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Volumn 55, Issue 25, 2016, Pages 3497-3503

Mutation of aryl binding pocket residues results in an unexpected activity switch in an oryza sativa tyrosine aminomutase

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; SUBSTRATES;

EID: 84976526329     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00331     Document Type: Article
Times cited : (3)

References (31)
  • 1
    • 34250824674 scopus 로고    scopus 로고
    • The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway
    • Christianson, C. V., Montavon, T. J., Van Lanen, S. G., Shen, B., and Bruner, S. D. (2007) The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway Biochemistry 46, 7205-7214 10.1021/bi7003685
    • (2007) Biochemistry , vol.46 , pp. 7205-7214
    • Christianson, C.V.1    Montavon, T.J.2    Van Lanen, S.G.3    Shen, B.4    Bruner, S.D.5
  • 2
    • 79953711463 scopus 로고    scopus 로고
    • Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase
    • Feng, L., Wanninayake, U., Strom, S., Geiger, J., and Walker, K. D. (2011) Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase Biochemistry 50, 2919-2930 10.1021/bi102067r
    • (2011) Biochemistry , vol.50 , pp. 2919-2930
    • Feng, L.1    Wanninayake, U.2    Strom, S.3    Geiger, J.4    Walker, K.D.5
  • 4
    • 84879416559 scopus 로고    scopus 로고
    • Recombinant L-phenylalanine ammonia lyase from Rhodosporidium toruloides as a potential anticancer agent
    • Babich, O. O., Pokrovsky, V. S., Anisimova, N. Y., Sokolov, N. N., and Prosekov, A. Y. (2013) Recombinant L-phenylalanine ammonia lyase from Rhodosporidium toruloides as a potential anticancer agent Biotechnol. Appl. Biochem. 60, 316-322 10.1002/bab.1089
    • (2013) Biotechnol. Appl. Biochem. , vol.60 , pp. 316-322
    • Babich, O.O.1    Pokrovsky, V.S.2    Anisimova, N.Y.3    Sokolov, N.N.4    Prosekov, A.Y.5
  • 5
    • 62149101848 scopus 로고    scopus 로고
    • Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF
    • Krug, D. and Mueller, R. (2009) Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF ChemBioChem 10, 741-750 10.1002/cbic.200800748
    • (2009) ChemBioChem , vol.10 , pp. 741-750
    • Krug, D.1    Mueller, R.2
  • 6
    • 34347376588 scopus 로고    scopus 로고
    • A modern view of phenylalanine ammonia lyase
    • (and references therein)
    • MacDonald, M. J. and D'Cunha, G. B. (2007) A modern view of phenylalanine ammonia lyase Biochem. Cell Biol. 85, 273-282 (and references therein). 10.1139/O07-018
    • (2007) Biochem. Cell Biol. , vol.85 , pp. 273-282
    • MacDonald, M.J.1    D'Cunha, G.B.2
  • 7
    • 0037070203 scopus 로고    scopus 로고
    • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein
    • Kyndt, J. A., Meyer, T. E., Cusanovich, M. A., and Van Beeumen, J. J. (2002) Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein FEBS Lett. 512, 240-244 10.1016/S0014-5793(02)02272-X
    • (2002) FEBS Lett. , vol.512 , pp. 240-244
    • Kyndt, J.A.1    Meyer, T.E.2    Cusanovich, M.A.3    Van Beeumen, J.J.4
  • 8
    • 0036223618 scopus 로고    scopus 로고
    • Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism
    • Baedeker, M. and Schulz, G. E. (2002) Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism Eur. J. Biochem. 269, 1790-1797 10.1046/j.1432-1327.2002.02827.x
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1790-1797
    • Baedeker, M.1    Schulz, G.E.2
  • 9
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede, T. F., Retey, J., and Schulz, G. E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile Biochemistry 38, 5355-5361 10.1021/bi982929q
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Retey, J.2    Schulz, G.E.3
  • 10
    • 0000338803 scopus 로고
    • Physiology and molecular biology of phenylpropanoid metabolism
    • Hahlbrock, K. and Scheel, D. (1989) Physiology and molecular biology of phenylpropanoid metabolism Annu. Rev. Plant Physiol. Plant Mol. Biol. 40, 347-369 10.1146/annurev.pp.40.060189.002023
    • (1989) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.40 , pp. 347-369
    • Hahlbrock, K.1    Scheel, D.2
  • 11
    • 35848971002 scopus 로고    scopus 로고
    • Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis
    • Van Lanen, S. G., Oh, T.-j., Liu, W., Wendt-Pienkowski, E., and Shen, B. (2007) Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis J. Am. Chem. Soc. 129, 13082-13094 10.1021/ja073275o
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 13082-13094
    • Van Lanen, S.G.1    Oh, T.-J.2    Liu, W.3    Wendt-Pienkowski, E.4    Shen, B.5
  • 12
    • 11144225850 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis
    • Walker, K. D., Klettke, K., Akiyama, T., and Croteau, R. (2004) Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in Taxol biosynthesis J. Biol. Chem. 279, 53947-53954 10.1074/jbc.M411215200
    • (2004) J. Biol. Chem. , vol.279 , pp. 53947-53954
    • Walker, K.D.1    Klettke, K.2    Akiyama, T.3    Croteau, R.4
  • 13
    • 84863519855 scopus 로고    scopus 로고
    • Assessing the deamination rate of a covalent aminomutase adduct by burst phase analysis
    • Wanninayake, U. and Walker, K. D. (2012) Assessing the deamination rate of a covalent aminomutase adduct by burst phase analysis Biochemistry 51, 5226-5228 10.1021/bi300569r
    • (2012) Biochemistry , vol.51 , pp. 5226-5228
    • Wanninayake, U.1    Walker, K.D.2
  • 14
    • 84881052336 scopus 로고    scopus 로고
    • A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction
    • Wanninayake, U. and Walker, K. D. (2013) A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction J. Am. Chem. Soc. 135, 11193-11204 10.1021/ja403918w
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 11193-11204
    • Wanninayake, U.1    Walker, K.D.2
  • 15
    • 34548259160 scopus 로고    scopus 로고
    • Unusual mechanism for an aminomutase rearrangement: Retention of configuration at the migration termini
    • Mutatu, W., Klettke, K. L., Foster, C., and Walker, K. D. (2007) Unusual mechanism for an aminomutase rearrangement: Retention of configuration at the migration termini Biochemistry 46, 9785-9794 10.1021/bi700691p
    • (2007) Biochemistry , vol.46 , pp. 9785-9794
    • Mutatu, W.1    Klettke, K.L.2    Foster, C.3    Walker, K.D.4
  • 16
    • 34250173075 scopus 로고    scopus 로고
    • β-Styryl- and β-aryl-β-alanine products of phenylalanine aminomutase catalysis
    • Klettke, K. L., Sanyal, S., Mutatu, W., and Walker, K. D. (2007) β-Styryl- and β-aryl-β-alanine products of phenylalanine aminomutase catalysis J. Am. Chem. Soc. 129, 6988-6989 10.1021/ja071328w
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6988-6989
    • Klettke, K.L.1    Sanyal, S.2    Mutatu, W.3    Walker, K.D.4
  • 17
    • 79957978699 scopus 로고    scopus 로고
    • Stereochemistry and mechanism of a microbial phenylalanine aminomutase
    • Ratnayake, N. D., Wanninayake, U., Geiger, J. H., and Walker, K. D. (2011) Stereochemistry and mechanism of a microbial phenylalanine aminomutase J. Am. Chem. Soc. 133, 8531-8533 10.1021/ja2030728
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8531-8533
    • Ratnayake, N.D.1    Wanninayake, U.2    Geiger, J.H.3    Walker, K.D.4
  • 18
    • 84877843867 scopus 로고    scopus 로고
    • A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway
    • Huang, S.-X., Lohman, J. R., Huang, T., and Shen, B. (2013) A new member of the 4-methylideneimidazole-5-one-containing aminomutase family from the enediyne kedarcidin biosynthetic pathway Proc. Natl. Acad. Sci. U. S. A. 110, 8069-8074 10.1073/pnas.1304733110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 8069-8074
    • Huang, S.-X.1    Lohman, J.R.2    Huang, T.3    Shen, B.4
  • 20
    • 84954439131 scopus 로고    scopus 로고
    • A tyrosine aminomutase from rice (Oryza sativa) isomerizes (S)-α- to (R)-β-tyrosine with unique high enantioselectivity and retention of configuration
    • Walter, T., King, Z., and Walker, K. D. (2016) A tyrosine aminomutase from rice (Oryza sativa) isomerizes (S)-α- to (R)-β-tyrosine with unique high enantioselectivity and retention of configuration Biochemistry 55, 1-4 10.1021/acs.biochem.5b01331
    • (2016) Biochemistry , vol.55 , pp. 1-4
    • Walter, T.1    King, Z.2    Walker, K.D.3
  • 21
    • 2442643102 scopus 로고    scopus 로고
    • Toxicity caused by hydroxycinnamoyl-coenzyme A thioester accumulation in mutants of Acinetobacter sp. Strain ADP1
    • Parke, D. and Ornston, L. N. (2004) Toxicity caused by hydroxycinnamoyl-coenzyme A thioester accumulation in mutants of Acinetobacter sp. strain ADP1 Appl. Environ. Microbiol. 70, 2974-2983 10.1128/AEM.70.5.2974-2983.2004
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2974-2983
    • Parke, D.1    Ornston, L.N.2
  • 22
    • 84872497791 scopus 로고    scopus 로고
    • Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice
    • Sun, H., Li, Y., Feng, S., Zou, W., Guo, K., Fan, C., Si, S., and Peng, L. (2013) Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice Biochem. Biophys. Res. Commun. 430, 1151-1156 10.1016/j.bbrc.2012.12.019
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 1151-1156
    • Sun, H.1    Li, Y.2    Feng, S.3    Zou, W.4    Guo, K.5    Fan, C.6    Si, S.7    Peng, L.8
  • 23
    • 77954628731 scopus 로고    scopus 로고
    • Probing the active site of MIO-dependent 2,3-aminomutases, key catalysts in the biosynthesis of β-amino acids incorporated in secondary metabolites
    • Bruner, S. D. and Cooke, H. A. (2010) Probing the active site of MIO-dependent 2,3-aminomutases, key catalysts in the biosynthesis of β-amino acids incorporated in secondary metabolites Biopolymers 93, 802-810 10.1002/bip.21500
    • (2010) Biopolymers , vol.93 , pp. 802-810
    • Bruner, S.D.1    Cooke, H.A.2
  • 24
    • 33845496747 scopus 로고    scopus 로고
    • Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family
    • Watts, K. T., Mijts, B. N., Lee, P. C., Manning, A. J., and Schmidt-Dannert, C. (2006) Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family Chem. Biol. 13, 1317-1326 10.1016/j.chembiol.2006.10.008
    • (2006) Chem. Biol. , vol.13 , pp. 1317-1326
    • Watts, K.T.1    Mijts, B.N.2    Lee, P.C.3    Manning, A.J.4    Schmidt-Dannert, C.5
  • 25
    • 33845482046 scopus 로고    scopus 로고
    • Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases
    • Louie, G. V., Bowman, M. E., Moffitt, M. C., Baiga, T. J., Moore, B. S., and Noel, J. P. (2006) Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases Chem. Biol. 13, 1327 10.1016/j.chembiol.2006.11.011
    • (2006) Chem. Biol. , vol.13 , pp. 1327
    • Louie, G.V.1    Bowman, M.E.2    Moffitt, M.C.3    Baiga, T.J.4    Moore, B.S.5    Noel, J.P.6
  • 26
    • 77958485266 scopus 로고    scopus 로고
    • Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase
    • Wu, B., Szymanski, W., Wijma, H. J., Crismaru, C. G., de Wildeman, S., Poelarends, G. J., Feringa, B. L., and Janssen, D. B. (2009) Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase Chem. Commun. 46, 8157-8159 10.1039/c0cc02768e
    • (2009) Chem. Commun. , vol.46 , pp. 8157-8159
    • Wu, B.1    Szymanski, W.2    Wijma, H.J.3    Crismaru, C.G.4    De Wildeman, S.5    Poelarends, G.J.6    Feringa, B.L.7    Janssen, D.B.8
  • 27
    • 70349769685 scopus 로고    scopus 로고
    • A single residue influences the reaction mechanism of ammonia lyases and mutases
    • Bartsch, S. and Bornscheuer, U. T. (2009) A single residue influences the reaction mechanism of ammonia lyases and mutases Angew. Chem., Int. Ed. 48, 3362-3365 10.1002/anie.200900337
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 3362-3365
    • Bartsch, S.1    Bornscheuer, U.T.2
  • 28
    • 84858177898 scopus 로고    scopus 로고
    • Insights into the mechanistic pathway of the Pantoea agglomerans phenylalanine aminomutase
    • Strom, S., Wanninayake, U., Ratnayake, N. D., Walker, K. D., and Geiger, J. H. (2012) Insights into the mechanistic pathway of the Pantoea agglomerans phenylalanine aminomutase Angew. Chem., Int. Ed. 51, 2898-2902 10.1002/anie.201108525
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 2898-2902
    • Strom, S.1    Wanninayake, U.2    Ratnayake, N.D.3    Walker, K.D.4    Geiger, J.H.5
  • 30
    • 84928161840 scopus 로고    scopus 로고
    • Ironing out their differences: Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase
    • Heberling, M. M., Masman, M. F., Bartsch, S., Wybenga, G. G., Dijkstra, B. W., Marrink, S. J., and Janssen, D. B. (2015) Ironing out their differences: Dissecting the structural determinants of a phenylalanine aminomutase and ammonia lyase ACS Chem. Biol. 10, 989-997 10.1021/cb500794h
    • (2015) ACS Chem. Biol. , vol.10 , pp. 989-997
    • Heberling, M.M.1    Masman, M.F.2    Bartsch, S.3    Wybenga, G.G.4    Dijkstra, B.W.5    Marrink, S.J.6    Janssen, D.B.7
  • 31
    • 84860196682 scopus 로고    scopus 로고
    • Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes
    • Chesters, C., Wilding, M., Goodall, M., and Micklefield, J. (2012) Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes Angew. Chem., Int. Ed. 51, 4344-4348 10.1002/anie.201200669
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 4344-4348
    • Chesters, C.1    Wilding, M.2    Goodall, M.3    Micklefield, J.4


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