Disease relevance of C01936

• The LSL-mediated hemolysis was protected osmotically by polyethylene glycol 4000 and maltohexaose [1].
• Besides alpha-cyclodextrin, maltohexaose was also taken up by the K. oxytoca cym system, but because of the inability of maltodextrins to induce the cym system, growth of E. coli mal mutants on linear maltodextrin was not observed when the cells harbored only the cym uptake system [2].
• Expression, crystallization and preliminary X-ray crystallographic studies of Klebsiella pneumoniae maltohexaose-producing alpha-amylase [3].
• Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft [4].
• Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes [5].

High impact information on C01936

• To elucidate the orientation, we performed point mutations at each side of the channel and analyzed the ion current fluctuation caused by an asymmetric maltohexaose addition [6].
• The so developed approach has been tested with experimental data for a single maltoporin trimer being reconstituted in black lipid membranes when studied in the presence of maltohexaose as the substrate [7].
• ESI tandem mass spectrometry of the ABDEAE-derivatized maltohexaose provides structural information at the low-picomole level [8].
• A hybrid region between residues 34-76 is demonstrated to correlate with the alpha-amylases' substrate specificity, i.e. either hydrolysis or accumulation of maltohexaose [9].
• Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic Bacillus sp. #707 and structural similarity to liquefying type alpha-amylases [10].

Biological context of C01936

• The molecular characterization of the maltohexaose-producing amylase gene of Klebsiella pneumoniae revealed an open reading frame in which 2,031 base pairs encode a protein of 677 amino acids with a calculated molecular weight of 75,921 [11].

Associations of C01936 with other chemical compounds

• The great potential of this method is demonstrated for the characterization of a beta-glucosidase (pI 8.4) from Trichoderma reesei QM 9414 and an alpha 1,4-glucan glucohydrolase from Aspergillus niger with cellotetraose and maltohexaose as examplary substrates [12].
• Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase [13].
• The glass transition temperatures of the pure compounds ranged from 364 K for maltose to 448 K for maltohexaose [14].
• 0. 80% of the activity was retained after 15 min at 50 degrees C. This enzyme produced maltohexaose from starch, amylose and amylopectin by exo-attack, but did not act on alpha- or beta-cyclodextrin, pullulan or maltohexaitol [5].

Gene context of C01936

• The properties of the recombinant beta-amylase were almost the same as those of barley beta-amylase except for the pI and the Km values for maltohexaose and maltoheptaose.(ABSTRACT TRUNCATED AT 250 WORDS)[15]

Analytical, diagnostic and therapeutic context of C01936

• Metastable decay rates of alpha-cyclodextrin and maltohexaose coordinated to proton and alkali metal ions were determined from ions produced by liquid secondary ion mass spectrometry in an external source Fourier transform mass spectrometry instrument [16].
• The products were purified by paper chromatography, or maltohexaose was specifically obtained from purified alpha-cyclodextrin by the action of cyclodextrinase of K. oxytoca M5a1 [17].

References