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- W2074430711 abstract "A novel enzyme catalyzing the phosphorylation of d-tagatose to d-tagatose 6-phosphate with ATP has been identified in extracts of dulcitol-grown Mycobacterium butyricum. The enzyme was purified 100-fold with 29% recovery. It required Mg2+, Mn2+ or Fe2+ and showed maximum activity at pH 7.5. The molecular weight as determined by Sephadex G-100 filtration amounted to 63 000. The apparent Michaelis constants for d-tagatose and ATP were 0.8 and 1.0 mM, respectively. Apart from tagatose, none of 14 common sugars including fructose and sorbose served as a substrate. The enzyme preparations were not very sensitive to SH group inhibitors and heavy metals but rapidly lost activity on heating above 50°C." @default.
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- W2074430711 date "1981-08-01" @default.
- W2074430711 modified "2023-09-27" @default.
- W2074430711 title "A novel enzyme, tagatose kinase, from Mycobacterium butyricum" @default.
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- W2074430711 doi "https://doi.org/10.1016/0005-2744(81)90182-0" @default.
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