Valine inhibition of beta-isopropylmalate dehydrogenase takes part in the regulation of leucine biosynthesis in Candida maltosa.
The beta-isopropylmalate (IPM) dehydrogenase (EC 1.1.1.85) of Candida 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 beta-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 beta-IPM (Ki = 1.84 mM) and non-competitive with respect to NAD+ (Ki = 5.67 mM). Exogenous addition of L-valine to C. maltosa cells increased the intracellular pool of some intermediates of leucine biosynthesis (alpha-ketoisovalerate, alpha-IPM, beta-IPM), but has hardly influence on the leucine pool.
Bode
R
R
Institut für Biochemie, Ernst-Moritz-Arndt-Universität Greifswald, Germany.
D050539:3-Isopropylmalate Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000378:metabolism; D002175:Candida / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D007930:Leucine / Q000096:biosynthesis*; D014633:Valine / Q000494:pharmacology*
D000429:Alcohol Oxidoreductases; D050539:3-Isopropylmalate Dehydrogenase; D007930:Leucine; D014633:Valine