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- W2014336754 abstract "A soluble enzyme that catalyzes the oxidation of l-α-aminoadipate δ-emialdehyde to l-α-aminoadipic acid in the presence of NAD+ has been isolated and characterized from human liver. This enzyme l-α-aminoadipic δ-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-α-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-α-aminoadipate δ-semialdebyde were shown to be 181 μM and 71.4 pmol·min−1·mg−1, respectively, and for its coenzyme NAD+ to be 454 μM and 142.9 pmol·min−1·mg−1, respectively. The characteristics of the oxidoreductase obtained from the human liver and Pseudomonan putida were compared." @default.
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- W2014336754 title "l-Pipecolic acid metabolism in human liver: l-α-aminoadipate δ-semialdehyde oxidoreductase" @default.
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- W2014336754 doi "https://doi.org/10.1016/0167-4838(90)90241-7" @default.
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