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Volumn 291, Issue 20, 2016, Pages 10457-10475

Structure-function relationships in L-amino acid deaminase, a flavoprotein belonging to a novel class of biotechnologically relevant enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; SUBSTRATES;

EID: 84969255700     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.703819     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 1842473615 scopus 로고    scopus 로고
    • Enzyme catalysed deracemisation and dynamic kinetic resolution reactions
    • Turner, N. J. (2004) Enzyme catalysed deracemisation and dynamic kinetic resolution reactions. Curr. Opin. Chem. Biol. 8, 114-119
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 114-119
    • Turner, N.J.1
  • 2
    • 79956146208 scopus 로고    scopus 로고
    • New biotech applications from evolved D-amino acid oxidases
    • Pollegioni, L., and Molla, G. (2011) New biotech applications from evolved D-amino acid oxidases. Trends Biotechnol. 29, 276-283
    • (2011) Trends Biotechnol. , vol.29 , pp. 276-283
    • Pollegioni, L.1    Molla, G.2
  • 4
    • 84886883411 scopus 로고    scopus 로고
    • L-Amino acid oxidase as biocatalyst: A dream too far?
    • Pollegioni, L., Motta, P., and Molla, G. (2013) L-Amino acid oxidase as biocatalyst: a dream too far? Appl. Microbiol. Biotechnol. 97, 9323-9341
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 9323-9341
    • Pollegioni, L.1    Motta, P.2    Molla, G.3
  • 5
    • 0035931396 scopus 로고    scopus 로고
    • Purification and characterization of an L-amino acid deaminase used to prepare unnatural amino acids
    • Pantaleone, D. P., Geller, A. M., and Taylor, P. P. (2001) Purification and characterization of an L-amino acid deaminase used to prepare unnatural amino acids. J. Mol. Catal. B: Enzym. 11, 795-803
    • (2001) J. Mol. Catal. B: Enzym. , vol.11 , pp. 795-803
    • Pantaleone, D.P.1    Geller, A.M.2    Taylor, P.P.3
  • 6
    • 84906788805 scopus 로고    scopus 로고
    • Biocontrolled formal inversion or retention of L-α-amino acids to enantiopure (R)-or (S)-hydroxyacids
    • Busto, E., Richter, N., Grischek, B., and Kroutil, W. (2014) Biocontrolled formal inversion or retention of L-α-amino acids to enantiopure (R)-or (S)-hydroxyacids. Chemistry 20, 11225-11228
    • (2014) Chemistry , vol.20 , pp. 11225-11228
    • Busto, E.1    Richter, N.2    Grischek, B.3    Kroutil, W.4
  • 7
    • 84941995808 scopus 로고    scopus 로고
    • Production of phenylpyruvic acid from L-phenylalanine using an L-amino acid deaminase from Proteus mirabilis: Comparison of enzymatic and whole-cell biotransformation approaches
    • Hou, Y., Hossain, G. S., Li, J., Shin, H. D., Liu, L., and Du, G. (2015) Production of phenylpyruvic acid from L-phenylalanine using an L-amino acid deaminase from Proteus mirabilis: comparison of enzymatic and whole-cell biotransformation approaches. Appl. Microbiol. Biotechnol. 99, 8391-8402
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 8391-8402
    • Hou, Y.1    Hossain, G.S.2    Li, J.3    Shin, H.D.4    Liu, L.5    Du, G.6
  • 8
    • 79960186244 scopus 로고    scopus 로고
    • Phylogenetic analysis of the genera Proteus, Morganella, and Providencia by comparison of rpoB gene sequences of type and clinical strains suggests the reclassification of Proteus myxofaciens in a new genus, Cosenzaea gen. Nov., as Cosenzaea myxofaciens comb. Nov
    • Giammanco, G. M., Grimont, P. A., Grimont, F., Lefevre, M., Giammanco, G., and Pignato, S. (2011) Phylogenetic analysis of the genera Proteus, Morganella, and Providencia by comparison of rpoB gene sequences of type and clinical strains suggests the reclassification of Proteus myxofaciens in a new genus, Cosenzaea gen. nov., as Cosenzaea myxofaciens comb. nov. Int. J. Syst. Evol. Microbiol. 61, 1638-1644
    • (2011) Int. J. Syst. Evol. Microbiol. , vol.61 , pp. 1638-1644
    • Giammanco, G.M.1    Grimont, P.A.2    Grimont, F.3    Lefevre, M.4    Giammanco, G.5    Pignato, S.6
  • 9
    • 84872246445 scopus 로고    scopus 로고
    • Characterization of human DAAO variants potentially related to an increased risk of schizophrenia
    • Caldinelli, L., Sacchi, S., Molla, G., Nardini, M., and Pollegioni, L. (2013) Characterization of human DAAO variants potentially related to an increased risk of schizophrenia. Biochim. Biophys. Acta 1832, 400-410
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 400-410
    • Caldinelli, L.1    Sacchi, S.2    Molla, G.3    Nardini, M.4    Pollegioni, L.5
  • 12
    • 0035719831 scopus 로고    scopus 로고
    • PH and kinetic isotope effects in D-amino acid oxidase catalysis
    • Harris, C. M., Pollegioni, L., and Ghisla, S. (2001) pH and kinetic isotope effects in D-amino acid oxidase catalysis. Eur. J. Biochem. 268, 5504-5520
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5504-5520
    • Harris, C.M.1    Pollegioni, L.2    Ghisla, S.3
  • 13
    • 0034637448 scopus 로고    scopus 로고
    • Role of arginine 285 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study
    • Molla, G., Porrini, D., Job, V., Motteran, L., Vegezzi, C., Campaner, S., Pilone, M. S., and Pollegioni, L. (2000) Role of arginine 285 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study. J. Biol. Chem. 275, 24715-24721
    • (2000) J. Biol. Chem. , vol.275 , pp. 24715-24721
    • Molla, G.1    Porrini, D.2    Job, V.3    Motteran, L.4    Vegezzi, C.5    Campaner, S.6    Pilone, M.S.7    Pollegioni, L.8
  • 14
    • 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
    • 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
    • (1999) J. Biol. Chem. , vol.274 , pp. 36233-36240
    • Harris, C.M.1    Molla, G.2    Pilone, M.S.3    Pollegioni, L.4
  • 15
    • 20744438190 scopus 로고    scopus 로고
    • Dissecting the structural determinants of the stability of cholesterol oxidase containing covalently bound flavin
    • 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
    • (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
  • 19
    • 33746128802 scopus 로고    scopus 로고
    • Heterotetrameric sarcosine oxidase: Structure of a diflavin metalloenzyme at 1.85 Å resolution
    • Chen, Z. W., Hassan-Abdulah, A., Zhao, G., Jorns, M. S., and Mathews, F. S. (2006) Heterotetrameric sarcosine oxidase: structure of a diflavin metalloenzyme at 1.85 Å resolution. J. Mol. Biol. 360, 1000-1018
    • (2006) J. Mol. Biol. , vol.360 , pp. 1000-1018
    • Chen, Z.W.1    Hassan-Abdulah, A.2    Zhao, G.3    Jorns, M.S.4    Mathews, F.S.5
  • 21
  • 24
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • Finn, R. D., Clements, J., and Eddy, S. R. (2011) HMMER web server: interactive sequence similarity searching. Nucleic Acids Res. 39, W29-W37
    • (2011) Nucleic Acids Res. , vol.39 , pp. W29-W37
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 25
    • 79955684513 scopus 로고    scopus 로고
    • Representative proteomes: A stable, scalable and unbiased proteome set for sequence analysis and functional annotation
    • Chen, C., Natale, D. A., Finn, R. D., Huang, H., Zhang, J., Wu, C. H., and Mazumder, R. (2011) Representative proteomes: a stable, scalable and unbiased proteome set for sequence analysis and functional annotation. PLoS ONE 6, e18910
    • (2011) PLoS ONE , vol.6
    • Chen, C.1    Natale, D.A.2    Finn, R.D.3    Huang, H.4    Zhang, J.5    Wu, C.H.6    Mazumder, R.7
  • 26
    • 77949601825 scopus 로고    scopus 로고
    • CD-HIT Suite: A web server for clustering and comparing biological sequences
    • Huang, Y., Niu, B., Gao, Y., Fu, L., and Li, W. (2010) CD-HIT Suite: a web server for clustering and comparing biological sequences. Bioinformatics 26, 680-682
    • (2010) Bioinformatics , vol.26 , pp. 680-682
    • Huang, Y.1    Niu, B.2    Gao, Y.3    Fu, L.4    Li, W.5
  • 27
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • Gouy, M., Guindon, S., and Gascuel, O. (2010) SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol. Biol. Evol. 27, 221-224
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 28
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximumlikelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon, S., Dufayard, J. F., Lefort, V., Anisimova, M., Hordijk, W., and Gascuel, O. (2010) New algorithms and methods to estimate maximumlikelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 59, 307-321
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 29
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. (1985) Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39, 783-791
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 30
    • 79954545667 scopus 로고    scopus 로고
    • Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli
    • Baek, J. O., Seo, J. W., Kwon, O., Seong, S. I., Kim, I. H., and Kim, C. H. (2011) Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli. J. Basic Microbiol. 51, 129-135
    • (2011) J. Basic Microbiol. , vol.51 , pp. 129-135
    • Baek, J.O.1    Seo, J.W.2    Kwon, O.3    Seong, S.I.4    Kim, I.H.5    Kim, C.H.6
  • 31
    • 0014429425 scopus 로고
    • D-Amino acid oxidase. II. Studies of substrate-competitive inhibitors
    • Fonda, M. L., and Anderson, B. M. (1968) D-Amino acid oxidase. II. Studies of substrate-competitive inhibitors. J. Biol. Chem. 243, 1931-1935
    • (1968) J. Biol. Chem. , vol.243 , pp. 1931-1935
    • Fonda, M.L.1    Anderson, B.M.2
  • 33
    • 0019023686 scopus 로고
    • Active-site probes of flavoproteins
    • Massey, V., and Hemmerich, P. (1980) Active-site probes of flavoproteins. Biochem. Soc. Trans. 8, 246-257
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 246-257
    • Massey, V.1    Hemmerich, P.2
  • 34
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • 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
    • (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
  • 35
    • 0027210877 scopus 로고
    • Kinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and Trigonopsis variabilis
    • Pollegioni, L., Langkau, B., Tischer, W., Ghisla, S., and Pilone, M. S. (1993) Kinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and Trigonopsis variabilis. J. Biol. Chem. 268, 13850-13857
    • (1993) J. Biol. Chem. , vol.268 , pp. 13850-13857
    • Pollegioni, L.1    Langkau, B.2    Tischer, W.3    Ghisla, S.4    Pilone, M.S.5
  • 36
    • 84872126781 scopus 로고    scopus 로고
    • Crystal structure of the O-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b
    • Volbeda, A., Darnault, C., Parkin, A., Sargent, F., Armstrong, F. A., and Fontecilla-Camps, J. C. (2013) Crystal structure of the O-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b. Structure 21, 184-190
    • (2013) Structure , vol.21 , pp. 184-190
    • Volbeda, A.1    Darnault, C.2    Parkin, A.3    Sargent, F.4    Armstrong, F.A.5    Fontecilla-Camps, J.C.6
  • 38
    • 0020522469 scopus 로고
    • The membrane-bound b and c-type cytochromes of Proteus mirabilis grown under different conditions. Characterization by means of coupled spectrum deconvolution and potentiometric analysis
    • van Wielink, J. E., Reijnders, W. N., Oltmann, L. F., Leeuwerik, F. J., and Stouthamer, A. H. (1983) The membrane-bound b and c-type cytochromes of Proteus mirabilis grown under different conditions. Characterization by means of coupled spectrum deconvolution and potentiometric analysis. Arch. Microbiol. 134, 118-122
    • (1983) Arch. Microbiol. , vol.134 , pp. 118-122
    • Van Wielink, J.E.1    Reijnders, W.N.2    Oltmann, L.F.3    Leeuwerik, F.J.4    Stouthamer, A.H.5
  • 39
    • 77954288803 scopus 로고    scopus 로고
    • Isolation and purification of complex II from Proteus mirabilis strain ATCC 29245
    • Shabbiri K, Ahmad W, Syed Q, Adnan A. (2010) Isolation and purification of complex II from Proteus mirabilis strain ATCC 29245. Braz. J. Microbiol. 41, 796-804
    • (2010) Braz. J. Microbiol. , vol.41 , pp. 796-804
    • Shabbiri, K.1    Ahmad, W.2    Syed, Q.3    Adnan, A.4
  • 40
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K., and Stoffel, W. (1993) TMbase - a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374, 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 41
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FADcontaining proteins
    • Dym, O., and Eisenberg, D. (2001) Sequence-structure analysis of FADcontaining proteins. Protein Sci. 10, 1712-1728
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 42
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 43
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 44
    • 24744462313 scopus 로고    scopus 로고
    • Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii
    • Tsuge, H., Kawakami, R., Sakuraba, H., Ago, H., Miyano, M., Aki, K., Katunuma, N., and Ohshima, T. (2005) Crystal structure of a novel FAD-, FMN-, and ATP-containing L-proline dehydrogenase complex from Pyrococcus horikoshii. J. Biol. Chem. 280, 31045-31049
    • (2005) J. Biol. Chem. , vol.280 , pp. 31045-31049
    • Tsuge, H.1    Kawakami, R.2    Sakuraba, H.3    Ago, H.4    Miyano, M.5    Aki, K.6    Katunuma, N.7    Ohshima, T.8
  • 46
    • 77958065317 scopus 로고    scopus 로고
    • Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96
    • Moriguchi, T., Ida, K., Hikima, T., Ueno, G., Yamamoto, M., and Suzuki, H. (2010) Channeling and conformational changes in the heterotetrameric sarcosine oxidase from Corynebacterium sp. U-96. J. Biochem. 148, 491-505
    • (2010) J. Biochem. , vol.148 , pp. 491-505
    • Moriguchi, T.1    Ida, K.2    Hikima, T.3    Ueno, G.4    Yamamoto, M.5    Suzuki, H.6
  • 48
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31, 276-283
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 50
    • 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
    • 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
    • (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
  • 51
    • 84924251672 scopus 로고    scopus 로고
    • Systems biocatalysis: An artificial metabolism for interconversion of functional groups
    • Tessaro, D., Pollegioni, L., Piubelli, L., D'Arrigo, P., and Servi, S. (2015) Systems biocatalysis: an artificial metabolism for interconversion of functional groups. ACS Catal. 5, 1604-1608
    • (2015) ACS Catal. , vol.5 , pp. 1604-1608
    • Tessaro, D.1    Pollegioni, L.2    Piubelli, L.3    D'Arrigo, P.4    Servi, S.5


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