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Chemical Compound Review

CHEBI:62006     (2R,3R,4R,5R)-4- [(2S,3R,4R,5S,6R)-5-[(2R...

Synonyms: AC1L3XPY, AR-1L8571, I14-90801, EINECS 252-118-9
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Disease relevance of maltopentaose


High impact information on maltopentaose

  • To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography [5].
  • Amylose was prepared by enzymatic polymerization of alpha-D-glucose 1-phosphate dipotassium catalyzed by a phosphorylase using two kinds of the primers derived from maltopentaose, and then it was chemically bonded to silica gel to be used as a chiral stationary phase (CSP) in high-performance liquid chromatography [6].
  • The insight into substrate recognition derived from this mutagenesis study corroborates a binding model where maltopentaose fits into the phosphorylase b structure in a distorted form [7].
  • Analysis of the power density spectra using a previously proposed simple model (Benz, R., A. Schmid, and G. H. Vos-Scheperkeuter. 1987. J. Membr. Biol. 100: 12-29), allowed the evaluation of the on- and the off-rate constants for the maltopentaose binding to the binding site inside the LamB channels [8].
  • The kinetics of hydrolysis of two synthetic linear maltosaccharides, namely maltotriose and maltopentaose, were studied [9].

Chemical compound and disease context of maltopentaose


Biological context of maltopentaose


Associations of maltopentaose with other chemical compounds


Gene context of maltopentaose

  • The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites [17].
  • The resulting, purified 6HisMalR(SI) was shown to bind to two motifs within the S. lividans malR-malE intergenic region and to dissociate in the presence of maltopentaose [18].
  • An enzyme, 6-alpha-glucosyltransferase, which is involved in CTS synthesis from starch, from Bacillus globisporus C11 produced 4-O-alpha-glucosyl-CTS (4G-CTS) from a mixture containing CTS and maltopentaose [19].

Analytical, diagnostic and therapeutic context of maltopentaose

  • Stability constants for binding of maltopentaose to the mutant channels were measured using titration experiments with the carbohydrate [3].
  • HPLC analysis for identifying the anomers of products indicated that the AA hydrolyzed maltopentaose (G5) at the third glycoside bond predominantly, which differed from Taka-amylase A and the neutral alpha-amylase (NA) from the citric acid-koji [20].


  1. Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose. Fujimoto, Z., Takase, K., Doui, N., Momma, M., Matsumoto, T., Mizuno, H. J. Mol. Biol. (1998) [Pubmed]
  2. Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose. Yoshioka, Y., Hasegawa, K., Matsuura, Y., Katsube, Y., Kubota, M. J. Mol. Biol. (1997) [Pubmed]
  3. Site-directed mutagenesis of the greasy slide aromatic residues within the LamB (maltoporin) channel of Escherichia coli: effect on ion and maltopentaose transport. Denker, K., Orlik, F., Schiffler, B., Benz, R. J. Mol. Biol. (2005) [Pubmed]
  4. Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose. Miyake, H., Kurisu, G., Kusunoki, M., Nishimura, S., Kitamura, S., Nitta, Y. Biochemistry (2003) [Pubmed]
  5. 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]
  6. Preparation of silica gel-bonded amylose through enzyme-catalyzed polymerization and chiral recognition ability of its phenylcarbamate derivative in HPLC. Enomoto, N., Furukawa, S., Ogasawara, Y., Akano, H., Kawamura, Y., Yashima, E., Okamoto, Y. Anal. Chem. (1996) [Pubmed]
  7. Mutational analysis of the oligosaccharide recognition site at the active site of Escherichia coli maltodextrin phosphorylase. Drueckes, P., Boeck, B., Palm, D., Schinzel, R. Biochemistry (1996) [Pubmed]
  8. Noise analysis of ion current through the open and the sugar-induced closed state of the LamB channel of Escherichia coli outer membrane: evaluation of the sugar binding kinetics to the channel interior. Nekolla, S., Andersen, C., Benz, R. Biophys. J. (1994) [Pubmed]
  9. Kinetic studies on glucoamylase of rabbit small intestine. Sivakami, S., Radhakrishnan, A.N. Biochem. J. (1976) [Pubmed]
  10. Cloning and nucleotide sequence of the maltopentaose-forming amylase gene from Pseudomonas sp. KO-8940. Shida, O., Takano, T., Takagi, H., Kadowaki, K., Kobayashi, S. Biosci. Biotechnol. Biochem. (1992) [Pubmed]
  11. Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. Li, C.P., Enomoto, H., Ohki, S., Ohtomo, H., Aoki, T. J. Dairy Sci. (2005) [Pubmed]
  12. Substrate-dependent shift of optimum pH in porcine pancreatic alpha-amylase-catalyzed reactions. Ishikawa, K., Matsui, I., Honda, K., Nakatani, H. Biochemistry (1990) [Pubmed]
  13. The mechanism of porcine pancreatic alpha-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose. Al Kazaz, M., Desseaux, V., Marchis-Mouren, G., Prodanov, E., Santimone, M. Eur. J. Biochem. (1998) [Pubmed]
  14. Controlled release of saccharides from matrix tablets. Mäki, R., Suihko, E., Korhonen, O., Pitkänen, H., Niemi, R., Lehtonen, M., Ketolainen, J. European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft für Pharmazeutische Verfahrenstechnik e.V. (2006) [Pubmed]
  15. Mechanism of action and the substrate-dependent pH maximum shift of the alpha-amylase of Bacillus coagulans. Keating, L., Kelly, C., Fogarty, W. Carbohydr. Res. (1998) [Pubmed]
  16. Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic alpha-amylase. Matsumoto, T., Makimoto, S., Taniguchi, Y. Biochim. Biophys. Acta (1997) [Pubmed]
  17. Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides. Payan, F., Qian, M. J. Protein Chem. (2003) [Pubmed]
  18. Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR. Schlösser, A., Weber, A., Schrempf, H. FEMS Microbiol. Lett. (2001) [Pubmed]
  19. Enzymatic synthesis of glycosyl cyclic tetrasaccharide with 6-alpha-glucosyltransferase and 3-alpha-isomaltosyltransferase. Aga, H., Higashiyama, T., Watanabe, H., Sonoda, T., Yuen, R., Nishimoto, T., Kubota, M., Fukuda, S., Kurimoto, M., Tsujisaka, Y. J. Biosci. Bioeng. (2004) [Pubmed]
  20. N-terminal sequence of amino acids and some properties of an acid-stable alpha-amylase from citric acid-koji (Aspergillus usamii var.). Suganuma, T., Tahara, N., Kitahara, K., Nagahama, T., Inuzuka, K. Biosci. Biotechnol. Biochem. (1996) [Pubmed]
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