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• W2032193721 abstract "A phosphatase has been purified 1767-fold, to a final specific activity of 53.0 (μmol pyruvate produced per min per mg protein), from the bulb of Allium cepa L. The enzyme has high specificity for a phosphoenolpyruvate (PEP) substrate. The molecular mass of the enzyme is approximately 240 kDa, as determined by gel column chromatography. Although 52 and 42 kDa polypeptides were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), their N-terminal amino acid sequences were the same. We deduce, therefore, that the enzyme consists of four polypeptide subunits of 52 kDa. The purified enzyme hydrolyzes a wide variety of phosphate esters, and the lowest Km was obtained with PEP (0.44 mM). The enzyme consumed 1 mol of PEP, with the release of 1 mol of phosphate and 1 mol of pyruvate, with no ATP formation during the enzymatic reaction in the presence of ADP and Mg2+. Therefore, the enzyme is thought to be a PEP phosphatase. A cDNA that encodes PEP phosphatase, the deduced amino acid sequence of which resembles that of the plant acid phosphatases, was also isolated from onion bulb RNA." @default.
• W2032193721 created "2016-06-24" @default.
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• W2032193721 date "2001-10-01" @default.
• W2032193721 modified "2023-09-26" @default.
• W2032193721 title "Characteristics of phosphoenolpyruvate phosphatase purified from Allium cepa" @default.
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• W2032193721 doi "https://doi.org/10.1016/s0168-9452(01)00480-0" @default.
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