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- W2357862535 abstract "A malic enzyme from a cell-free extract of Pseudomonas diminuta IFO-13182 was purified to electrophoretic homogeneity by DEAE-Sepharose, Sephacryl, and Blue-Sepharose chromatographies. The purified enzyme required either NAD+ or NADP+ as a coenzyme. From the results of coenzyme specificity, the enzyme should be classified as l-malate: NAD+ oxidoreductase (decarboxylating) [EC 1.1.1.39]. The purified enzyme was most active at pH 7.5 and 50°C and was stable in the pH range from 7.0 to 9.0. The isoelectric point was pH 4.3. Its molecular weight was 680,000 by COSMOSIL 5-Diol high performance liquid gel filtration on chromatography and 65,000 by SDS polyacrylamide gel electrophoresis. This indicates that the enzyme consisted of 10 subunits. The malic enzyme activity with NADP+ was about twice that measured with NAD+." @default.
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- W2357862535 date "1967-12-01" @default.
- W2357862535 modified "2023-09-26" @default.
- W2357862535 title "Allosteric activation of DPN-linked malic enzyme from Escherichiacoli by aspartate" @default.
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- W2357862535 doi "https://doi.org/10.1016/0006-291x(67)90276-8" @default.
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