6-PHOSPHOGLUCONATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES
- 1 December 1955
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 70 (6) , 730-734
- https://doi.org/10.1128/jb.70.6.730-734.1955
Abstract
A 6-phosphogluconate dehydrogenase from L. mesenteroides was purified partially and characterized. The rate of diphospho-pyridine nucleotide (DPN) reduction is 25 times greater than that of triphosphpyridine nucleotide (TPN). Stimulation of enzymatic activity by Mg++ was demonstrable after dialysis against 0.04 [image] glycylglycine at pH 7.5. Dissociation constants were 7.78 x 10-5 [image] 6-phosphoglyconate, and 3.5 x 10-5 [image] DPN. The role of the enzyme is discussed in relation to the hexosemonophosphate pathways described for yeast and Escherichia coli.Keywords
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