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    Biochem Biophys Res Commun. 1992 Nov 30;189(1):450-4.

    Purification and characterization of bovine brain gamma-aminobutyraldehyde dehydrogenase.

    Lee JE, Cho YD.

    Department of Biochemistry, College of Science, Yonsei University, Seoul, Korea.

    gamma-Aminobutyraldehyde dehydrogenase was purified to homogeneity from bovine brain. The molecular weight of the native enzyme and subunit were 230,000 and 58,000, respectively. The Km value for gamma-aminobutyraldehyde and NAD+ were 154 microM and 53 microM, respectively. The optimum pH and temperature were 8.0 and 37 degrees C, respectively. N-terminal sequence of the enzyme is as follows: NH2-S-A-A-T-Q-A-V-P-T-P-N-Q-Q-COOH. The enzyme migrates on isoelectric focusing with pI = 6.5. Enhancement of the enzyme activity by polyamine, Mn2+, Mg2+ and inhibition by gamma-aminobutyric acid and Zn2+ will enhance the limited information on regulation of the gamma-ABALDH activity and GABA metabolism to some extent.

    PMID: 1449496 [PubMed - indexed for MEDLINE]

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