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Volumn 3, Issue , 2013, Pages 467-472

Asparagine 42 of the conserved endo-inulinase INU2 motif WMNDPN from Aspergillus ficuum plays a role in activity specificity

Author keywords

Activity modification; Endo inuinase; N42G mutant; Site directed mutagenesis

Indexed keywords

ASPARAGINE; ASPARAGINE 42; ENDOINULINASE INU2; INULINASE; UNCLASSIFIED DRUG;

EID: 84887395683     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2013.10.009     Document Type: Article
Times cited : (14)

References (25)
  • 1
    • 59449083826 scopus 로고    scopus 로고
    • Inulinase-expressing microorganisms and applications of inulinases
    • Chi Z., Chi Z., Zhang T., Liu G., Yue L. Inulinase-expressing microorganisms and applications of inulinases. Appl. Microbiol. Biotechnol. 2009, 82:211-220.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 211-220
    • Chi, Z.1    Chi, Z.2    Zhang, T.3    Liu, G.4    Yue, L.5
  • 3
    • 33947136322 scopus 로고    scopus 로고
    • Prebiotics: the concept revisited
    • Roberfroid M. Prebiotics: the concept revisited. J. Nutr. 2007, 137:830S-837S.
    • (2007) J. Nutr. , vol.137
    • Roberfroid, M.1
  • 5
    • 0043157836 scopus 로고    scopus 로고
    • Trp17 and Glu20 residues in conserved WMN(D/E)PN motif are essential for Aspergillus ficuum endoinulinase (EC 3.2.1.7) activity
    • Park S., Han Y., Kim H., Song S., Uhm T.B., Chae K.S. Trp17 and Glu20 residues in conserved WMN(D/E)PN motif are essential for Aspergillus ficuum endoinulinase (EC 3.2.1.7) activity. Biochemistry (Mosc). 2003, 68:658-661.
    • (2003) Biochemistry (Mosc). , vol.68 , pp. 658-661
    • Park, S.1    Han, Y.2    Kim, H.3    Song, S.4    Uhm, T.B.5    Chae, K.S.6
  • 6
    • 0025340159 scopus 로고
    • Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis
    • Reddy V.A., Maley F. Identification of an active-site residue in yeast invertase by affinity labeling and site-directed mutagenesis. J. Biol. Chem. 1990, 265:10817-10820.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10817-10820
    • Reddy, V.A.1    Maley, F.2
  • 7
    • 17544374099 scopus 로고    scopus 로고
    • Studies on identifying the catalytic role of Glu-204 in the active site of yeast invertase
    • Reddy A., Maley F. Studies on identifying the catalytic role of Glu-204 in the active site of yeast invertase. J. Biol. Chem. 1996, 271:13953-13957.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13953-13957
    • Reddy, A.1    Maley, F.2
  • 8
    • 0242490546 scopus 로고    scopus 로고
    • Structural framework of fructosyl transfer in Bacillus subtilis levansucrase
    • Meng G., Futterer K. Structural framework of fructosyl transfer in Bacillus subtilis levansucrase. Nat. Struct. Biol. 2003, 10:935-941.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 935-941
    • Meng, G.1    Futterer, K.2
  • 10
    • 84867404044 scopus 로고    scopus 로고
    • First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity
    • Pouyez J., Mayard A., Vandamme A.M., Roussel G., Perpete E.A., Wouters J., Housen I., Michaux C. First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity. Biochimie. 2012, 94:2423-2430.
    • (2012) Biochimie. , vol.94 , pp. 2423-2430
    • Pouyez, J.1    Mayard, A.2    Vandamme, A.M.3    Roussel, G.4    Perpete, E.A.5    Wouters, J.6    Housen, I.7    Michaux, C.8
  • 11
    • 84887333825 scopus 로고    scopus 로고
    • Invitrogen, EasySelect Pichia Expression Kit. A manual of methods for expression of recombinant proteins using pPICZ and pPICZalpha in Picha pastoris. in EasySelect Pichia Expression Kit Version G 122701 (Technologies, I. l., ed).
    • Invitrogen (2001) EasySelect Pichia Expression Kit. A manual of methods for expression of recombinant proteins using pPICZ and pPICZalpha in Picha pastoris. in EasySelect Pichia Expression Kit Version G 122701 (Technologies, I. l., ed).
    • (2001)
  • 14
    • 1042291218 scopus 로고    scopus 로고
    • Three acidic residues are at the active site of a beta-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68
    • Pons T., Naumoff D.G., Martinez-Fleites C., Hernandez L. Three acidic residues are at the active site of a beta-propeller architecture in glycoside hydrolase families 32, 43, 62, and 68. Proteins. 2004, 54:424-432.
    • (2004) Proteins. , vol.54 , pp. 424-432
    • Pons, T.1    Naumoff, D.G.2    Martinez-Fleites, C.3    Hernandez, L.4
  • 15
    • 0031756740 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of the endoinulinase-encoding gene, inu2, from Aspergillus ficuum
    • Uhm T., C.S., Lee D., Kim S., Cassart J.-P., Vandenhaute J. Cloning and nucleotide sequence of the endoinulinase-encoding gene, inu2, from Aspergillus ficuum. Biotechnol. Lett. 1998, 20:809-812.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 809-812
    • Uhm, T.C.S.1    Lee, D.2    Kim, S.3    Cassart, J.-P.4    Vandenhaute, J.5
  • 17
    • 69049106308 scopus 로고    scopus 로고
    • Xylanase XYL1p from Scytalidium acidophilum: site-directed mutagenesis and acidophilic adaptation
    • Al Balaa B., Brijs K., Gebruers K., Vandenhaute J., Wouters J., Housen I. Xylanase XYL1p from Scytalidium acidophilum: site-directed mutagenesis and acidophilic adaptation. Bioresour. Technol. 2009, 100:6465-6471.
    • (2009) Bioresour. Technol. , vol.100 , pp. 6465-6471
    • Al Balaa, B.1    Brijs, K.2    Gebruers, K.3    Vandenhaute, J.4    Wouters, J.5    Housen, I.6
  • 18
    • 59049093202 scopus 로고    scopus 로고
    • Insights into the catalytic properties of bamboo vacuolar invertase through mutational analysis of active site residues
    • Chen T.H., Huang Y.C., Yang C.S., Yang C.C., Wang A.Y., Sung H.Y. Insights into the catalytic properties of bamboo vacuolar invertase through mutational analysis of active site residues. Phytochemistry. 2009, 70:25-31.
    • (2009) Phytochemistry. , vol.70 , pp. 25-31
    • Chen, T.H.1    Huang, Y.C.2    Yang, C.S.3    Yang, C.C.4    Wang, A.Y.5    Sung, H.Y.6
  • 19
    • 84856757011 scopus 로고    scopus 로고
    • Properties of the inulinase gene levH1 of Lactobacillus casei IAM 1045; cloning, mutational and biochemical characterization
    • Kuzuwa S., Yokoi K.J., Kondo M., Kimoto H., Yamakawa A., Taketo A., Kodaira K. Properties of the inulinase gene levH1 of Lactobacillus casei IAM 1045; cloning, mutational and biochemical characterization. Gene. 2012, 495:154-162.
    • (2012) Gene. , vol.495 , pp. 154-162
    • Kuzuwa, S.1    Yokoi, K.J.2    Kondo, M.3    Kimoto, H.4    Yamakawa, A.5    Taketo, A.6    Kodaira, K.7
  • 20
    • 40249107467 scopus 로고    scopus 로고
    • Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose
    • Lammens W., Le Roy K., Van Laere A., Rabijns A., Van den Ende W. Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose. J. Mol. Biol. 2008, 377:378-385.
    • (2008) J. Mol. Biol. , vol.377 , pp. 378-385
    • Lammens, W.1    Le Roy, K.2    Van Laere, A.3    Rabijns, A.4    Van den Ende, W.5
  • 21
    • 62349102392 scopus 로고    scopus 로고
    • Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications
    • Lammens W., Le Roy K., Schroeven L., Van Laere A., Rabijns A., Van den Ende W. Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications. J. Exp. Bot. 2009, 60:727-740.
    • (2009) J. Exp. Bot. , vol.60 , pp. 727-740
    • Lammens, W.1    Le Roy, K.2    Schroeven, L.3    Van Laere, A.4    Rabijns, A.5    Van den Ende, W.6
  • 22
    • 35848947357 scopus 로고    scopus 로고
    • Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase
    • Le Roy K., Lammens W., Verhaest M., De Coninck B., Rabijns A., Van Laere A., Van den Ende W. Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase. Plant Physiol. 2007, 145:616-625.
    • (2007) Plant Physiol. , vol.145 , pp. 616-625
    • Le Roy, K.1    Lammens, W.2    Verhaest, M.3    De Coninck, B.4    Rabijns, A.5    Van Laere, A.6    Van den Ende, W.7
  • 24
    • 33646253657 scopus 로고    scopus 로고
    • Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose
    • Alberto F., Jordi E., Henrissat B., Czjzek M. Crystal structure of inactivated Thermotoga maritima invertase in complex with the trisaccharide substrate raffinose. Biochem. J. 2006, 395:457-462.
    • (2006) Biochem. J. , vol.395 , pp. 457-462
    • Alberto, F.1    Jordi, E.2    Henrissat, B.3    Czjzek, M.4
  • 25
    • 33747411238 scopus 로고    scopus 로고
    • Single amino acid residue changes in subsite -1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized
    • Ozimek L.K., Kralj S., Kaper T., van der Maarel M.J., Dijkhuizen L. Single amino acid residue changes in subsite -1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized. FEBS J. 2006, 273:4104-4113.
    • (2006) FEBS J. , vol.273 , pp. 4104-4113
    • Ozimek, L.K.1    Kralj, S.2    Kaper, T.3    van der Maarel, M.J.4    Dijkhuizen, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.