Characterization and site-directed mutagenesis of an α-galactosidase from the deep-sea bacterium Bacillus megaterium

Enzyme and Microbial Technology

Volumn 56, Issue , 2014, Pages 46-52

  Xu, Haibo ^a   Qin, Yongjun ^a   Huang, Zongqing ^a   Liu, Ziduo ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Galactosidase; Glycoside hydrolase family 4; NAD+ binding; Site directed mutagenesis

Indexed keywords

BACILLUS MEGATERIUM; CATALYTIC EFFICIENCIES; DIFFERENT SUBSTRATES; ESCHERICHIA COLI BL21; GALACTOSIDASES; GLYCOSIDE HYDROLASES; NAD+ BINDING; SITE DIRECTED MUTAGENESIS;

AMINO ACIDS; BACTERIA; BACTERIOLOGY; CLONING; ESCHERICHIA COLI; GENE ENCODING;

ENZYME ACTIVITY;

ALPHA GALACTOSIDASE; AMINO ACID; BUFFER; ENZYME; GLYCOSIDASE; RAFFINOSE;

ARTICLE; BACILLUS; BACILLUS HALODURANS; BACILLUS MEGATERIUM; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE; KINETICS; MOLECULAR MODEL; MOLECULAR WEIGHT; MUTANT; NONHUMAN; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; WILD TYPE;

GLYCOSIDE HYDROLASE FAMILY 4; NAD(+) BINDING; SITE-DIRECTED MUTAGENESIS; Α-GALACTOSIDASE;

ALPHA-GALACTOSIDASE; AMINO ACID SEQUENCE; BACILLUS MEGATERIUM; BACTERIAL PROTEINS; CLONING, MOLECULAR; CONSENSUS SEQUENCE; DNA, BACTERIAL; GENES, BACTERIAL; GENOME, BACTERIAL; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAD; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84893478931     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.01.004     Document Type: Article

References (24)

1. Anggraeni A.A., Sakka M., Kimura T., Ratanakhaokchai K., Kitaoka M., Sakka K. Characterization of Bacillus halodurans α-galactosidase Mel4A encoded by the mel4A gene (BH2228). Biosci Biotechnol Biochem 2008, 72:2459-2462.
2. Fujimoto Z., Kaneko S., Momma M., Kobayashi H., Mizuno H. Crystal structure of rice α-galactosidase complexed with d-galactose. J Biol Chem 2003, 278:20313-20318.
3. Margolles-Clark E., Tenkanen M., Luonteri E., Three Penttilä M. α-galactosidase genes of Trichoderma reesei cloned by expression in yeast. Eur J Biochem 1996, 240:104-111.
4. Ishiguro M., Kaneko S., Kuno A., Koyama Y., Yoshida S., Park G-G., et al. Purification and characterization of the recombinant Thermus sp. strain T2 α-galactosidase expressed in Escherichia coli. Appl Environ Microbiol 2001, 67:1601-1606.
5. Jindou S., Karita S., Fujino E., Fujino T., Hayashi H., Kimura T., et al. α-Galactosidase Aga27A, an enzymatic component of the Clostridium josui cellulosome. J Bacteriol 2002, 184:600-604.
6. Post D.A., Luebke V.E. Purification, cloning, and properties of α-galactosidase from Saccharopolyspora erythraea and its use as a reporter system. Appl Microbiol Biotechnol 2005, 67:91-96.
7. +-dependent glycosidases. J Biol Chem 2003, 278:19151-19158.
8. Thompson J., Robrish S.A., Immel S., Lichtenhtaler F.W., Hall B.G., Pikis A. Metabolism of sucrose and its five linkage-isomeric α-d-Glucosyl-d-fructoses by Klebsiella pneumoniae. Participation and properties of sucrose-6-phosphate hydrolase and phospho-α-glucosidase. J Biol Chem 2001, 276:37415-37425.
9. Liljestoüm P.L., Liljestrom P. Nucleotide sequence of the melA gene, coding for α-galactosidase in Escherichia coli K-12. Nucleic Acids Res 1987, 15:2213-2220.
10. Thompson J., Pikis A., Ruvinov S.B., Henrissat B., Yamamoto H., Sekiguchi J. The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-α-glucosidase. J Biol Chem 1998, 273:27347-27356.
11. Bouma C.L., Reizer J., Reizer A., Robrish S.A., Thompson J. 6-phospho-α-d-glucosidase from Fusobacterium mortiferum: cloning, expression, and assignment to family 4 of the glycosylhydrolases. J Bacteriol 1997, 179:4129-4137.
12. Suresh C., Rus'd A.A., Kitaoka M., Hayashi K. Evidence that the putative α-glucosidase of Thermotoga maritima MSB8 is a pNP α-d-glucuronopyranoside hydrolyzing α-glucuronidase. FEBS Lett 2002, 517:159-162.
13. Wierenga R.K., De Maeyer M.C.H., Hol W.G.J. Interaction of pyrophosphate moieties with α-helixes in dinucleotide-binding proteins. Biochemistry 1985, 24:1346-1357.
14. Rossman M.G., Liljas A., Brändén C.I., Banaszak L.J. Evolutionary and structural relationships among dehydrogenases. Enzymes 1975, 11:61-102.
15. + binding by the Thermotoga maritima α-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett 2002, 517:267-271.
16. Chakladar S., Cheng L., Choi M., Liu J., Bennet A.J. Mechanistic evaluation of MelA α-galactosidase from Citrobacter freundii: a family 4 glycosyl hydrolase in which oxidation is rate-limiting. Biochemistry 2011, 50:4298-4308.
17. Larkin M., Blackshields G., Brown N., Chenna R., McGettigan P.A., McWilliam H., et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007, 23:2947-2948.
18. Schwede T., Kopp J., Guex N., Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 2003, 31:3381-3385.
19. Guex N., Peitsch M.C. SWISS-MODEL the Swiss-Pdb viewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
20. Wu G., Feng C., Hong Y., Guo A., Cao S., Dong J., et al. Soluble expression and purification of the anthrax protective antigen in E. coli and identification of a novel dominant-negative mutant N435C. Appl Microbiol Biotechnol 2010, 87:609-616.
21. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
22. Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 1959, 31:426-428.
23. Baik S.H., Saito K., Yokota A., Asano K., Tomita F. Molecular cloning and high-level expression in Escherichia coli of fungal α-galactosidase from Absidia corymbifera IFO 8084. J Biosci Bioeng 2000, 90:168-173.
24. Fridjonsson O., Watzlawick H., Gehweiler A., Rohrhirsch T., Mattes R. Cloning of the gene encoding a novel thermostable α-galactosidase from Thermus brockianus ITI360. Appl Environ Microbiol 1999, 65:3955-3963.