Abstract:
:Succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of γ-aminobutyric acid degradation. Here, we characterized Bacillus subtilis SSADH (BsSSADH) regarding its cofactor discrimination and substrate inhibition. BsSSADH showed similar values of the catalytic efficiency (kcat/Km) in both NAD(+) and NADP(+) as cofactors, and exhibited complete uncompetitive substrate inhibition at higher SSA concentrations. Further analyses of the sequence alignment and homology modeling indicated that the residues of catalytic and cofactor-binding sites in other SSADHs were highly conserved in BsSSADH.
journal_name
J Microbiol Biotechnoljournal_title
Journal of microbiology and biotechnologyauthors
Park SA,Park YS,Lee KSdoi
10.4014/jmb.1402.02054subject
Has Abstractpub_date
2014-07-01 00:00:00pages
954-8issue
7eissn
1017-7825issn
1738-8872pii
10.4014/jmb.1402.02054journal_volume
24pub_type
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