The catalytic and other residues essential for the activity of the midgut trehalase from Spodoptera frugiperda

Insect Biochemistry and Molecular Biology

Volumn 40, Issue 10, 2010, Pages 733-741

  Silva, Maria C P ^a   Terra, Walter R ^a   Ferreira, Clélia ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Activity rescue; Catalytic groups; Recombinant trehalase; Trehalase; Trehalase essential groups

Indexed keywords

INSECT PROTEIN; TREHALASE; TREHALOSE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; ARMYWORM; ARTICLE; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DIGESTIVE SYSTEM; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BIOCATALYSIS; CATALYTIC DOMAIN; DIGESTIVE SYSTEM; INSECT PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SPODOPTERA; TREHALASE; TREHALOSE;

BACTERIA (MICROORGANISMS); FUNGI; HEXAPODA; LEPIDOPTERA; SPODOPTERA FRUGIPERDA;

EID: 77956990799     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2010.07.006     Document Type: Article

References (41)

1. Andrade M.A., Chacón P., Merelo J.J., Morán F. Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network. Prot. Eng. 1993, 6:383-390.
2. Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics 2006, 22:195-200.
3. Bates P.A., Kelley L.A., MacCallum R.M., Sternberg M.J.E. Enhancement of protein modeling by human Intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins: Structure, Funct. Genetics, Suppl. 2001, 5:39-46.
4. Bounias M., Bahjou A., Gordoux L., Moreau R. Molecular activation of a trehalase purified from the fat body of a coleopteran insect (Tenebrio molitor), by an endogenous insulin-like peptide. Biochem. Mol. Biol. Int. 1993, 31:249-266.
5. Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
6. Bravman T., Belakhov V., Solomon D., Shoham G., Henrissat B., Baasov T., Shoham Y. Identification of the catalytic residues in family 52 glycoside hydrolase, a beta-xylosidase from Geobacillus stearothermophilus T-6. J. Biol. Chem. 2003, 278:26742-26749.
7. Cantarel B.L., Coutinho P.M., Rancure l.C., Bernard T., Lombard V., Henrissat B. The carbohydrate-Active enzymes database (CAZY): an expert resource for glucogenomics. Nucleic Acids Res. (Database issue) 2009, 37:D233-D238.
8. Cobucci-Ponzano B., Trincone A., Giordano A., Rossi M., Moracci M. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry 2003, 42:9525-9531.
9. Combet C., Jambon M., Deléage G., Geourjon C. Geno3D: automatic comparative molecular modeling of protein. Bioinformatics 2002, 18:213-214.
10. Dahlqvist A. Assay of intestinal dissaccharidases. Analyt. Biochem. 1968, 22:99-107.
11. Davis I.W., Leaver-Fay A., Chen V.B., Block J.N., Kapral G.J., Wang X., Murray L.W., Arendall W.B., Snoeyink J., Richardson J.S., Richardson D.C. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 2007, 35:W375-W383.
12. Elbein A.D., Pan Y.T., Pastuszak I., Carroll D. New insights on trehalose: a multifunctional molecule. Glycobiology 2003, 13:417-427.
13. Fersht A.R. The hydrogen bonding in molecular recognition. TIBS 1987, 12:301-304.
14. Fersht A.R. Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. Lond. B 1974, 187:397-407.
15. Fersht A.R., Leatherbarrow R.J., Wells N.C. Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthase. TIBS 1986, 11:321-325.
16. Fersht A.R., Shi J.-P., Knill-Jones J., Lowe D.M., Wilkinson A.J., Blow D.M., Brick P., Carter P., Waye M.M.Y., Winter G. Hydrogen bonding and biological specificity analyzed by protein engineering. Nature 1987, 314:235-238.
17. Frandsen T.P., Dupont C., Lehmbeck J., Stoffer B., Sierks M.R., Honzatko R.B., Svensson B. Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the gamma-carboxylate group of glutamic acid 400. Biochemistry 1994, 46:13808-13886.
18. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. Protein identification and analysis tools on the ExPASy Server. The Proteomics Protocols Handbook 2005, 571-607. Humana Press. J.M. Walker (Ed.).
19. Gibson R.P., Gloster T.M., Roberts S., Warren R.A., Storch de Gracia I., García A., Chiara J.L., Davies G.J. Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Angew Chem. Int. Ed. Engl. 2007, 46:4115-4119.
20. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
21. Higuchi R. Recombinant PCR. PCR Protocols. A Guide to Methods and Applications 1990, 177-183. Academic Press, San Diego, CA. M.A. Innis, D.H. Gelfand, J.J. Sninsky, T.J. White (Eds.).
22. Kelley L.A., Sternberg M.J.E. Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
23. Krissinel E., Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Cryst. 2004, 60:2256-2268.
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
25. Lambert C., Leonard N., De Bolle X., Depiereux E. ESyPred3D: prediction of proteins 3D structures. Bioinformatics 2002, 18:1250-1256.
26. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 1993, 26:283-291.
27. Lee J.H., Tsuji M., Nakamura M., Nishimoto M., Okuyama M., Mori H., Kimura A., Matsui H., Chiba S. Purification and identification of the essential ionizable groups of honeybee, Apis mellifera L., trehalase. Biosci. Biotechnol. Biochem. 2001, 65:2657-2665.
28. Lund, O., Nielsen, M., Lundegaard, C., Worning, P., 2002. CPH models 2.0: X3M a Computer program to extract 3D Models. CASP5 conference A102.
29. Ly H.D., Withers S.G. Mutagenesis of glycosidases. Annu. Ver. Biochem. 1999, 68:487-522.
30. Marana S.R., Jacobs-Lorena M., Terra W.R., Ferreira C. Amino acid residues involved in substrate binding and catalysis in an insect digestive b-glycosidase. Biochim. Biophys. Acta 2001, 1545:41-52.
31. Merelo J.J., Andrade M.A., Prieto A., Morán F. Proteinotopic feature maps. Neurocomputing 1994, 6:443-454.
32. Miyake H., Otsuka C., Nishimura S., Nitta Y. Catalytic Mechanism of ß-Amylase from Bacillus cereus var. mycoides: chemical rescue of hydrolytic activity for a catalytic site mutant (Glu367Ala) by Azide. J. Biochem. (Tokyo) 2002, 131:587-591.
33. Paal K., Ito M., Withers G. Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues. Biochem. J. 2004, 378:141-149.
34. Segel I.H. Enzyme Kinetics 1975, Wiley, New York.
35. Silva M.C.P., Ribeiro A.F., Terra W.R., Ferreira C. Sequencing of Spodoptera frugiperda midgut trehalases and demonstration of secretion of soluble trehalase by midgut columnar cells. Insect Molec. Biol. 2009, 18:769-784.
36. Silva M.C.P., Terra W.R., Ferreira C. The role of carboxyl, guanidine and imidazole groups in catalysis by a midgut trehalase purified from an insect larvae. Insect Biochem. Molec. Biol. 2004, 34:1089-1099.
37. Terra W.R., Ferreira C., de Bianchi A.G. Physical properties and Tris inhibition of an insect trehalase and a thermodynamic approach to the nature of its active site. Biochem. Biophys. Acta 1978, 524:131-141.
38. Terra W.R., Terra I.C.M., Ferreira C., de Bianchi A.G. Carbodiimide-reactive carboxyl groups at the active site of an insect midgut trehalase. Biochem. Biophys. Acta 1979, 571:79-85.
39. Teodorescu O., Galor T., Pillardy J., Elber R. Enriching the sequence substitution matrix by structural information. Proteins: Structure, Funct. Bioinform. 2004, 54:41-48.
40. Wiederstein M., Sippl M.J. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 2007, 35:W407-W410.
41. Zechel D.L., Withers S.G. Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 2000, 33:11-18.