Abstract
The β-isopropylmalate (IPM) dehydrogenase (EC 1.1.1.85) ofCandida maltosa, the third pathway-specific enzyme of leucine biosynthesis, was purified, some properties of the enzyme were studied and a novel regulatory pattern was found. The Km values of the enzyme were estimated to be 0.42 mM for β-IPM and 0.34 mM for NAD+. It is demonstrated that the enzyme can be regulated by L-valine. The inhibition was competitive with respect to β-IPM (Ki=1.84 mM) and non-competitive with respect to NAD+ (Ki=5.67 mM). Exogenous addition of L-valine toC. maltosa cells increased the intracellular pool of some intermediates of leucine biosynthesis (α-ketoisovalerate, α-IPM, β-IPM), but has hardly influence on the leucine pool.
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Bode, R. Valine inhibition of β-isopropylmalate dehydrogenase takes part in the regulation of leucine biosynthesis inCandida maltosa . Antonie van Leeuwenhoek 60, 125–130 (1991). https://doi.org/10.1007/BF00572702
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DOI: https://doi.org/10.1007/BF00572702