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dihydroxy-acid dehydratase
dihydroxy-acid dehydratase catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis
This protein, dihydroxy-acid dehydratase, catalyzes the fourth step in valine and isoleucine biosynthesis. Family members from spinach and from Mycobacterium tuberculosis were shown to contains catalytically essential [2Fe-2S] cluster, while in older work, the enzyme from Escherichia coli was interpreted as containing a [4Fe-4S] cluster.
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