Chang Y F, Ghosh P, Rao V V
Department of Biochemistry, University of Maryland, Dental School, Baltimore 21201.
Biochim Biophys Acta. 1990 May 8;1038(3):300-5. doi: 10.1016/0167-4838(90)90241-7.
A soluble enzyme that catalyzes the oxidation of L-alpha-aminoadipate delta-semialdehyde to L-alpha-aminoadipic acid in the presence of NAD+ has been isolated and characterized from human liver. This enzyme L-alpha-aminoadipic delta-semialdehyde oxidoreductase has been found to be localized in the cytosol using subcellular fractionation and marker enzyme assays. The reaction product of this enzyme has been identified as L-alpha-aminoadipic acid by use of an amino acid analyzer and thin layer chromatography. The enzymatic reaction was irreversible and has a pH optimum of 8. The enzyme was stimulated by Mg2+, Cu2+ and Mn2+, and has a requirement of free -SH groups. The Km and Vmax values for its substrate L-alpha-aminoadipate delta-semialdehyde were shown to be 181 microM and 71.4 pmol.min-1.mg-1, respectively, and for its coenzyme NAD+ to be 454 microM and 142.9 pmol.min-1.mg-1, respectively. The characteristics of the oxidoreductase obtained from the human liver and Pseudomonas putida were compared.
