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AMY2  -  amylase, alpha 2B (pancreatic)

Sus scrofa

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Disease relevance of AMY2B

  • The crystal structure of the complex formed between the 498 amino acid residue porcine pancreatic alpha-amylase (PPA) and the 74 amino acid residue inhibitor Tendamistat secreted from Streptomyces tendae, has been determined by multiple isomorphous replacement in a crystal of space group P6(5)22 (a = b = 77.7 A, c = 359.5 A) [1].
  • The compounds were tested for their antimuscarinic activities by: (a) inhibition of [N-methyl-3H]scopolamine binding to the muscarinic receptors of N4TG1 neuroblastoma cells, (b) inhibition of carbachol-induced alpha-amylase release from rat pancreas acini, and (c) blocking of acetylcholine-induced contraction of guinea pig ileum [2].
  • In order to obtain information on their structure, a hepatopancreas cDNA library constructed in phage lambda-Zap II (Strategene) was screened using a synthetic oligonucleotide based on the amino acid sequence of a V8 staphylococcal protease peptide of P. vannamei alpha-amylase [3].
  • It was concluded that the minimal adjuvant-active subunit of cell wall peptidoglycan for the induction of delayed-type hypersensitivity to monoazobenzenearsonate-N-acetyl-L-tyrosine and for circulating-antibody formation to bacterial alpha-amylase and the thymus-independent antigen DNP-Ficoll was N-acetylmuramyldipeptide, MurNAc-L-Ala-D-isoGln [4].
  • Acid hydrolysis of retrograded amylose gave a resistant fragment having an average d.p. of 32, human-salivary and porcine-pancreatic alpha amylases gave a resistant fragment of d.p. 43, and Bacillus subtilis alpha amylase gave a resistant fragment of d.p. 50 [5].

High impact information on AMY2B

  • After immunization of a dromedary with bovine erythrocyte carbonic anhydrase and porcine pancreatic alpha-amylase, it was demonstrated that a considerable amount of heavy-chain antibodies, acting as true competitive inhibitors, circulate in the bloodstream [6].
  • Affinity-purified, monospecific rabbit antibodies against rat pancreatic alpha-amylase and bovine pancreatic alpha-chymotrypsinogen were used for immunoferritin observations of ultrathin frozen sections of mildly fixed exocrine pancreatic tissue from secretion-stimulated (pilocarpine) rats and from overnight-fasted rats and guinea pigs [7].
  • The most thermostable alpha-amylase from Bacillus licheniformis (apparent transition temperature, T(1/2) approximately 100 degrees C) shows an unfolding rate which is four orders of magnitude smaller as compared with the alpha-amylase from pig pancreas (T(1/2) approximately 65 degrees C) [8].
  • Binding with biotin-polymer sugar probes revealed that the alpha-amylase has affinity to alpha-mannose, alpha-N-acetylneuraminic acid, and beta-N-acetyllactosamine, which are components of N-glycans [9].
  • 0. A binary complex formation out of equimolar amounts of the inhibitor and alpha-amylase, was demonstrated by polyacrylamide gel electrophoresis, and Bio-Gel P-100 chromatography [10].

Chemical compound and disease context of AMY2B


Biological context of AMY2B


Anatomical context of AMY2B

  • Fractions were analyzed for protein, alpha-amylase (EC and 5'-nucleotidase (EC as marker enzymes for zymogen granule content and membranes, respectively [18].
  • In isolated parotid gland lobules alpha-amylase secretion proceeded at a linear rate already during the first 1 min of stimulation, whereas in pancreatic lobules a measurable rate of alpha-amylase secretion did not occur before 5 min [19].
  • Only one distinct peak, with coincident alpha-amylase and 5'-nucleotidase activity, and most protein was detected, which reflects the presence of a single population of intact zymogen granules [18].
  • Starch granules are digested by pancreatic alpha-amylase in the small intestine [20].
  • New allelic variants of salivary gland alpha-amylase in pigs (AMY-1C, AMY-1D) have been detected using affinity electrophoresis [21].

Associations of AMY2B with chemical compounds


Other interactions of AMY2B


Analytical, diagnostic and therapeutic context of AMY2B


  1. The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat. Wiegand, G., Epp, O., Huber, R. J. Mol. Biol. (1995) [Pubmed]
  2. Distance geometry of alpha-substituted 2,2-diphenylpropionate antimuscarinics. Gordon, R.K., Breuer, E., Padilla, F.N., Smejkal, R.M., Chiang, P.K. Mol. Pharmacol. (1989) [Pubmed]
  3. Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea decapoda): evolutionary aspects. Van Wormhoudt, A., Sellos, D. J. Mol. Evol. (1996) [Pubmed]
  4. Adjuvant activity of mycobacterial fractions: adjuvant activity of synthetic N-acetylmuramyl-dipeptide and the related compounds. Azuma, I., Sugimura, K., Taniyama, T., Yamawaki, M., Yamamura, Y. Infect. Immun. (1976) [Pubmed]
  5. Structure studies of amylose-V complexes and retrograded amylose by action of alpha amylases, and a new method for preparing amylodextrins. Jane, J., Robyt, J.F. Carbohydr. Res. (1984) [Pubmed]
  6. Potent enzyme inhibitors derived from dromedary heavy-chain antibodies. Lauwereys, M., Arbabi Ghahroudi, M., Desmyter, A., Kinne, J., Hölzer, W., De Genst, E., Wyns, L., Muyldermans, S. EMBO J. (1998) [Pubmed]
  7. Immunocytochemical localization of amylase and chymotrypsinogen in the exocrine pancreatic cell with special attention to the Golgi complex. Geuze, J.J., Slot, J.W., Tokuyasu, K.T. J. Cell Biol. (1979) [Pubmed]
  8. Thermostability of irreversible unfolding alpha-amylases analyzed by unfolding kinetics. Duy, C., Fitter, J. J. Biol. Chem. (2005) [Pubmed]
  9. Porcine pancreatic alpha-amylase shows binding activity toward N-linked oligosaccharides of glycoproteins. Matsushita, H., Takenaka, M., Ogawa, H. J. Biol. Chem. (2002) [Pubmed]
  10. alpha-Amylase inhibitor from fungus Cladosporium herbarum F-828. Saito, N. J. Biol. Chem. (1982) [Pubmed]
  11. Correlation of LUMO localization with the alpha-amylase inhibition constant in a Tendamistat-based series of linear and cyclic peptides. Heyl, D.L., Fernandes, S., Khullar, L., Stephens, J., Blaney, E., Opang-Owusu, H., Stahelin, B., Pasko, T., Jacobs, J., Bailey, D., Brown, D., Milletti, M.C. Bioorg. Med. Chem. (2005) [Pubmed]
  12. Comparison of o-phthalaldehyde modification of alpha-amylases from porcine pancreas and Bacillus subtilis with Taka-amylase A. Ueyama, H., Chiba, Y., Kobayashi, M. Biosci. Biotechnol. Biochem. (1995) [Pubmed]
  13. Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides. Payan, F., Qian, M. J. Protein Chem. (2003) [Pubmed]
  14. Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase. D'Amico, S., Sohier, J.S., Feller, G. J. Mol. Biol. (2006) [Pubmed]
  15. Refined molecular structure of pig pancreatic alpha-amylase at 2.1 A resolution. Larson, S.B., Greenwood, A., Cascio, D., Day, J., McPherson, A. J. Mol. Biol. (1994) [Pubmed]
  16. De novo design of alpha-amylase inhibitor: a small linear mimetic of macromolecular proteinaceous ligands. Dolecková-Maresová, L., Pavlík, M., Horn, M., Mares, M. Chem. Biol. (2005) [Pubmed]
  17. Adjuvant activity of purified peptidoglycan of Listeria monocytogenes in mice and guinea pigs. Saiki, I., Kamisango, K., Tanio, Y., Okumura, H., Yamamura, Y., Azuma, I. Infect. Immun. (1982) [Pubmed]
  18. Separation and analysis of pig pancreatic zymogen granules with free flow electrophoresis and lectins. Spaans, M.C., Tobler, M., Ammann, R.W., Freiburghaus, A.U. Electrophoresis (1994) [Pubmed]
  19. Effects of stimulation of muscarinic and of beta-catecholamine receptors on the intracellular distribution of protein kinase C in guinea pig exocrine glands. Machado-de Domenech, E., Söling, H.D. Biochem. J. (1987) [Pubmed]
  20. Digestion and absorption of carbohydrates in fowl and events through perinatal development. Moran, E.T. J. Nutr. (1985) [Pubmed]
  21. Salivary gland amylase polymorphism in pigs and cattle detected by affinity electrophoresis. Rozhkov YuI, n.u.l.l., Galimov, I.R. Anim. Genet. (1990) [Pubmed]
  22. Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase. Qian, M., Ajandouz, e.l. .H., Payan, F., Nahoum, V. Biochemistry (2005) [Pubmed]
  23. Detection of alpha-amylase activity in unprocessed preamylase produced in the cell-free translation of porcine pancreatic RNA. Brown, T.L., Wold, F. J. Biol. Chem. (1981) [Pubmed]
  24. Some aspects of the mechanism of complexation of red kidney bean alpha-amylase inhibitor and alpha-amylase. Wilcox, E.R., Whitaker, J.R. Biochemistry (1984) [Pubmed]
  25. Detection of noncovalent complex between alpha-amylase and its microbial inhibitor tendamistat by electrospray ionization mass spectrometry. Douglas, D.J., Collings, B.A., Numao, S., Nesatyy, V.J. Rapid Commun. Mass Spectrom. (2001) [Pubmed]
  26. Changes of clinical biochemical values after bilateral nephrectomy and allotransplantation of the kidney in pigs. Fortýn, K., Hruban, V., Hradecký, J., Horák, V. International urology and nephrology. (1988) [Pubmed]
  27. Characterization of porcine reproductive and respiratory syndrome virus hemagglutinin. Jusa, E.R., Inaba, Y., Kouno, M., Asagoe, T., Uwatoko, K., Yamaura, K., Hirose, O. J. Vet. Med. Sci. (1997) [Pubmed]
  28. Molecular cloning and primary structure analysis of porcine pancreatic alpha-amylase. Darnis, S., Juge, N., Guo, X.J., Marchis-Mouren, G., Puigserver, A., Chaix, J.C. Biochim. Biophys. Acta (1999) [Pubmed]
  29. Hormonal stimulation of alpha-amylase synthesis in porcine pancreatic minces. Rosenfeld, M.G., Abrass, I., Chang, B. Endocrinology (1976) [Pubmed]
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