Characterization of the interdependency between residues that bind the substrate in a β-glycosidase

Brazilian Journal of Medical and Biological Research

Volumn 43, Issue 1, 2010, Pages 8-12

  Tomassi, M H ^a   Rozenfeld, J H K ^a   Goncalves L M ^a   Marana, S R ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Site directed mutagenesis; Spodoptera frugiperda; Substrate specificity; glycosidase

Indexed keywords

4 NITROPHENYL BETA FUCOSIDE; 4 NITROPHENYL BETA GALACTOSIDE; AMINO ACID; BETA GLUCOSIDASE; ENZYME; GALACTOSIDE; HYDROXYL GROUP; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; BACTERIUM; CRYSTALLOGRAPHY; ENERGY; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROGEN BOND; LEPIDOPTERA; MUTANT; NONHUMAN; PURIFICATION; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

SPODOPTERA FRUGIPERDA;

EID: 75649107616     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/s0100-879x2009007500033     Document Type: Article

References (20)

1. Wells JA. Additivity of mutational effects in proteins. Biochemistry 1990; 29: 8509-8517.
2. Kuliopulos A, Talalay P, Mildvan AS. Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction. Biochemistry 1990; 29: 10271-10280.
3. Mildvan AS, Weber DJ, Kuliopulos A. Quantitative interpretations of double mutations of enzymes. Arch Biochem Biophys 1992; 294: 327-340.
4. Mildvan AS. Inverse thinking about double mutants of enzymes. Biochemistry 2004; 43: 14517-14520.
5. Coutinho P, Henrissat B. Carbohydrate-active enzymes: an integrated database approach. In: Gilbert HJ, Davies G, Henrissat B, Svensson B (Editors), Recent advances in carbohydrate bioengineering. Cambridge: The Royal Society of Chemistry; 1999. p 3-12.
6. Davies GJ, Wilson KS, Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 1997; 321 (Part 2): 557-559.
7. Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure 1997; 5: 663-675.
8. Cicek M, Blanchard D, Bevan DR, Esen A. The aglycone specificity- determining sites are different in 2, 4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (Maize beta-glucosidase) and dhurrinase (Sorghum betaglucosidase). J Biol Chem 2000; 275: 20002-20011.
9. Gloster TM, Roberts S, Ducros VM, Perugino G, Rossi M, Hoos R, et al. Structural studies of the beta-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors. Biochemistry 2004; 43: 6101-6109.
10. Fernandez P, Canada FJ, Jimenez-Barbero J, Martin-Lomas M. Substrate specificity of small-intestinal lactase: study of the steric effects and hydrogen bonds involved in enzyme-substrate interaction. Carbohydr Res 1995; 271: 31-42.
11. Namchuk MN, Withers SG. Mechanism of Agrobacterium beta-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions. Biochemistry 1995; 34: 16194-16202.
12. Marana SR, Terra WR, Ferreira C. The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda beta-glycosidase. Eur J Biochem 2002; 269: 3705-3714.
13. Marana SR, Andrade EH, Ferreira C, Terra WR. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. Eur J Biochem 2004; 271: 4169-4177.
14. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
15. Gill SC, von Hippel PH. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989; 182: 319-326.
16. Wilkinson AJ, Fersht AR, Blow DM, Winter G. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry 1983; 22: 3581-3586.
17. Marana SR. Molecular basis of substrate specificity in family 1 glycoside hydrolases. IUBMB Life 2006; 58: 63-73.
18. Sanz-Aparicio J, Hermoso JA, Martinez-Ripoll M, Lequerica JL, Polaina J. Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases. J Mol Biol 1998; 275: 491-502.
19. Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, et al. Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside. Biochem J 2001; 354: 37-46.
20. Verdoucq L, Moriniere J, Bevan DR, Esen A, Vasella A, Henrissat B, et al. Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate. J Biol Chem 2004; 279: 31796-31803.