L-PIPECOLIC ACID METABOLISM IN HUMAN LIVER - L-ALPHA-AMINOADIPATE DELTA-SEMIALDEHYDE OXIDOREDUCTASE

被引：32

作者：

CHANG, YF

GHOSH, P

RAO, VV

机构：

[1] Department of Biochemistry, University of Maryland, Dental School, Baltimore, MD

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1038卷 / 03期

关键词：

l-α-Aminoadipate δ-semialdehyde oxidoreductase; l-α-Aminoadipic acid; Lysine metabolism; Peroxisome defect; Pipecolic acid metabolism; Zellweger syndrome;

D O I：

10.1016/0167-4838(90)90241-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1990.

引用

页码：300 / 305

页数：6

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