메뉴 건너뛰기




Volumn 11, Issue 1, 2016, Pages

Kinetic characterization of 100 glycoside hydrolase mutants enables the discovery of structural features correlated with kinetic constants

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME VARIANT; GLYCOSIDASE; MUTANT PROTEIN;

EID: 84958231511     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0147596     Document Type: Article
Times cited : (35)

References (26)
  • 1
    • 84903827354 scopus 로고    scopus 로고
    • Computational enzyme design: Transitioning from catalytic proteins to enzymes
    • 25005925
    • Mak WS, Siegel JB (2014) Computational enzyme design: Transitioning from catalytic proteins to enzymes. Current opinion in structural biology 27:87-94. doi: 10.1016/j.sbi.2014.05.010 PMID: 25005925
    • (2014) Current Opinion in Structural Biology , vol.27 , pp. 87-94
    • Mak, W.S.1    Siegel, J.B.2
  • 3
    • 84891421517 scopus 로고    scopus 로고
    • Computational tools for designing and engineering enzymes
    • 24780274
    • Damborsky J, Brezovsky J (2014) Computational tools for designing and engineering enzymes. Current Opinion in Chemical Biology 19:8-16. doi: 10.1016/j.cbpa.2013.12.003 PMID: 24780274
    • (2014) Current Opinion in Chemical Biology , vol.19 , pp. 8-16
    • Damborsky, J.1    Brezovsky, J.2
  • 5
    • 84860211608 scopus 로고    scopus 로고
    • A Synthetic Recursive "+1" Pathway for Carbon Chain Elongation
    • 22242720
    • Marcheschi RJ, Li H, Zhang K, Noey EL, Kim S, et al. (2012) A Synthetic Recursive "+1" Pathway for Carbon Chain Elongation. ACS Chemical Biology 7:689-697. doi: 10.1021/cb200313e PMID: 22242720
    • (2012) ACS Chemical Biology , vol.7 , pp. 689-697
    • Marcheschi, R.J.1    Li, H.2    Zhang, K.3    Noey, E.L.4    Kim, S.5
  • 6
    • 84862776507 scopus 로고    scopus 로고
    • Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis
    • 22306579
    • Khare SD, Kipnis Y, Greisen P Jr., Takeuchi R, Ashani Y, et al. (2012) Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis. Nat Chem Biol 8:294-300. doi: 10. 1038/nchembio.777 PMID: 22306579
    • (2012) Nat Chem Biol , vol.8 , pp. 294-300
    • Khare, S.D.1    Kipnis, Y.2    Greisen, P.3    Takeuchi, R.4    Ashani, Y.5
  • 7
    • 33644874615 scopus 로고    scopus 로고
    • ProTherm and ProNIT: Thermodynamic databases for proteins and protein-nucleic acid interactions
    • 16381846
    • Kumar MS, Bava KA, Gromiha MM, Prabakaran P, Kitajima K, et al. (2006) ProTherm and ProNIT: thermodynamic databases for proteins and protein-nucleic acid interactions. Nucleic Acids Research 34:D204-D206. PMID: 16381846
    • (2006) Nucleic Acids Research , vol.34 , pp. D204-D206
    • Kumar, M.S.1    Bava, K.A.2    Gromiha, M.M.3    Prabakaran, P.4    Kitajima, K.5
  • 8
    • 79551470095 scopus 로고    scopus 로고
    • Role of conformational sampling in computing mutation-induced changes in protein structure and stability
    • Kellogg EH, Leaver-Fay A, Baker D (2011) Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins: Structure, Function, and Bioinformatics 79:830-838.
    • (2011) Proteins: Structure, Function, and Bioinformatics , vol.79 , pp. 830-838
    • Kellogg, E.H.1    Leaver-Fay, A.2    Baker, D.3
  • 9
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • 12079393
    • Guerois R, Nielsen JE, Serrano L (2002) Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. Journal of molecular biology 320:369-387. PMID: 12079393
    • (2002) Journal of Molecular Biology , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 11
    • 84921266847 scopus 로고    scopus 로고
    • Mapping of amino acid substitutions conferring herbicide resistance in wheat glutathione transferase
    • 24905764
    • Govindarajan S, Mannervik B, Silverman JA, Wright K, Regitsky D, et al. (2014) Mapping of amino acid substitutions conferring herbicide resistance in wheat glutathione transferase. ACS synthetic biology 4:221-227. doi: 10.1021/sb500242x PMID: 24905764
    • (2014) ACS Synthetic Biology , vol.4 , pp. 221-227
    • Govindarajan, S.1    Mannervik, B.2    Silverman, J.A.3    Wright, K.4    Regitsky, D.5
  • 14
    • 84923321398 scopus 로고    scopus 로고
    • Evolvability as a Function of Purifying Selection in TEM-1 β-Lactamase
    • 25723163
    • Stiffler MA, Hekstra DR, Ranganathan R (2015) Evolvability as a Function of Purifying Selection in TEM-1 β-Lactamase. Cell 160:882-892. doi: 10.1016/j.cell.2015.01.035 PMID: 25723163
    • (2015) Cell , vol.160 , pp. 882-892
    • Stiffler, M.A.1    Hekstra, D.R.2    Ranganathan, R.3
  • 15
    • 34547597634 scopus 로고    scopus 로고
    • Crystal Structures of Paenibacillus polymyxa β-Glucosidase B Complexes Reveal the Molecular Basis of Substrate Specificity and Give New Insights into the Catalytic Machinery of Family I Glycosidases
    • 17585934
    • Isorna P, Polaina J, Latorre-Garcia L, Canada FJ, Gonzalez B, et al. (2007) Crystal Structures of Paenibacillus polymyxa β-Glucosidase B Complexes Reveal the Molecular Basis of Substrate Specificity and Give New Insights into the Catalytic Machinery of Family I Glycosidases. Journal of Molecular Biology 371:1204-1218. PMID: 17585934
    • (2007) Journal of Molecular Biology , vol.371 , pp. 1204-1218
    • Isorna, P.1    Polaina, J.2    Latorre-Garcia, L.3    Canada, F.J.4    Gonzalez, B.5
  • 18
    • 80052723466 scopus 로고    scopus 로고
    • Improvement of a potential anthrax therapeutic by computational protein design
    • 21768086
    • Wu SJ, Eiben CB, Carra JH, Huang I, Zong D, et al. (2011) Improvement of a potential anthrax therapeutic by computational protein design. Journal of Biological Chemistry 286:32586-32592. doi: 10. 1074/jbc. M111.251041 PMID: 21768086
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 32586-32592
    • Wu, S.J.1    Eiben, C.B.2    Carra, J.H.3    Huang, I.4    Zong, D.5
  • 19
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proceedings of the National Academy of Sciences 82:488-492.
    • (1985) Proceedings of the National Academy of Sciences , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 22
    • 0028609166 scopus 로고
    • Mechanisms of enzymatic glycoside hydrolysis
    • 7712292
    • McCarter JD, Withers SG (1994) Mechanisms of enzymatic glycoside hydrolysis. Curr Opin Struct Biol 4:885-892. PMID: 7712292
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 885-892
    • McCarter, J.D.1    Withers, S.G.2
  • 23
    • 0030879888 scopus 로고    scopus 로고
    • Orbital steering in the catalytic power of enzymes: Small structural changes with large catalytic consequences
    • 9211842
    • Mesecar AD, Stoddard BL, Koshland DE Jr., (1997) Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences. Science 277:202-206. PMID: 9211842
    • (1997) Science , vol.277 , pp. 202-206
    • Mesecar, A.D.1    Stoddard, B.L.2    Koshland, D.E.3
  • 24
    • 84929156528 scopus 로고    scopus 로고
    • Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site
    • Sunden F, Peck A, Salzman J, Ressl S, Herschlag D (2015) Extensive site-directed mutagenesis reveals interconnected functional units in the alkaline phosphatase active site. eLife 4.
    • (2015) ELife , vol.4
    • Sunden, F.1    Peck, A.2    Salzman, J.3    Ressl, S.4    Herschlag, D.5
  • 25
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • 19363495
    • Gibson DG, Young L, Chuang R-Y, Venter JC, Hutchison CA, et al. (2009) Enzymatic assembly of DNA molecules up to several hundred kilobases. Nature methods 6:343-345. doi: 10.1038/nmeth.1318 PMID: 19363495
    • (2009) Nature Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1    Young, L.2    Chuang, R.-Y.3    Venter, J.C.4    Hutchison, C.A.5
  • 26
    • 79956088540 scopus 로고    scopus 로고
    • De novo enzyme design using Rosetta3
    • 21603656
    • Richter F, Leaver-Fay A, Khare SD, Bjelic S, Baker D (2011) De novo enzyme design using Rosetta3. PLoS One 6:e19230. doi: 10.1371/journal.pone.0019230 PMID: 21603656
    • (2011) PLoS One , vol.6 , pp. e19230
    • Richter, F.1    Leaver-Fay, A.2    Khare, S.D.3    Bjelic, S.4    Baker, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.