.1    Pollegioni, L.2    Molla, G.3    Diederichs, K.4    Welte, W.5    Pilone, M.S.6    Ghisla, S.7
  • 12
    • 34250002745 scopus 로고    scopus 로고
    • Physiological functions of D-amino acid oxidases: From yeast to humans
    • CrossRef PubMed
    • Pollegioni, L., Piubelli, L., Sacchi, S., Pilone, M. S. and Molla, G. (2007) Physiological functions of D-amino acid oxidases: from yeast to humans. Cell. Mol. Life Sci. 64, 1373-1394 CrossRef PubMed
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1373-1394
    • Pollegioni, L.1    Piubelli, L.2    Sacchi, S.3    Pilone, M.S.4    Molla, G.5
  • 13
    • 79956146208 scopus 로고    scopus 로고
    • New biotech applications from evolved D-amino acid oxidases
    • CrossRef PubMed
    • Pollegioni, L. and Molla, G. (2011) New biotech applications from evolved D-amino acid oxidases. Trends Biotechnol. 29, 276-283 CrossRef PubMed
    • (2011) Trends Biotechnol. , vol.29 , pp. 276-283
    • Pollegioni, L.1    Molla, G.2
  • 14
    • 84861596959 scopus 로고    scopus 로고
    • Role of operon aaoSo -mutT in antioxidant defense in Streptococcus oligofermentans
    • CrossRef PubMed
    • Zhou, P., Liu, L., Tong, H. and Dong, X. (2012) Role of operon aaoSo -mutT in antioxidant defense in Streptococcus oligofermentans. PLoS ONE 7, e38133 CrossRef PubMed
    • (2012) PLoS ONE , vol.7 , pp. e38133
    • Zhou, P.1    Liu, L.2    Tong, H.3    Dong, X.4
  • 15
    • 0028831526 scopus 로고
    • Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta
    • CrossRef PubMed
    • Lyles, G. A. and Chalmers, J. (1995) Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta. Biochem. Pharmacol. 49, 416-419 CrossRef PubMed
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 416-419
    • Lyles, G.A.1    Chalmers, J.2
  • 17
    • 77951076300 scopus 로고    scopus 로고
    • Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli
    • CrossRef PubMed
    • Volontè, F., Pollegioni, L., Molla, G., Frattini, L., Marinelli, F. and Piubelli, L. (2010) Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli. BMC Biotechnol. 10, 33 CrossRef PubMed
    • (2010) BMC Biotechnol. , vol.10 , pp. 33
    • Volontè, F.1    Pollegioni, L.2    Molla, G.3    Frattini, L.4    Marinelli, F.5    Piubelli, L.6
  • 18
    • 80655125152 scopus 로고    scopus 로고
    • Enzymatic detection of D-amino acids
    • (Pollegioni, L. and Servi, S., eds) , Humana Press, Totowa CrossRef
    • Molla, G., Piubelli, L., Volonte, F. and Pilone, M. S. (2012) Enzymatic detection of D-amino acids. In Unnatural Amino Acids: Methods and Protocols (Pollegioni, L. and Servi, S., eds), pp. 273-289, Humana Press, Totowa CrossRef
    • (2012) Unnatural Amino Acids: Methods and Protocols , pp. 273-289
    • Molla, G.1    Piubelli, L.2    Volonte, F.3    Pilone, M.S.4
  • 19
    • 0014231053 scopus 로고
    • The oxidation of aminoacetone by a species of Arthrobacter
    • PubMed
    • Green, M. L. and Lewis, J. B. (1968) The oxidation of aminoacetone by a species of Arthrobacter . Biochem. J. 106, 267-270 PubMed
    • (1968) Biochem. J. , vol.106 , pp. 267-270
    • Green, M.L.1    Lewis, J.B.2
  • 20
    • 0017817482 scopus 로고
    • Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins
    • CrossRef PubMed
    • Massey, V. and Hemmerich, P. (1978) Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Biochemistry 17, 9-17 CrossRef PubMed
    • (1978) Biochemistry , vol.17 , pp. 9-17
    • Massey, V.1    Hemmerich, P.2
  • 21
    • 0033579446 scopus 로고    scopus 로고
    • Studies on the reaction mechanism of Rhodotorula gracilis D-amino-acid oxidase: Role of the highly conserved Tyr-223 on substrate binding and catalysis
    • CrossRef PubMed
    • Harris, C. M., Molla, G., Pilone, M. S. and Pollegioni, L. (1999) Studies on the reaction mechanism of Rhodotorula gracilis D-amino-acid oxidase: role of the highly conserved Tyr-223 on substrate binding and catalysis. J. Biol. Chem. 274, 36233-36240 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 36233-36240
    • Harris, C.M.1    Molla, G.2    Pilone, M.S.3    Pollegioni, L.4
  • 22
    • 0036510613 scopus 로고    scopus 로고
    • Glycine oxidase from Bacillus subtilis: Characterization of a new flavoprotein
    • CrossRef PubMed
    • Job, V., Marcone, G. L., Pilone, M. S. and Pollegioni, L. (2002) Glycine oxidase from Bacillus subtilis: characterization of a new flavoprotein. J. Biol. Chem. 277, 6985-6993 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 6985-6993
    • Job, V.1    Marcone, G.L.2    Pilone, M.S.3    Pollegioni, L.4
  • 24
    • 0002435359 scopus 로고
    • Simple method for the determination of redox potentials
    • (Curti, B., Ronchi, S. and Zanetti, G., eds) , Walter de Gruyter & Co., Berlin
    • Massey, V. A. (1991) simple method for the determination of redox potentials. In In Flavins and Flavoproteins (Curti, B., Ronchi, S. and Zanetti, G., eds), pp. 59-66, Walter de Gruyter & Co., Berlin
    • (1991) Flavins and Flavoproteins , pp. 59-66
    • Massey, V.A.1
  • 25
    • 0033778027 scopus 로고    scopus 로고
    • Redox potentials and their pH dependence of D-amino acid oxidase of Rhodotorula gracilis and Trigonopsis variabilis
    • CrossRef PubMed
    • Pollegioni, L., Porrini, D., Molla, G. and Pilone, M. S. (2000) Redox potentials and their pH dependence of D-amino acid oxidase of Rhodotorula gracilis and Trigonopsis variabilis. Eur. J. Biochem. 267, 6624-6632 CrossRef PubMed
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6624-6632
    • Pollegioni, L.1    Porrini, D.2    Molla, G.3    Pilone, M.S.4
  • 27
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • CrossRef PubMed
    • Evans, P. (2006) Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62, 72-82 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 72-82
    • Evans, P.1
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • CrossRef PubMed
    • Murshudov, G. N., Vagin, A. A. and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240-255 CrossRef PubMed
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • CrossRef PubMed
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 CrossRef PubMed
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 33
    • 38349152169 scopus 로고    scopus 로고
    • Properties and applications of microbial D-amino acid oxidases: Current state and perspectives
    • CrossRef PubMed
    • Pollegioni, L., Molla, G., Sacchi, S., Rosini, E., Verga, R. and Pilone, M. S. (2008) Properties and applications of microbial D-amino acid oxidases: current state and perspectives. Appl. Microbiol. Biotechnol. 78, 1-16 CrossRef PubMed
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 1-16
    • Pollegioni, L.1    Molla, G.2    Sacchi, S.3    Rosini, E.4    Verga, R.5    Pilone, M.S.6
  • 34
    • 73049116896 scopus 로고    scopus 로고
    • FAD binding in glycine oxidase from Bacillus subtilis
    • CrossRef PubMed
    • Caldinelli, L., Pedotti, M., Motteran, L., Molla, G. and Pollegioni, L. (2009) FAD binding in glycine oxidase from Bacillus subtilis. Biochimie 91, 1499-1508 CrossRef PubMed
    • (2009) Biochimie , vol.91 , pp. 1499-1508
    • Caldinelli, L.1    Pedotti, M.2    Motteran, L.3    Molla, G.4    Pollegioni, L.5
  • 35
    • 0242267926 scopus 로고    scopus 로고
    • Deflavination and reconstitution of flavoproteins
    • CrossRef PubMed
    • Hefti, M. H., Vervoort, J. and van Berkel, W. J. (2003) Deflavination and reconstitution of flavoproteins. Eur. J. Biochem. 270, 4227-4242 CrossRef PubMed
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4227-4242
    • Hefti, M.H.1    Vervoort, J.2    Van Berkel, W.J.3
  • 36
    • 20744438190 scopus 로고    scopus 로고
    • Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin
    • CrossRef PubMed
    • Caldinelli, L., Iametti, S., Barbiroli, A., Bonomi, F., Fessas, D., Molla, G., Pilone, M. S. and Pollegioni, L. (2005) Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin. J. Biol. Chem. 280, 22572-22581 CrossRef PubMed
    • (2005) J. Biol. Chem. , vol.280 , pp. 22572-22581
    • Caldinelli, L.1    Iametti, S.2    Barbiroli, A.3    Bonomi, F.4    Fessas, D.5    Molla, G.6    Pilone, M.S.7    Pollegioni, L.8
  • 37
    • 84868200797 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • CrossRef
    • Louis-Jeune, C., Andrade-Navarro, M. A. and Perez-Iratxeta, C. (2012) Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins 80, 374-381 CrossRef
    • (2012) Proteins , vol.80 , pp. 374-381
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3
  • 38
    • 0019023686 scopus 로고
    • Active-site probes of flavoproteins
    • PubMed
    • Massey, V. and Hemmerich, P. (1980) Active-site probes of flavoproteins. Biochem. Soc. Trans. 8, 246-257 PubMed
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 246-257
    • Massey, V.1    Hemmerich, P.2
  • 39
    • 0034823588 scopus 로고    scopus 로고
    • L-Amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma : Comparative sequence analysis and characterization of active and inactive forms of the enzyme
    • CrossRef PubMed
    • Macheroux, P., Seth, O., Bollschweiler, C., Schwarz, M., Kurfurst, M., Au, L. C. and Ghisla, S. (2001) L-Amino-acid oxidase from the Malayan pit viper Calloselasma rhodostoma : comparative sequence analysis and characterization of active and inactive forms of the enzyme. Eur. J. Biochem. 268, 1679-1686 CrossRef PubMed
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1679-1686
    • Macheroux, P.1    Seth, O.2    Bollschweiler, C.3    Schwarz, M.4    Kurfurst, M.5    Au, L.C.6    Ghisla, S.7
  • 40
  • 41
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • CrossRef PubMed
    • Holm, L. and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 CrossRef PubMed
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 42
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • CrossRef PubMed
    • Dym, O. and Eisenberg, D. (2001) Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10, 1712-1728 CrossRef PubMed
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 43
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05Åresolution
    • CrossRef PubMed
    • Song, H., Parsons, M. R., Rowsell, S., Leonard, G. and Phillips, S. E. (1999) Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05Åresolution. J. Mol. Biol. 285, 1245-1256 CrossRef PubMed
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 44
    • 0037413727 scopus 로고    scopus 로고
    • Structure of the topoisomerase VI-B subunit: Implications for type II topoisomerase mechanism and evolution
    • CrossRef PubMed
    • Corbett, K. D. and Berger, J. M. (2003) Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution. EMBO J. 22, 151-163 CrossRef PubMed
    • (2003) EMBO J. , vol.22 , pp. 151-163
    • Corbett, K.D.1    Berger, J.M.2
  • 45
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • CrossRef
    • Krissinel, E. and Henrick, K. (2005) Detection of protein assemblies in crystals. Lect. Notes Comput. Sci. 3695, 163-174 CrossRef
    • (2005) Lect. Notes Comput. Sci. , vol.3695 , pp. 163-174
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 0013783250 scopus 로고
    • On the interpretation of the absorption spectra of flavoproteins with special reference to D-amino acid oxidase
    • CrossRef PubMed
    • Massey, V. and Ganther, H. (1965) On the interpretation of the absorption spectra of flavoproteins with special reference to D-amino acid oxidase. Biochemistry 4, 1161-1173 CrossRef PubMed
    • (1965) Biochemistry , vol.4 , pp. 1161-1173
    • Massey, V.1    Ganther, H.2
  • 47
    • 0034802987 scopus 로고    scopus 로고
    • Aerobic oxidation of aminoacetone, a threonine catabolite: Iron catalysis and coupled iron release from ferritin
    • CrossRef PubMed
    • Dutra, F., Knudsen, F. S., Curi, D. and Bechara, E. J. H. (2001) Aerobic oxidation of aminoacetone, a threonine catabolite: Iron catalysis and coupled iron release from ferritin. Chem. Res. Toxicol. 14, 1323-1329 CrossRef PubMed
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1323-1329
    • Dutra, F.1    Knudsen, F.S.2    Curi, D.3    Bechara, E.J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.