Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes

Journal of Structural Biology

Volumn 174, Issue 1, 2011, Pages 196-202

  Qin, Xiaohong ^a   Ren, Limei ^a   Yang, Xue ^a   Bai, Fang ^a   Wang, Lele ^a   Geng, Peng ^b   Bai, Gang ^a   Shen, Yuequan ^a  

^a NANKAI UNIVERSITY   (China)

^b TIANJIN MEDICAL UNIVERSITY   (China)

Author keywords

Amylase; Acarviostatin; Crystal structure; Inhibitor; Type II diabetes

Indexed keywords

ACARBOSE; ACARVIOSTATIN I03; ACARVIOSTATIN II03; ACARVIOSTATIN III03; ACARVIOSTATIN IV03; AMYLASE; TRESTATIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DRUG DESIGN; HUMAN; HYDROLYSIS; NON INSULIN DEPENDENT DIABETES MELLITUS; POLYMERIZATION; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; DIABETES MELLITUS, TYPE 2; DRUG DESIGN; ENZYME INHIBITORS; HUMANS; PANCREATIC ALPHA-AMYLASES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

STREPTOMYCES COELICOFLAVUS;

EID: 79952456013     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.11.020     Document Type: Article

References (32)

1. Abbatecola A.M., Maggi S., Paolisso G. New approaches to treating type 2 diabetes mellitus in the elderly: role of incretin therapies. Drugs Aging 2008, 25:913-925.
2. Boel E., Brady L., Brzozowski A.M., Derewenda Z., Dodson G.G., Jensen V.J., Petersen S.B., Swift H., Thim L., Woldike H.F. Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-Å resolution of two enzymes from Aspergillus. Biochemistry 1990, 29:6244-6249.
3. Brayer G.D., Luo Y., Withers S.G. The structure of human pancreatic alpha-amylase at 1.8Å resolution and comparisons with related enzymes. Protein Sci 1995, 4:1730-1742.
4. Brayer G.D., Sidhu G., Maurus R., Rydberg E.H., Braun C., Wang Y., Nguyen N.T., Overall C.M., Withers S.G. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry 2000, 39:4778-4791.
5. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., Warren G.L. Crystallography and NMR system: a new software suite for macro-molecular structure determination. Acta Crystallogr. Sect. D: Biol. Crystallogr. 1998, 54:905-921.
6. Clissold S.P., Edwards C. Acarbose: a preliminary review of its pharmacodynamic and pharmacokinetic properties, and therapeutic potential. Drugs 1988, 35:214-243.
7. Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., Beier L., Wilson K.S., Davies G.J. X-ray structure of novamyl, the five-domain " maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7Å resolution. Biochemistry 1999, 38:8385-8392.
8. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D: Biol. Crystallogr. 2004, 60:2126-2132.
9. Geng P., Bai G. Two novel aminooligosaccharides isolated from the culture of Streptomyces coelicoflavus ZG0656 as potent inhibitors of alpha-amylase. Carbohydr. Res. 2008, 343:470-476.
10. Geng P., Bai G., Shi Q., Zhang L., Gao Z., Zhang Q. Taxonomy of the Streptomyces strain ZG0656 that produces acarviostatin alpha-amylase inhibitors and analysis of their effects on blood glucose levels in mammalian systems. J. Appl. Microbiol. 2009, 106:525-533.
11. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 280:309-316.
12. Henrissat B., Callebaut I., Fabrega S., Lehn P., Mornon J.P., Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc. Natl. Acad. Sci. USA 1995, 92:7090-7094.
13. Kadziola A., Abe J., Svensson B., Haser R. Crystal and molecular structure of barley alpha-amylase. J. Mol. Biol. 1994, 239:104-121.
14. Li C., Begum A., Numao S., Park K.H., Withers S.G., Brayer G.D. Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts. Biochemistry 2005, 44:3347-3357.
15. Low L.C. The epidemic of type 2 diabetes mellitus in the Asia-Pacific region. Pediatr. Diabetes 2010, 11:212-215.
16. Machius M., Vertesy L., Huber R., Wiegand G. Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics. J. Mol. Biol. 1996, 260:409-421.
17. McCoy A.J. Solving structures of protein complexes by molecular replacement with phaser. Acta Crystallogr. Sect. D: Biol. Crystallogr. 2007, 63:32-41.
18. Noda K., Umeda F., Nawata H. Effect of acarbose on glucose intolerance in patients with non-insulin-dependent diabetes mellitus. Diabetes Res. Clin. Pract. 1997, 37:129-136.
19. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
20. Papanas N., Maltezos E. Oral antidiabetic agents: anti-atherosclerotic properties beyond glucose lowering?. Curr. Pharm. Des. 2009, 15:3179-3192.
21. Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F. Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex. Biochemistry 2001, 40:7700-7709.
22. Rabasa-Lhoret R., Chiasson J.L. Potential of alpha-glucosidase inhibitors in elderly patients with diabetes mellitus and impaired glucose tolerance. Drugs Aging 1998, 13:131-143.
23. Ramasubbu N., Paloth V., Luo Y., Brayer G.D., Levine M.J. Structure of human salivary alpha-amylase at 1.6Å resolution: implications for its role in the oral cavity. Acta Crystallogr. Sect. D: Biol. Crystallogr. 1996, 52:435-446.
24. Rydberg E.H., Sidhu G., Vo H.C., Hewitt J., Cote H.C., Wang Y., Numao S., MacGillivray R.T., Overall C.M., Brayer G.D., Withers S.G. Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Protein Sci. 1999, 8:635-643.
25. Sim L., Quezada-Calvillo R., Sterchi E.E., Nichols B.L., Rose D.R. Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. J. Mol. Biol. 2008, 375:782-792.
26. Sim L., Jayakanthan K., Mohan S., Nasi R., Johnston B.D., Pinto B.M., Rose D.R. New glucosidase inhibitors from an ayurvedic herbal treatment for type 2 diabetes: structures and inhibition of human intestinal maltase-glucoamylase with compounds from Salacia reticulata. Biochemistry 2010, 49:443-451.
27. Smith R.J., Nathan D.M., Arslanian S.A., Groop L., Rizza R.A., Rotter J.I. Individualizing therapies in type 2 diabetes mellitus based on patient characteristics: what we know and what we need to know. J. Clin. Endocrinol. Metab. 2010, 95:1566-1574.
28. Tarling C.A., Woods K., Zhang R., Brastianos H.C., Brayer G.D., Andersen R.J., Withers S.G. The search for novel human pancreatic alpha-amylase inhibitors: high-throughput screening of terrestrial and marine natural product extracts. ChemBioChem 2008, 9:433-438.
29. Whitmore C. Type 2 diabetes and obesity in adults. Br. J. Nurs. 2010, 19(880):882-886.
30. Yee H.S., Fong N.T. A review of the safety and efficacy of acarbose in diabetes mellitus. Pharmacotherapy 1996, 16:792-805.
31. Yokose K., Ogawa K., Sano T., Watanabe K., Maruyama H.B., Suhara Y. New alpha-amylase inhibitor, trestatins. I. Isolation, characterization and biological activities of trestatins A, B and C. J. Antibiot. (Tokyo) 1983, 36:1157-1165.
32. Zhang R., Li C., Williams L.K., Rempel B.P., Brayer G.D., Withers S.G. Directed " in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase. Biochemistry 2009, 48:10752-10764.