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Chemical Compound Review

Maltoheptose     (2R,3R,4S,5S,6R)-2- [(3R,4S,5S,6R)-2-[(2R...

Synonyms: AC1MI2BT, 23846-82-4
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Disease relevance of Maltoheptaose


High impact information on Maltoheptaose

  • Additional soaking of these crystals with maltoheptaose resulted in replacement of Tris in the active site with maltoheptaose, allowing the mapping of the -1 to +5 binding subsites [3].
  • The 22-residue deletion mutant (Nd22) had overall kinetic properties similar to the WT enzyme, except that Nd22 was a better substrate for the protein kinase and the rate of phosphorylation was unaffected by maltoheptaose [4].
  • We have determined the 2.0 and 2.5 A X-ray structures of E257A/D229A CGTase in complex with maltoheptaose and maltohexaose [5].
  • D-enzyme was partially purified from wheat endosperm and shown to exhibit disproportionating activity in vitro by cleaving maltotriose to produce glucose as well as being able to use maltoheptaose as the donor for the addition of glucans to the outer chains of glycogen and amylopectin [6].
  • SusC protein proved to be essential for utilization not only of starch but also of intermediate-sized maltooligosaccharides (maltose to maltoheptaose) [7].

Chemical compound and disease context of Maltoheptaose


Biological context of Maltoheptaose

  • Increases in activation energy of maltoheptaose hydrolysis in most of the mutant glucoamylases suggested cleavage of individual hydrogen bonds in enzyme-substrate complexes [9].
  • The maltoheptaose derivatives were attached by reductive amination or hydrosilation to amino- or SiH-terminated polystyrene (synthesized by anionic polymerization), respectively [10].

Anatomical context of Maltoheptaose


Associations of Maltoheptaose with other chemical compounds


Gene context of Maltoheptaose

  • The hydrolysis of DP 4900-amylose, reduced (r) DP18-maltodextrin and maltoheptaose (catalysed by AMY1 and AMY2) was followed in the absence and in the presence of inhibitor [17].
  • (a) Collisional activation of permethylated oligosaccharide molecular ions (MS2) as illustrated by maltoheptaose, produces abundant fragments from glycosidic bond cleavages which indicate composition and sequence, and weak cross-ring cleavage products which denote specific linkages within the oligosaccharide [18].
  • Glycogen-enzyme interactions were modeled starting from the crystallographic AS: maltoheptaose complex, where two key oligosaccharide binding sites, OB1 and OB2, were identified [19].
  • At a 40% digestion point of maltoheptaose (G7), for example, maltooligosaccharide products larger than maltodecaose (G10) amounted to approx. 60% of the total product from the mutant enzyme reaction, whereas no such large products were observed in the native enzyme reaction [20].
  • In pH 10.0 buffers, tetrakis(4-sulfonatophenyl)porphyrin (TSPP) has been found to form complexes with malto-oligosaccharides from maltose to maltoheptaose and soluble starch [21].

Analytical, diagnostic and therapeutic context of Maltoheptaose


  1. Identification of a new porin, RafY, encoded by raffinose plasmid pRSD2 of Escherichia coli. Ulmke, C., Lengeler, J.W., Schmid, K. J. Bacteriol. (1997) [Pubmed]
  2. Maltodextrin acceptor reactions of Streptococcus mutans 6715 glucosyltransferases. Fu, D.T., Robyt, J.F. Carbohydr. Res. (1991) [Pubmed]
  3. Oligosaccharide and sucrose complexes of amylosucrase. Structural implications for the polymerase activity. Skov, L.K., Mirza, O., Sprogøe, D., Dar, I., Remaud-Simeon, M., Albenne, C., Monsan, P., Gajhede, M. J. Biol. Chem. (2002) [Pubmed]
  4. Mechanism of regulation in yeast glycogen phosphorylase. Lin, K., Hwang, P.K., Fletterick, R.J. J. Biol. Chem. (1995) [Pubmed]
  5. Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity. Uitdehaag, J.C., van Alebeek, G.J., van Der Veen, B.A., Dijkhuizen, L., Dijkstra, B.W. Biochemistry (2000) [Pubmed]
  6. Characterisation of disproportionating enzyme from wheat endosperm. Bresolin, N.S., Li, Z., Kosar-Hashemi, B., Tetlow, I.J., Chatterjee, M., Rahman, S., Morell, M.K., Howitt, C.A. Planta (2006) [Pubmed]
  7. Characterization of four outer membrane proteins that play a role in utilization of starch by Bacteroides thetaiotaomicron. Reeves, A.R., Wang, G.R., Salyers, A.A. J. Bacteriol. (1997) [Pubmed]
  8. The recognition of maltodextrins by Escherichia coli. Ferenci, T. Eur. J. Biochem. (1980) [Pubmed]
  9. Cassette mutagenesis of Aspergillus awamori glucoamylase near its general acid residue to probe its catalytic and pH properties. Bakir, U., Coutinho, P.M., Sullivan, P.A., Ford, C., Reilly, P.J. Protein Eng. (1993) [Pubmed]
  10. New routes to the synthesis of amylose-block-polystyrene rod-coil block copolymers. Loos, K., Müller, A.H. Biomacromolecules (2002) [Pubmed]
  11. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry of oligosaccharides derivatized by reductive amination and N,N-dimethylation. Broberg, S., Broberg, A., Duus, J.O. Rapid Commun. Mass Spectrom. (2000) [Pubmed]
  12. Purification and biochemical characterization of an alpha-glucosidase from Xanthophyllomyces dendrorhous. Marín, D., Linde, D., Lobato, M.F. Yeast (2006) [Pubmed]
  13. Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori. Sierks, M.R., Ford, C., Reilly, P.J., Svensson, B. Protein Eng. (1990) [Pubmed]
  14. Proton NMR spectroscopy assignment of D-glucose residues in highly acetylated starch. Laignel, B., Bliard, C., Massiot, G., Nuzillard, J.M. Carbohydr. Res. (1997) [Pubmed]
  15. Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius. Gueguen, Y., Rolland, J.L., Schroeck, S., Flament, D., Defretin, S., Saniez, M.H., Dietrich, J. FEMS Microbiol. Lett. (2001) [Pubmed]
  16. Purification and properties of alpha-amylase from Aspergillus oryzae ATCC 76080. Chang, C.T., Tang, M.S., Lin, C.F. Biochem. Mol. Biol. Int. (1995) [Pubmed]
  17. On the mechanism of alpha-amylase. Oudjeriouat, N., Moreau, Y., Santimone, M., Svensson, B., Marchis-Mouren, G., Desseaux, V. Eur. J. Biochem. (2003) [Pubmed]
  18. Characterization of oligosaccharide composition and structure by quadrupole ion trap mass spectrometry. Weiskopf, A.S., Vouros, P., Harvey, D.J. Rapid Commun. Mass Spectrom. (1997) [Pubmed]
  19. Towards the molecular understanding of glycogen elongation by amylosucrase. Albenne, C., Skov, L.K., Tran, V., Gajhede, M., Monsan, P., Remaud-Sim??on, M., Andr??-Leroux, G. Proteins (2007) [Pubmed]
  20. An increase in the transglycosylation activity of Saccharomycopsis alpha-amylase altered by site-directed mutagenesis. Matsui, I., Ishikawa, K., Miyairi, S., Fukui, S., Honda, K. Biochim. Biophys. Acta (1991) [Pubmed]
  21. Molecular recognition of malto-oligosaccharides by free and metal tetrakis(4-sulfonatophenyl)porphyrins in basic aqueous solutions. Hamai, S. Journal of nanoscience and nanotechnology. (2001) [Pubmed]
  22. Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. Sorimachi, K., Jacks, A.J., Le Gal-Coëffet, M.F., Williamson, G., Archer, D.B., Williamson, M.P. J. Mol. Biol. (1996) [Pubmed]
  23. Action pattern of human pancreatic alpha-amylase on maltoheptaose, a substrate for determining alpha-amylase in serum. Haegele, E.O., Schaich, E., Rauscher, E., Lehmann, P., Grassl, M. J. Chromatogr. (1981) [Pubmed]
  24. Malononitrile as a new derivatizing reagent for high-sensitivity analysis of oligosaccharides by electrospray ionization mass spectrometry. Ahn, Y.H., Yoo, J.S. Rapid Commun. Mass Spectrom. (1998) [Pubmed]
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