ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract The α-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 α-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-(B-aminoethyl)-l-cysteine (Ki of 0.007 mM and δ-hydroxylysine (Ki of 1.65 mM) inhibited the enzyme activity. The inhibition was competitive with respect to α-aminodipate and non-competitive with respect to both ATP and NADPH.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1990.tb03774.x
