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KMID : 0380219940270010075
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 1 p.75 ~ p.79
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Purification and Properties of Succinic Semialdehyde Dehydrogenase from Lumbricus rubellus
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Abstract
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Abstract:
@EN Succinic semialdehyde dehydrogenase (EC 1.2.1.24) from Lumbricus rubellus was purified to homogeneity by a combination of DEAE Sepharose, Blue Sepharose and AMP-Sepharose chromatography. The purified enzyme is a dimeric protein composed of
identical
subunits with a molecular weight of 56.000 daltons. Optimum pH for the enzymatic reaction was 9.5and Km value of the enzyme for succinic semialdehyde was 1 μM. Studies on substrate specificity revealed that aromatic aldehyde has lower Km value
(20
to
40 μM) than short chain aliphatic aldehyde(0.5 to 1 mM). Succinic semialdehyde dehydrogenase was sensitive to inhibition by the alcohol aversive drug disulfiram and by the thiol-blocking reagent 5,5-dithiobis (2-nitrobenzoic acid). The catalytic
function of the enzyme was also inactivated by pyridoxal-5'-phosphate. However, the presence of NAD+ in the reaction mixture could protect enzyme against the inactivation.
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KEYWORD
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