메뉴 건너뛰기




Volumn 177, Issue 2, 2012, Pages 392-401

Structural basis of specificity in tetrameric Kluyveromyces lactis β-galactosidase

Author keywords

Galactosidase; Biotechnology; Kluyveromyces lactis; Lactase; X ray crystal structure

Indexed keywords

BETA GALACTOSIDASE; FUNGAL ENZYME; GALACTOSE; MONOMER; TETRAMER;

EID: 84857033927     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.11.031     Document Type: Article
Times cited : (88)

References (43)
  • 1
    • 0031922937 scopus 로고    scopus 로고
    • Micro-scale purification of β-galactosidase from Kluyveromyces lactis reveals that dimeric and tetrameric forms are active
    • Becerra M., Cerdán M.E., González-Siso M.I. Micro-scale purification of β-galactosidase from Kluyveromyces lactis reveals that dimeric and tetrameric forms are active. Biotechnol. Tech. 1998, 12:253-256.
    • (1998) Biotechnol. Tech. , vol.12 , pp. 253-256
    • Becerra, M.1    Cerdán, M.E.2    González-Siso, M.I.3
  • 3
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics
    • Cantarel B., Coutinho P., Rancurel C., Bernard T., Lombard, et al. The Carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 2009, 37:D233-238.
    • (2009) Nucleic Acids Res. , vol.37
    • Cantarel, B.1    Coutinho, P.2    Rancurel, C.3    Bernard, T.4    Lombard5
  • 5
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D. Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. Sect. D: Biol. Crystallogr. 2006, 62:1002-1011.
    • (2006) Acta Crystallogr. Sect. D: Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 7
    • 3142734091 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, USA, 40
    • DeLano W.L. Pymol: An open-source molecular graphics tool 2002, The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, USA, 40.
    • (2002) Pymol: An open-source molecular graphics tool
    • DeLano, W.L.1
  • 8
    • 78649261616 scopus 로고    scopus 로고
    • Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase Escherichia coli
    • Dugdale M.L., Dymianiw D.L., Minhas B.K., D'Angelo I., Huber R.E. Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase Escherichia coli. Biochem. Cell Biol. 2010, 88:861-869.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 861-869
    • Dugdale, M.L.1    Dymianiw, D.L.2    Minhas, B.K.3    D'Angelo, I.4    Huber, R.E.5
  • 11
    • 44549084060 scopus 로고    scopus 로고
    • Lactose: crystallization, hydrolysis and value-added derivatives
    • Ganzle M., Haase G. Lactose: crystallization, hydrolysis and value-added derivatives. Int. Dairy J. 2008.
    • (2008) Int. Dairy J.
    • Ganzle, M.1    Haase, G.2
  • 12
    • 76749088556 scopus 로고    scopus 로고
    • Recent advances refining galactooligosaccharide production from lactose
    • Gosling A., Stevens G., Barber A., Kentish S. Recent advances refining galactooligosaccharide production from lactose. Food Chem. 2010, 121:307-318.
    • (2010) Food Chem. , vol.121 , pp. 307-318
    • Gosling, A.1    Stevens, G.2    Barber, A.3    Kentish, S.4
  • 13
    • 77949567900 scopus 로고    scopus 로고
    • Fermentation of lactose to bio-ethanol by yeasts as part of integrated solutions for the valorisation of cheese whey
    • Guimarães P.M.R., Teixeira J.A., Domingues L. Fermentation of lactose to bio-ethanol by yeasts as part of integrated solutions for the valorisation of cheese whey. Biotech. Adv. 2010, 28:375-384.
    • (2010) Biotech. Adv. , vol.28 , pp. 375-384
    • Guimarães, P.M.R.1    Teixeira, J.A.2    Domingues, L.3
  • 15
    • 0036968554 scopus 로고    scopus 로고
    • Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus thermophilus a4 and the structure of its complex with galactose
    • Hidaka M., Fushinobu S., Ohtsu N., Motoshima H., Matsuzawa H., et al. Trimeric crystal structure of the glycoside hydrolase family 42 β-galactosidase from Thermus thermophilus a4 and the structure of its complex with galactose. J. Mol. Biol. 2002, 322:79-91.
    • (2002) J. Mol. Biol. , vol.322 , pp. 79-91
    • Hidaka, M.1    Fushinobu, S.2    Ohtsu, N.3    Motoshima, H.4    Matsuzawa, H.5
  • 16
    • 0037452499 scopus 로고    scopus 로고
    • Trp-999 of β-galactosidase (Escherichia coli) is a key residue for binding, catalysis and synthesis of allolactose, the natural lac operon inducer
    • Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A. Trp-999 of β-galactosidase (Escherichia coli) is a key residue for binding, catalysis and synthesis of allolactose, the natural lac operon inducer. Biochem. 2003, 42:1796-1803.
    • (2003) Biochem. , vol.42 , pp. 1796-1803
    • Huber, R.E.1    Hakda, S.2    Cheng, C.3    Cupples, C.G.4    Edwards, R.A.5
  • 17
    • 76749169409 scopus 로고    scopus 로고
    • Beta galactosidases and their potential applications: a review
    • Husain Q. Beta galactosidases and their potential applications: a review. Crit. Rev. Biotechnol. 2010, 30:41-62.
    • (2010) Crit. Rev. Biotechnol. , vol.30 , pp. 41-62
    • Husain, Q.1
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 1991, 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 79251595403 scopus 로고    scopus 로고
    • Cloning, purification and characterization of β-galactosidase from Bacillus licheniformis DSM 13
    • Juajun O., Nguyen T.H., Maischberger T., Iqbal S., Haltrich D., et al. Cloning, purification and characterization of β-galactosidase from Bacillus licheniformis DSM 13. Appl. Microbiol. Biotechnol. 2011, 89:645-654.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 645-654
    • Juajun, O.1    Nguyen, T.H.2    Maischberger, T.3    Iqbal, S.4    Haltrich, D.5
  • 20
    • 0033820067 scopus 로고    scopus 로고
    • High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation
    • Juers D.H., Jacobson R., Wigley D., Zhang X., Huber R.E., et al. High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation. Protein Sci. 2000, 9:1685-1699.
    • (2000) Protein Sci. , vol.9 , pp. 1685-1699
    • Juers, D.H.1    Jacobson, R.2    Wigley, D.3    Zhang, X.4    Huber, R.E.5
  • 21
    • 0035846526 scopus 로고    scopus 로고
    • A structural view of the action of Escherichia coli (lacZ) β-galactosidase
    • Juers D.H., Heightman T., Vasella A., McCarter J., Mackenzie L., et al. A structural view of the action of Escherichia coli (lacZ) β-galactosidase. Biochem. 2001, 40:14781-14794.
    • (2001) Biochem. , vol.40 , pp. 14781-14794
    • Juers, D.H.1    Heightman, T.2    Vasella, A.3    McCarter, J.4    Mackenzie, L.5
  • 22
    • 0344391955 scopus 로고    scopus 로고
    • Structural basis for the altered activity of Gly794 variants of Escherichia coli β-galactosidase
    • Juers D.H., Hakda S., Matthews B.W., Huber R.E. Structural basis for the altered activity of Gly794 variants of Escherichia coli β-galactosidase. Biochem. 2003, 42:13505-13511.
    • (2003) Biochem. , vol.42 , pp. 13505-13511
    • Juers, D.H.1    Hakda, S.2    Matthews, B.W.3    Huber, R.E.4
  • 23
    • 66349103352 scopus 로고    scopus 로고
    • Direct and indirect roles of His-418 in metal binding and in the activity of β-galactosidase (E. Coli)
    • Juers D.H., Rob B., Dugdale M.L., Rahimzadeh N., Giang C., et al. Direct and indirect roles of His-418 in metal binding and in the activity of β-galactosidase (E. Coli). Protein Sci. 2009, 18:1281-1292.
    • (2009) Protein Sci. , vol.18 , pp. 1281-1292
    • Juers, D.H.1    Rob, B.2    Dugdale, M.L.3    Rahimzadeh, N.4    Giang, C.5
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography
    • Leslie, A., 1992. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography 26, 27-33.
    • (1992) , vol.26 , pp. 27-33
    • Leslie, A.1
  • 28
    • 79952445041 scopus 로고    scopus 로고
    • Crystal structures of Trichoderma reesei β-galactosidase reveal conformational changes in the active site
    • Maksimainen M., Hakulinen N., Kallio J.M., Timoharju T., Turunen O., et al. Crystal structures of Trichoderma reesei β-galactosidase reveal conformational changes in the active site. J. Struct. Biol. 2011, 174:156-163.
    • (2011) J. Struct. Biol. , vol.174 , pp. 156-163
    • Maksimainen, M.1    Hakulinen, N.2    Kallio, J.M.3    Timoharju, T.4    Turunen, O.5
  • 29
    • 35548990133 scopus 로고    scopus 로고
    • Optimization of conditions for galactooligosaccharide synthesis during lactose hydrolysis by β-galactosidase from Kluyveromyces lactis (Lactozym 3000 L HP G)
    • Martínez-Villaluenga C., Cardelle-Cobas A., Corzo N., Olano A., Villamiel M. Optimization of conditions for galactooligosaccharide synthesis during lactose hydrolysis by β-galactosidase from Kluyveromyces lactis (Lactozym 3000 L HP G). Food Chem. 2008, 107:258-264.
    • (2008) Food Chem. , vol.107 , pp. 258-264
    • Martínez-Villaluenga, C.1    Cardelle-Cobas, A.2    Corzo, N.3    Olano, A.4    Villamiel, M.5
  • 31
    • 80053439614 scopus 로고    scopus 로고
    • Recombinant microbial systems for improved β-galactosidase production and biotechnological applications
    • (in press).
    • Oliveira, C., Guimarães, P.M.R., Domingues, L., 2011. Recombinant microbial systems for improved β-galactosidase production and biotechnological applications. Biotechnol. Adv. (in press).
    • (2011) Biotechnol. Adv.
    • Oliveira, C.1    Guimarães, P.M.R.2    Domingues, L.3
  • 32
    • 76649107887 scopus 로고    scopus 로고
    • Galacto-oligosaccharide production using microbial β-galactosidase: current state and perspectives
    • Park A.R., Oh D.K. Galacto-oligosaccharide production using microbial β-galactosidase: current state and perspectives. Appl. Microbiol. Biotechnol. 2010, 85:1279-1286.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1279-1286
    • Park, A.R.1    Oh, D.K.2
  • 36
    • 6344266960 scopus 로고    scopus 로고
    • Crystal Structures of β-galactosidase from Penicillium sp. and its complex with galactose
    • Rojas A., Nagem R., Neustroev K., Arand M., Adamska M., et al. Crystal Structures of β-galactosidase from Penicillium sp. and its complex with galactose. J. Mol. Biol. 2004, 343:1281-1292.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1281-1292
    • Rojas, A.1    Nagem, R.2    Neustroev, K.3    Arand, M.4    Adamska, M.5
  • 37
    • 17544376273 scopus 로고    scopus 로고
    • The β-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose
    • Roth N.J., Huber R.E. The β-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose. J. Biol. Chem. 1996, 271:14296-14301.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14296-14301
    • Roth, N.J.1    Huber, R.E.2
  • 38
    • 0032516464 scopus 로고    scopus 로고
    • His-357 of β-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis
    • Roth N.J., Rob B., Huber R.E. His-357 of β-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis. Biochem. 1998, 37:10099-10107.
    • (1998) Biochem. , vol.37 , pp. 10099-10107
    • Roth, N.J.1    Rob, B.2    Huber, R.E.3
  • 39
    • 31644451519 scopus 로고    scopus 로고
    • Endless versatility in the biotechnological applications of Kluyveromyces LAC genes
    • Rubio-Texeira M. Endless versatility in the biotechnological applications of Kluyveromyces LAC genes. Biotechnol. Adv. 2006, 24:212-225.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 212-225
    • Rubio-Texeira, M.1
  • 40
    • 25144447229 scopus 로고    scopus 로고
    • Cold-active β-galactosidase from Arthrobacter sp. c2-2 forms compact 660kda hexamers: crystal structure at 1.9Ǻ resolution
    • Skálová T., Dohnálek J., Spiwok V., Lipovová P., Vondráčková E., et al. Cold-active β-galactosidase from Arthrobacter sp. c2-2 forms compact 660kda hexamers: crystal structure at 1.9Ǻ resolution. J. Mol. Biol 2005, 353:282-294.
    • (2005) J. Mol. Biol , vol.353 , pp. 282-294
    • Skálová, T.1    Dohnálek, J.2    Spiwok, V.3    Lipovová, P.4    Vondráčková, E.5
  • 41
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
    • Stein N. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J. Appl. Crystallogr. 2008, 41:641-643.
    • (2008) J. Appl. Crystallogr. , vol.41 , pp. 641-643
    • Stein, N.1
  • 42
    • 0026117693 scopus 로고
    • Applications of the steak seeding technique in protein crystallization
    • Stura E.A., Wilson I.A. Applications of the steak seeding technique in protein crystallization. J. Cryst. Growth 1991, 110:271-282.
    • (1991) J. Cryst. Growth , vol.110 , pp. 271-282
    • Stura, E.A.1    Wilson, I.A.2
  • 43
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A.A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.