Inhibition of alpha-aminoadipate-semialdehyde dehydrogenase from Trichosporon adeninovorans by lysine and lysine analogues.
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.
Schmidt
H
H
Institut für Biochemie, Ernst-Moritz-Arndt-Universität, Greifswald, G.D.R.
Bode
R
R
Birnbaum
D
D
D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D001667:Binding, Competitive; D003545:Cysteine / Q000031:analogs & derivatives / Q000494:pharmacology; D005971:Glutamates / Q000494:pharmacology; D018698:Glutamic Acid; D006901:Hydroxylysine / Q000494:pharmacology; D007700:Kinetics; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine / Q000031:analogs & derivatives / Q000494:pharmacology*; D003904:Mitosporic Fungi / Q000201:enzymology*; D014250:Trichosporon / Q000187:drug effects / Q000201:enzymology*
D005971:Glutamates; C000204:S-2-aminoethyl cysteine; D006901:Hydroxylysine; D018698:Glutamic Acid; D000445:Aldehyde Oxidoreductases; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine; D003545:Cysteine