Disease relevance of maltopentaose

• Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose [1].
• The three-dimensional structures of the catalytic residue Glu219-->Gln mutant of Pseudomonas stutzeri maltotetraose-forming exo-alpha-amylase, and its complex with carbohydrate obtained by cocrystallization with maltopentaose were determined [2].
• Site-directed mutagenesis of the greasy slide aromatic residues within the LamB (maltoporin) channel of Escherichia coli: effect on ion and maltopentaose transport [3].
• Crystal structure of a catalytic site mutant of beta-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose [4].

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

• The X-ray crystal structure of a catalytic-site mutant EQ208 [Glu208-->Gln] of alpha-amylase from Bacillus subtilis cocrystallized with maltopentaose (G5) and acarbose has been determined by multiple isomorphous replacement at 2.5 A resolution [1].

Biological context of maltopentaose

• Cloning and nucleotide sequence of the maltopentaose-forming amylase gene from Pseudomonas sp. KO-8940 [10].
• The stability of WPI against heat-induced insolubility at pH 7.0 was improved by conjugation with MP alone, and further improved by phosphorylation [11].

Associations of maltopentaose with other chemical compounds

• The optimum pH for the oligosaccharides consisting of more than five glucose residues, such as maltopentaose and maltohexaitol, was 6 [12].
• The mechanism of porcine pancreatic alpha-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose [13].
• NAG release kinetics followed square root of time kinetics, while in the case of maltose monohydrate and maltopentaose, the release kinetics were zero order in both phases [14].
• 0. Studies using reducing end 14C-labeled maltooligosaccharides revealed a substrate-dependent pH maximum shift; hydrolysis of radiolabeled maltotriose (G3*) was maximal at pH 5.0 while the pH maximum for hydrolysis of radiolabeled maltopentaose (G5*) and maltohexaose (G6*) was pH 6 [15].
• Effect of pressure on the mechanism of hydrolysis of maltotetraose, maltopentaose, and maltohexose catalyzed by porcine pancreatic alpha-amylase [16].

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].

References