Maltose Phosphorylase

<strong>Maltose Phosphorylase</strong> <strong>Catalog number:</strong> B2020187 <strong>Lot number:</strong> Batch Dependent <strong>Expiration Date:</strong> Batch dependent <strong>Amount:</strong> 1 kU <strong>Molecular Weight or Concentration:</strong> 220 kDa <strong>Supplied as:</strong> Lyophilized <strong>Applications:</strong> a molecular tool for various biochemical applications <strong>Storage:</strong> -20C <strong>Keywords:</strong> MPL-EP, Maltose : orthophosphate 1-_-D-glucosyltransferase <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um. <strong>References:</strong> 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. 2: Hüwel 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. 3: Li G, Wei X, Wu R, Zhou W, Li Y, Zhu Z, You C. Stoichiometric Conversion of Maltose for Biomanufacturing by In Vitro Synthetic Enzymatic Biosystems Biodes Res. 2022 Jul 1;2022:9806749. 4: 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. 5: Le Breton Y, Pichereau V, Sauvageot N, Auffray Y, Rincé A. Maltose utilization in Enterococcus faecalis J Appl Microbiol. 2005;98(4):806-13. 6: 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. 7: Nakai H, Petersen BO, Westphal Y, Dilokpimol A, Abou Hachem M, Duus JØ, 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. 8: Isono N, Yagura S, Yamanaka K, Masuda Y, Mukai K, Katsuzaki H. Enzymatic synthesis of _-d-fructofuranosyl _-d-glucopyranosyl-(1_2)-_-d-glucopyranoside using Escherichia coli glycoside phosphorylase YcjT Biosci Biotechnol Biochem. 2023 Sep 21;87(10):1249-1253. 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. <a href="https://pubmed.ncbi.nlm.nih.gov/12596853">10: 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. </a> <br><strong>Products Related to Maltose Phosphorylase can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>