Maltose Phosphorylase from Enterococcus sp

<strong>Maltose Phosphorylase from Enterococcus sp</strong>_x000D_ <strong>Catalog number:</strong> B2013883_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 250 units_x000D_ <strong>Molecular Weight or Concentration:</strong> 90 kDa_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> Maltose:orthophosphate 1-β-D-Glucosyltransferase_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Gao Y, Saburi W, Taguchi Y, Mori H. Biochemical characteristics of maltose phosphorylase MalE from Bacillus sp. AHU2001 and chemoenzymatic synthesis of oligosaccharides by the enzyme Biosci Biotechnol Biochem. 2019 Nov;83(11):2097-2109._x000D_ 2: H_wel S, Haalck L, Conrath N, Spener F. Maltose phosphorylase from Lactobacillus brevis: purification, characterization, and application in a biosensor for ortho-phosphate Enzyme Microb Technol. 1997 Nov 1;21(6):413-20._x000D_ 3: Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H. Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases Structure. 2001 Aug;9(8):689-97._x000D_ 4: Inoue Y, Ishii K, Tomita T, Fukui F. Purification and characterization of maltose phosphorylase from Bacillus sp. RK-1 Biosci Biotechnol Biochem. 2001 Dec;65(12):2644-9._x000D_ 5: Inoue Y, Yasutake N, Oshima Y, Yamamoto Y, Tomita T, Miyoshi S, Yatake T. Cloning of the maltose phosphorylase gene from Bacillus sp. strain RK-1 and efficient production of the cloned gene and the trehalose phosphorylase gene from Bacillus stearothermophilus SK-1 in Bacillus subtilis Biosci Biotechnol Biochem. 2002 Dec;66(12):2594-9._x000D_ 6: H_wel S, Haalck L, Conrath N, Spener F. Production and stabilization of pure maltose phosphorylase from Lactobacillus brevis for sensing inorganic phosphate Ann N Y Acad Sci. 1996 Oct 12;799:701-6._x000D_ 7: Nakai H, Petersen BO, Westphal Y, Dilokpimol A, Abou Hachem M, Duus J, Schols HA, Svensson B. Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase Protein Eng Des Sel. 2010 Oct;23(10):781-7._x000D_ 8: de Kok S, Yilmaz D, Suir E, Pronk JT, Daran JM, van Maris AJ. Increasing free-energy (ATP) conservation in maltose-grown Saccharomyces cerevisiae by expression of a heterologous maltose phosphorylase Metab Eng. 2011 Sep;13(5):518-26._x000D_ 9: Tsumuraya Y, Brewer CF, Hehre EJ. Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzyme's glucosyltransferase activity Arch Biochem Biophys. 1990 Aug 15;281(1):58-65._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/22940176">10: Nihira T, Saito Y, Kitaoka M, Otsubo K, Nakai H. Identification of Bacillus selenitireducens MLS10 maltose phosphorylase possessing synthetic ability for branched -D-glucosyl trisaccharides Carbohydr Res. 2012 Oct 1;360:25-30. </a>_x000D_ _x000D_ <strong>Products Related to Maltose Phosphorylase from Enterococcus sp can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>