Disease relevance of maltotetraose

• Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri [1].
• The crystal structures of Klebsiella pneumoniae pullulanase and its complex with glucose (G1), maltose (G2), isomaltose (isoG2), maltotriose (G3), or maltotetraose (G4), have been refined at around 1.7-1.9A resolution by using a synchrotron radiation source at SPring-8 [2].
• Due to its structural similarity to maltotetraose, we have investigated whether acarbose is recognized as a substrate by the maltose/maltodextrin system of Escherichia coli [3].
• Isolation of maltotetraose from Streptomyces as an antibiotic against Erwinia carotovora [4].
• Studies on multiple forms of maltotetraose-forming amylase from Alcaligenes sp [5].

Psychiatry related information on maltotetraose

• Malto-oligosaccharides ranging from maltotetraose to maltoheptaose were also hydrolyzed; however, maltotriose and maltose were not hydrolyzed even with a prolonged reaction time [6].

High impact information on maltotetraose

• Mutants lacking amylomaltase (encoded by malQ), the major maltose utilizing enzyme, cannot grow on maltose, maltotriose, or maltotetraose, despite the fact that they contain an effective transport system and MalZ [7].
• In the crystals soaked in alpha-cyclodextrin and maltoheptaose, a maltotetraose molecule is observed to bind in the active site [8].
• The genetic structure of the locus reveals the presence of an upstream gene necessary for growth on maltotetraose medium (malA) [9].
• The OE2 carboxyl of Glu 186 is below the plane of the penultimate glucose residue (Glc 2) of bound maltotetraose, 2.6 A from the oxygen atom of that ligand's penultimate alpha-1,4-glucosidic linkage [10].
• All three were similar in amino acid composition, pH optimum, substrate specificity, calcium requirement, heat inactivation, and Km for maltotetraose substrate [11].

Chemical compound and disease context of maltotetraose

• Maltohexaose producing amylase (EC 3.2.1.-) is the fourth known exo-amylase, the three previously known being glucoamylase, beta-amylase and Pseudomonas stutzeri maltotetraose producing amylase [12].

Biological context of maltotetraose

• Hydrolysis of maltotetraose by human pancreatic alpha-amylase, with liquid-chromatographic determination of the products [13].
• Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19 [14].
• This was investigated by measuring breast-milk amylase activity by hydrolysis of maltotetraose in 63 English mothers of parity 1-5 and 107 Gambian mothers of parity 1-12 who were at various stages of lactation (0.5-27 mo) [15].
• Northern hybridization and S1 nuclease mapping revealed that the amyP gene coding for maltotetraose-forming amylase of Pseudomonas stutzeri MO-19 is transcribed as a monocistronic mRNA of 2.0 kilobases and that the transcription start site is located 81 base pairs upstream from the first nucleotide of the initiation codon [16].
• Maltotriose and maltotetraose inhibited the cyclisation reaction competitively, the inhibition kinetics pointing to the binding of two effector-molecules to the enzyme [17].

Anatomical context of maltotetraose

• Tris, maltotriose, maltotetraose, and maltopentaose were inhibitors of granulocyte neutral maltase [18].

Associations of maltotetraose with other chemical compounds

• The products of starch hydrolysis by B. ruminicola were even more complex, yielding glucose through maltotetraose, maltohexaose, and maltoheptaose but little maltopentaose [19].
• For the hydrolysis of maltotriose, Kii = 25(+/-8) mM, and maltotetraose, Kii = 30(+/-4) mM was found [20].
• The mode of action during hydrolysis of starch indicated an exo-acting type of amylolytic enzyme mainly producing maltohexaose and maltotetraose [21].
• In order to better understand the protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined at 2.0 A resolution with a final crystallographic R value of 0.163 for all data [22].
• The hydrolysis of substrates (maltoheptaose, maltopentaose, and maltotetraose) catalyzed by soybean beta-amylase [EC 3.2.1.2] at pH 5.4 and 25 degrees C was followed by monitoring small changes in the quenching of fluorescence due to tryptophan residues by the stopped-flow method [23].

Gene context of maltotetraose

• The pores of the C. crescentus porins are slightly larger than those of E. coli K-12, since maltotetraose supported growth of the C. crescentus malA mutant but failed to support growth of the E. coli lamB mutant [24].
• The malA mutant was unable to grow on maltodextrins larger than maltotetraose [24].
• FhuA delta335-355 rendered cells sensitive to sodium dodecyl sulfate and supported diffusion of maltotetraose and maltopentaose in a lamB mutant lacking the maltodextrin-specific channel in the outer membrane [25].
• Deletion of two C. crescentus genes homologous to the exbB exbD genes of Escherichia coli abolished [(14)C]maltodextrin binding and transport and growth on maltodextrins larger than maltotetraose [24].
• Sera supplemented with porcine or bovine pancreatic amylase gave significantly lower values when assayed by methods using maltotetraose as substrate than when assayed by methods using maltopentaose or other oligosaccharides as substrate [26].

Analytical, diagnostic and therapeutic context of maltotetraose

• Using X-ray crystallography, the structures were solved for TmCBM41 in an uncomplexed form and in complex with maltotetraose and 6(3)-alpha-d-glucosyl-maltotriose (GM3) [27].
• In contrast, titrations with maltotetraose reveal three conformations: ligand-free, a low-affinity liganded state, and a high affinity liganded state [28].
• Based on the electrophoretic homogeneity of the purified three bands and the enzymatic activities identified by a thin layer chromatography of the soluble starch hydrolysates, all the three bands were confirmed to be maltotetraose-forming amylase but in multiple forms [5].
• Immobilization of alpha-amylase results in the formation of less polymerized products resulting in an apparent decrease in the number of transglycosylation reactions, for both maltotetraose and starch as substrates, when compared with free enzyme [29].
• Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri [30].

References