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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Studies on analogues of succinic semialdehyde as substrates for succinate semialdehyde dehydrogenase from rat brain.

The methyl ester of succinic semialdehyde (SSA) was examined as a substrate for succinate semialdehyde dehydrogenase (SSADH) from rat brain. It was found that the ester can be oxidized by the enzyme. Values of Km for SSA-Me were higher than for those for SSA, and for this substrate the enzyme showed a substrate-dependent inhibition. This finding suggests that the carboxylate group of SSA is not essential in the process of inhibition of SSADH by the substrate. Cyclopropyl analogues of SSA, cis- and trans-1-formyl-cyclopropan-2-carboxylic acids, were also individually tested as substrates of SSADH. Only the trans isomer was found to be oxidized to the corresponding dicarboxylic acid; it inhibited the enzyme in the same range of concentrations as SSA. The above data suggest that, as for gamma-aminobutyric acid, SSA is present in an unfolded, transoid conformation at the active site of SSADH.[1]

References

  1. Studies on analogues of succinic semialdehyde as substrates for succinate semialdehyde dehydrogenase from rat brain. Manzocchi, A., Biondi, P., Secchi, C., Santaniello, E. J. Neurochem. (1986) [Pubmed]
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