Inhibition of α-aminoadipate-semialdehyde dehydrogenase from Trichosporon adeninovorans bvy lysine and lysine analogues |
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Authors: | H. Schmidt R. Bode D. Birnbaum |
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Affiliation: | Institut für Biochemie, Ernst-Moritz-Arndt-Universit?t, Greifswald, G.D.R. |
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Abstract: | The alpha-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) of Trichosporon adeninovorans, an enzyme of lysine biosynthesis, was partially 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 0.78 mM for alpha-aminoadipate, 1.0 mM for ATP, 0.23 mM for NADPH and 0.77 mM for MgCl2. It is demonstrated that the enzyme can be regulated by lysine and lysine analogues. L-Lysine (Ki of 0.09 mM), S-(beta-aminoethyl)-L-cysteine (Ki of 0.007 mM) and delta-hydroxylysine (Ki of 1.65 mM) inhibited the enzyme activity. The inhibition was competitive with respect to alpha-aminoadipate and non-competitive with respect to both ATP and NADPH. |
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Keywords: | Lysine biosynthesis α-Aminodipate-semialdehyde dehydrogenase Trichosporon adeninovorans |
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