메뉴 건너뛰기




Volumn 288, Issue 34, 2013, Pages 24441-24451

Structural and functional evolution of positively selected sites in pine glutathione S-transferase enzyme family

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL PROPERTIES; GLUTATHIONE-S-TRANSFERASE; PHYLOGENETIC ANALYSIS; PLANT STRESS TOLERANCE; SITE DIRECTED MUTAGENESIS; STRUCTURAL DIVERGENCE; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING SITES;

EID: 84883163913     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.456863     Document Type: Article
Times cited : (49)

References (51)
  • 2
    • 75649127974 scopus 로고    scopus 로고
    • Extensive functional diversification of the Populus glutathione S-transferase supergene family
    • Lan, T., Yang, Z. L., Yang, X., Liu, Y. J., Wang, X. R., and Zeng, Q. Y. (2009) Extensive functional diversification of the Populus glutathione S-transferase supergene family. Plant Cell 21, 3749-3766
    • (2009) Plant Cell , vol.21 , pp. 3749-3766
    • Lan, T.1    Yang, Z.L.2    Yang, X.3    Liu, Y.J.4    Wang, X.R.5    Zeng, Q.Y.6
  • 3
    • 64949203222 scopus 로고    scopus 로고
    • Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily
    • Dixon, D. P., Hawkins, T., Hussey, P. J., and Edwards, R. (2009) Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily. J. Exp. Bot. 60, 1207-1518
    • (2009) J. Exp. Bot. , vol.60 , pp. 1207-1518
    • Dixon, D.P.1    Hawkins, T.2    Hussey, P.J.3    Edwards, R.4
  • 4
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan, N., Gam, J., Olsen, M. J., Georgiou, G., and Iverson, B. L. (2005) Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc. Natl. Acad. Sci. U.S.A. 102, 6855-6860
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 5
    • 34548107903 scopus 로고    scopus 로고
    • Positive selection for single amino acid change promotes substrate discrimination of a plant volatile-producing enzyme
    • Barkman, T. J., Martins, T. R., Sutton, E., and Stout, J. T. (2007) Positive selection for single amino acid change promotes substrate discrimination of a plant volatile-producing enzyme. Mol. Biol. Evol. 24, 1320-1329
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1320-1329
    • Barkman, T.J.1    Martins, T.R.2    Sutton, E.3    Stout, J.T.4
  • 6
    • 77951610835 scopus 로고    scopus 로고
    • Positions under positive selection-key for selectivity and potency of scorpion α-toxins
    • Weinberger, H., Moran, Y., Gordon, D., Turkov, M., Kahn, R., and Gurevitz, M. (2010) Positions under positive selection-key for selectivity and potency of scorpion α-toxins. Mol. Biol. Evol. 27, 1025-1034
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 1025-1034
    • Weinberger, H.1    Moran, Y.2    Gordon, D.3    Turkov, M.4    Kahn, R.5    Gurevitz, M.6
  • 7
    • 35348861423 scopus 로고    scopus 로고
    • Largescale, lineage-specific expansion of a bric-A-brac/tramtrack/broad complex ubiquitin-ligase gene family in rice
    • Gingerich, D. J., Hanada, K., Shiu, S. H., and Vierstra, R. D. (2007) Largescale, lineage-specific expansion of a bric-a-brac/tramtrack/broad complex ubiquitin-ligase gene family in rice. Plant Cell 19, 2329-2348
    • (2007) Plant Cell , vol.19 , pp. 2329-2348
    • Gingerich, D.J.1    Hanada, K.2    Shiu, S.H.3    Vierstra, R.D.4
  • 8
    • 0037186564 scopus 로고    scopus 로고
    • Adaptive protein evolution in Drosophila
    • Smith, N. G., and Eyre-Walker, A. (2002) Adaptive protein evolution in Drosophila. Nature 415, 1022-1024
    • (2002) Nature , vol.415 , pp. 1022-1024
    • Smith, N.G.1    Eyre-Walker, A.2
  • 9
    • 0034625046 scopus 로고    scopus 로고
    • Rapid evolution in plant chitinases. Molecular targets of selection in plant-pathogen coevolution
    • Bishop, J. G., Dean, A. M., and Mitchell-Olds, T. (2000) Rapid evolution in plant chitinases. Molecular targets of selection in plant-pathogen coevolution. Proc. Natl. Acad. Sci. U.S.A. 97, 5322-5327
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5322-5327
    • Bishop, J.G.1    Dean, A.M.2    Mitchell-Olds, T.3
  • 10
    • 0033639150 scopus 로고    scopus 로고
    • Statistical methods for detecting molecular adaptation
    • Yang, Z., and Bielawski, J. P. (2000) Statistical methods for detecting molecular adaptation. Trends Ecol. Evol. 15, 496-503
    • (2000) Trends Ecol. Evol. , vol.15 , pp. 496-503
    • Yang, Z.1    Bielawski, J.P.2
  • 12
    • 0033768406 scopus 로고    scopus 로고
    • Glutathione and a UV light-induced glutathione S-transferase are involved in signaling to chalcone synthase in cell cultures
    • Loyall, L., Uchida, K., Braun, S., Furuya, M., and Frohnmeyer, H. (2000) Glutathione and a UV light-induced glutathione S-transferase are involved in signaling to chalcone synthase in cell cultures. Plant Cell 12, 1939-1950
    • (2000) Plant Cell , vol.12 , pp. 1939-1950
    • Loyall, L.1    Uchida, K.2    Braun, S.3    Furuya, M.4    Frohnmeyer, H.5
  • 14
    • 0033845760 scopus 로고    scopus 로고
    • AN9, a petunia glutathione S-transferase required for anthocyanin sequestration, is a flavonoid-binding protein
    • Mueller, L. A., Goodman, C. D., Silady, R. A., and Walbot, V. (2000) AN9, a petunia glutathione S-transferase required for anthocyanin sequestration, is a flavonoid-binding protein. Plant Physiol. 123, 1561-1570
    • (2000) Plant Physiol. , vol.123 , pp. 1561-1570
    • Mueller, L.A.1    Goodman, C.D.2    Silady, R.A.3    Walbot, V.4
  • 15
    • 0036892782 scopus 로고    scopus 로고
    • A pathogen-induced novel rice (Oryza sativa L.) gene encodes a putative protein homologous to type II glutathione S-transferases
    • Agrawal, G. K., Jwa, N. S., and Rakwal, R. (2002) A pathogen-induced novel rice (Oryza sativa L.) gene encodes a putative protein homologous to type II glutathione S-transferases. Plant Sci. 163, 1153-1160
    • (2002) Plant Sci. , vol.163 , pp. 1153-1160
    • Agrawal, G.K.1    Jwa, N.S.2    Rakwal, R.3
  • 16
    • 79953002942 scopus 로고    scopus 로고
    • Distinct niche divergence characterizes the homoploid hybrid speciation of Pinus densata on the Tibetan plateau
    • Mao, J. F., and Wang, X. R. (2011) Distinct niche divergence characterizes the homoploid hybrid speciation of Pinus densata on the Tibetan plateau. Am. Nat. 177, 424-439
    • (2011) Am. Nat. , vol.177 , pp. 424-439
    • Mao, J.F.1    Wang, X.R.2
  • 17
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione Stransferases. Enzymes with multiple functions in sickness and in health
    • Edwards, R., Dixon, D. P., and Walbot, V. (2000) Plant glutathione Stransferases. Enzymes with multiple functions in sickness and in health. Trends Plant Sci. 5, 193-198
    • (2000) Trends Plant Sci. , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 18
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE. Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE. Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 19
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41, 95-98
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 20
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon, S., and Gascuel, O. (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52, 696-704
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 21
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4. Phylogenetic analysis by maximum likelihood
    • Yang, Z. (2007) PAML 4. Phylogenetic analysis by maximum likelihood. Mol. Biol. Evol. 24, 1586-1591
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1586-1591
    • Yang, Z.1
  • 22
    • 0033979433 scopus 로고    scopus 로고
    • Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models
    • Yang, Z., and Nielsen, R. (2000) Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models. Mol. Biol. Evol. 17, 32-43
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 32-43
    • Yang, Z.1    Nielsen, R.2
  • 23
    • 16344378246 scopus 로고    scopus 로고
    • Bayes empirical bayes inference of amino acid sites under positive selection
    • Yang, Z., Wong, W. S., and Nielsen, R. (2005) Bayes empirical bayes inference of amino acid sites under positive selection. Mol. Biol. Evol. 22, 1107-1118
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1107-1118
    • Yang, Z.1    Wong, W.S.2    Nielsen, R.3
  • 24
    • 18144362132 scopus 로고    scopus 로고
    • Catalytic properties of glutathionebinding residues in a Tau class glutathione transferase (PtGSTU1) from Pinus tabulaeformis
    • Zeng, Q. Y., and Wang, X. R. (2005) Catalytic properties of glutathionebinding residues in a Tau class glutathione transferase (PtGSTU1) from Pinus tabulaeformis. FEBS Lett. 579, 2657-2662
    • (2005) FEBS Lett. , vol.579 , pp. 2657-2662
    • Zeng, Q.Y.1    Wang, X.R.2
  • 25
    • 16844373619 scopus 로고    scopus 로고
    • Molecular characterization of a glutathione transferase from Pinus tabulaeformis (Pinaceae)
    • Zeng, Q. Y., Lu, H., and Wang, X. R. (2005) Molecular characterization of a glutathione transferase from Pinus tabulaeformis (Pinaceae). Biochimie 87, 445-455
    • (2005) Biochimie , vol.87 , pp. 445-455
    • Zeng, Q.Y.1    Lu, H.2    Wang, X.R.3
  • 26
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig, W. H., Pabst, M. J., and Jakoby, W. B. (1974) glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 27
    • 0028262418 scopus 로고
    • Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
    • Ricci, G., Caccuri, A. M., Lo Bello, M., Pastore, A., Piemonte, F., and Federici, G. (1994) Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Anal. Biochem. 218, 463-465
    • (1994) Anal. Biochem. , vol.218 , pp. 463-465
    • Ricci, G.1    Caccuri, A.M.2    Lo Bello, M.3    Pastore, A.4    Piemonte, F.5    Federici, G.6
  • 28
    • 30144437159 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • Edwards, R., and Dixon, D. P. (2005) Plant glutathione transferases. Methods Enzymol. 401, 169-186
    • (2005) Methods Enzymol. , vol.401 , pp. 169-186
    • Edwards, R.1    Dixon, D.P.2
  • 29
    • 0034612339 scopus 로고    scopus 로고
    • Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA
    • Schonbrunn, E., Eschenburg, S., Luger, K., Kabsch, W., and Amrhein, N. (2000) Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc. Natl. Acad. Sci. U.S.A. 97, 6345-6349
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6345-6349
    • Schonbrunn, E.1    Eschenburg, S.2    Luger, K.3    Kabsch, W.4    Amrhein, N.5
  • 30
    • 84873245497 scopus 로고    scopus 로고
    • Functional divergence of the GST supergene family in Physcomitrella patens reveals complex patterns of large gene family evolution in land plants
    • Liu, Y. J., Han, X. M., Ren, L. L., Yang, H. L., and Zeng, Q. Y. (2013) Functional divergence of the GST supergene family in Physcomitrella patens reveals complex patterns of large gene family evolution in land plants. Plant Physiol. 161, 773-786
    • (2013) Plant Physiol. , vol.161 , pp. 773-786
    • Liu, Y.J.1    Han, X.M.2    Ren, L.L.3    Yang, H.L.4    Zeng, Q.Y.5
  • 31
    • 3142677326 scopus 로고    scopus 로고
    • Organisation and structural evolution of the rice glutathione S-transferase gene family
    • Soranzo, N., Sari Gorla, M., Mizzi, L., De Toma, G., and Frova, C. (2004) Organisation and structural evolution of the rice glutathione S-transferase gene family. Mol. Genet. Genomics 271, 511-521
    • (2004) Mol. Genet. Genomics , vol.271 , pp. 511-521
    • Soranzo, N.1    Sari Gorla, M.2    Mizzi, L.3    De Toma, G.4    Frova, C.5
  • 33
    • 27844439855 scopus 로고    scopus 로고
    • Evaluation of an improved branch-site likelihood method for detecting positive selection at the molecular level
    • Zhang, J., Nielsen, R., and Yang, Z. (2005) Evaluation of an improved branch-site likelihood method for detecting positive selection at the molecular level. Mol. Biol. Evol. 22, 2472-2479
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2472-2479
    • Zhang, J.1    Nielsen, R.2    Yang, Z.3
  • 34
    • 27844526579 scopus 로고    scopus 로고
    • Gene conversion and the evolution of three leucine-rich repeat gene families in Arabidopsis thaliana
    • Mondragon-Palomino, M., and Gaut, B. S. (2005) Gene conversion and the evolution of three leucine-rich repeat gene families in Arabidopsis thaliana. Mol. Biol. Evol. 22, 2444-2456
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2444-2456
    • Mondragon-Palomino, M.1    Gaut, B.S.2
  • 35
    • 0024356449 scopus 로고
    • Statistical tests for detecting gene conversion
    • Sawyer, S. (1989) Statistical tests for detecting gene conversion. Mol. Biol. Evol. 6, 526-538
    • (1989) Mol. Biol. Evol. , vol.6 , pp. 526-538
    • Sawyer, S.1
  • 36
    • 77957243284 scopus 로고    scopus 로고
    • RDP3. A flexible and fast computer program for analyzing recombination
    • Martin, D. P., Lemey, P., Lott, M., Moulton, V., Posada, D., and Lefeuvre, P. (2010) RDP3. A flexible and fast computer program for analyzing recombination. Bioinformatics 26, 2462-2463
    • (2010) Bioinformatics , vol.26 , pp. 2462-2463
    • Martin, D.P.1    Lemey, P.2    Lott, M.3    Moulton, V.4    Posada, D.5    Lefeuvre, P.6
  • 37
    • 0345255239 scopus 로고    scopus 로고
    • Adaptive evolution in the Arabidopsis MADS-box gene family inferred from its complete resolved phylogeny
    • Martinez-Castilla, L. P., and Alvarez-Buylla, E. R. (2003) Adaptive evolution in the Arabidopsis MADS-box gene family inferred from its complete resolved phylogeny. Proc. Natl. Acad. Sci. U.S.A. 100, 13407-13412
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13407-13412
    • Martinez-Castilla, L.P.1    Alvarez-Buylla, E.R.2
  • 38
    • 84874635344 scopus 로고    scopus 로고
    • Rapid birth-and-death evolution of the xenobiotic metabolizing NAT gene family in vertebrates with evidence of adaptive selection
    • Sabbagh, A., Marin, J., Veyssière, C., Lecompte, E., Boukouvala, S., Poloni, E. S., Darlu, P., and Crouau-Roy, B. (2013) Rapid birth-and-death evolution of the xenobiotic metabolizing NAT gene family in vertebrates with evidence of adaptive selection. BMC Evol. Biol. 13, 62
    • (2013) BMC Evol. Biol. , vol.13 , pp. 62
    • Sabbagh, A.1    Marin, J.2    Veyssière, C.3    Lecompte, E.4    Boukouvala, S.5    Poloni, E.S.6    Darlu, P.7    Crouau-Roy, B.8
  • 39
    • 33646178621 scopus 로고    scopus 로고
    • Designed divergent evolution of enzyme function
    • Yoshikuni, Y., Ferrin, T. E., and Keasling, J. D. (2006) Designed divergent evolution of enzyme function. Nature 440, 1078-1082
    • (2006) Nature , vol.440 , pp. 1078-1082
    • Yoshikuni, Y.1    Ferrin, T.E.2    Keasling, J.D.3
  • 40
    • 9244247603 scopus 로고    scopus 로고
    • Evolving protein functional diversity in new genes of Drosophila
    • Zhang, J., Dean, A. M., Brunet, F., and Long, M. (2004) Evolving protein functional diversity in new genes of Drosophila. Proc. Natl. Acad. Sci. U.S.A. 101, 16246-16250
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16246-16250
    • Zhang, J.1    Dean, A.M.2    Brunet, F.3    Long, M.4
  • 41
    • 0029557251 scopus 로고
    • A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity
    • Chen, R., Greer, A., and Dean, A. M. (1995) A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity. Proc. Natl. Acad. Sci. U.S.A. 92, 11666-11670
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11666-11670
    • Chen, R.1    Greer, A.2    Dean, A.M.3
  • 42
    • 0344237276 scopus 로고    scopus 로고
    • The plant glutathione transferase gene family: Genomic structure, functions, expression and evolution
    • Frova, C. (2003) The plant glutathione transferase gene family: genomic structure, functions, expression and evolution. Physiol. Plant 119, 469-479
    • (2003) Physiol. Plant , vol.119 , pp. 469-479
    • Frova, C.1
  • 43
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a Tau class glutathione S-transferase from wheat active in herbicide detoxification
    • Thom, R., Cummins, I., Dixon, D. P., Edwards, R., Cole, D. J., and Lapthorn, A. J. (2002) Structure of a Tau class glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry 41, 7008-7020
    • (2002) Biochemistry , vol.41 , pp. 7008-7020
    • Thom, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 44
    • 58149203984 scopus 로고    scopus 로고
    • Crystallographic and functional characterization of the fluorodifen-inducible glutathione transferase from Glycine max reveals an active site topography suited for diphenylether herbicides and a novel L-site
    • Axarli, I., Dhavala, P., Papageorgiou, A. C., and Labrou, N. E. (2009) Crystallographic and functional characterization of the fluorodifen-inducible glutathione transferase from Glycine max reveals an active site topography suited for diphenylether herbicides and a novel L-site. J. Mol. Biol. 385, 984-1002
    • (2009) J. Mol. Biol. , vol.385 , pp. 984-1002
    • Axarli, I.1    Dhavala, P.2    Papageorgiou, A.C.3    Labrou, N.E.4
  • 45
    • 71849104828 scopus 로고    scopus 로고
    • Biochemical and physiological characterization of a Tau class glutathione transferase from rice (Oryza sativa)
    • Yang, X., Sun, W., Liu, J. P., Liu, Y. J., and Zeng, Q. Y. (2009) Biochemical and physiological characterization of a Tau class glutathione transferase from rice (Oryza sativa). Plant Physiol. Biochem. 47, 1061-1068
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 1061-1068
    • Yang, X.1    Sun, W.2    Liu, J.P.3    Liu, Y.J.4    Zeng, Q.Y.5
  • 46
    • 0037424257 scopus 로고    scopus 로고
    • Identification of residues in glutathione transferase capable of driving functional diversification in evolution-A novel approach to protein redesign
    • Ivarsson, Y., Mackey, A. J., Edalat, M., Pearson, W. R., and Mannervik, B. (2003) Identification of residues in glutathione transferase capable of driving functional diversification in evolution-A novel approach to protein redesign. J. Biol. Chem. 278, 8733-8738
    • (2003) J. Biol. Chem. , vol.278 , pp. 8733-8738
    • Ivarsson, Y.1    MacKey, A.J.2    Edalat, M.3    Pearson, W.R.4    Mannervik, B.5
  • 47
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties. When are closer mutations better?
    • Morley, K. L., and Kazlauskas, R. J. (2005) Improving enzyme properties. When are closer mutations better? Trends Biotechnol. 23, 231-237
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 48
    • 65349190709 scopus 로고    scopus 로고
    • The effect of sequence evolution on protein structural divergence
    • Williams, S. G., and Lovell, S. C. (2009) The effect of sequence evolution on protein structural divergence. Mol. Biol. Evol. 26, 1055-1065
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 1055-1065
    • Williams, S.G.1    Lovell, S.C.2
  • 49
    • 0023488997 scopus 로고
    • Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes. Eleventh Keilin memorial lecture
    • Huber, R. (1987) Flexibility and rigidity, requirements for the function of proteins and protein pigment complexes. Eleventh Keilin memorial lecture. Biochem. Soc. Trans. 15, 1009-1020
    • (1987) Biochem. Soc. Trans. , vol.15 , pp. 1009-1020
    • Huber, R.1
  • 50
    • 77956021391 scopus 로고    scopus 로고
    • Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions
    • Padhi, S. K., Fujii, R., Legatt, G. A., Fossum, S. L., Berchtold, R., and Kazlauskas, R. J. (2010) Switching from an esterase to a hydroxynitrile lyase mechanism requires only two amino acid substitutions. Chem. Biol. 17, 863-871
    • (2010) Chem. Biol. , vol.17 , pp. 863-871
    • Padhi, S.K.1    Fujii, R.2    Legatt, G.A.3    Fossum, S.L.4    Berchtold, R.5    Kazlauskas, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.