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- W2024063904 abstract "L-Aspartate 4-carboxy-lyase of Cunninghamella elegans and Penicillium citrinum has a pH optimum of 5.5. Maximal activity of both enzymes is obtained at 40 degrees C, and both are thermolabile. The Km of the C. elegans enzyme for L-aspartate is 25 mM, while that of the P. citrinum enzyme is 27 mM. The two enzymes are specific for L-aspartate. They are activated by pyridoxal 5-phosphate and a number of alpha-keto acids. The catalytic activity of both enzymes is stimulated by Co2+, Fe2+, Ni2+ and Mn2+ ions and inhibited by Zn2+ and Cu2+. Inhibition by iodoacetate and activation by SH-compounds suggest that sulfhydryl groups may participate in enzyme activity." @default.
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- W2024063904 date "1994-09-01" @default.
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- W2024063904 title "Comparison of L-aspartate 4-carboxy-lyases ofCunninghamella elegansandPenicillium citrinum" @default.
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- W2024063904 doi "https://doi.org/10.1016/s0944-5013(11)80066-2" @default.
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