AI Article Synopsis
- Shikimate kinase II was isolated from a genetically modified E. coli strain that produced high amounts of the enzyme.
- Its Km values indicate a strong affinity for shikimate (200 µM) and ATP (160 µM), with shikimate kinase II showing much higher affinity for shikimate compared to shikimate kinase I.
- The enzyme requires metal ions to function properly in the aromatic biosynthesis pathway.
Article Abstract
Shikimate kinase II was purified to near homogeneity from an Escherichia coli strain which overproduced the enzyme. The apparent Km of this isoenzyme for shikimate was 200 microM, and for ATP it was 160 microM. The Km for shikimate is approximately 100-fold lower than the Km of shikimate kinase I, suggesting that shikimate kinase II is the isoenzyme normally functioning in aromatic biosynthesis. Shikimate kinase II is dependent on metal ions for activity.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC214414 | PMC |
| http://dx.doi.org/10.1128/jb.165.1.331-333.1986 | DOI Listing |
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