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- W1131504674 abstract "Publisher Summary This chapter describes the purification and properties of the enzyme 2-Keto-3-deoxy-D-xylonate aldolase that functions in the metabolism of D-xylose, and, presumably, other D-pentoses in a pseudomonad designated “MSU-I.” The continuous spectrophotometric assay measures the rate of pyruvate formation by coupling the reaction to lactate dehydrogenase. With the coupling enzyme in excess, the rate of 2-keto-3-deoxy-D-xylonate cleavage is equal to the rate of NADH oxidation as monitored at 340 nm. The purification process involves protamine sulfate treatment, ammonium sulfate fractionation, and chromatography on Sephadex G-200. Aldolase activity as a function of pH is maximal in the pH range of 7.4–8.2. The aldolase requires a divalent cation for activity when assayed in the presence of EDTA. The aldolase is insensitive to borohydride reduction, whether in the presence of pyruvate, glycolaldehyde, or 2-keto-3-deoxy-D-xylonate. The aldolases are specific for their respective enantiomeric 3-deoxypentulosonic acid substrates, have similar pH optima and equilibrium constants, and are unaffected by borohydride in the presence of either substrate or individual cleavage products." @default.
- W1131504674 created "2016-06-24" @default.
- W1131504674 creator A5035985862 @default.
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- W1131504674 date "1982-01-01" @default.
- W1131504674 modified "2023-09-27" @default.
- W1131504674 title "[42] 2-Keto-3-deoxy-d-xylonate aldolase (3-deoxy-d-pentulosonic acid aldolase)" @default.
- W1131504674 cites W1499107772 @default.
- W1131504674 cites W1775749144 @default.
- W1131504674 doi "https://doi.org/10.1016/s0076-6879(82)90138-0" @default.
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- W1131504674 hasPublicationYear "1982" @default.
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