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Characterization of succinic semialdehyde dehydrogenase from Aspergillus niger.
Indian J Exp Biol ; 2015 Feb; 53(2): 67-74
Article in English | IMSEAR | ID: sea-158377
ABSTRACT
The catabolism of fungal 4-aminobutyrate (GABA) occurs via succinic semialdehyde (SSA). Succinic semialdehyde dehydrogenase (SSADH) from the acidogenic fungus Aspergillus niger was purified from GABA grown mycelia to the highest specific activity of 277 nmol min-1 mg-1, using phenyl Sepharose and DEAE Sephacel chromatography. The purified enzyme was specific for its substrates SSA and NAD+. The substrate inhibition observed with SSA was uncompetitive with respect to NAD+. While product inhibition by succinate was not observed, NADH inhibited the enzyme competitively with respect to NAD+ and noncompetitively with respect to SSA. Dead-end inhibition by AMP and p-hydroxybenzaldehyde (pHB) was analyzed. The pHB inhibition was competitive with SSA and uncompetitive with NAD+; AMP competed with NAD+. Consistent with the kinetic data, a sequential, ordered Bi Bi mechanism is proposed for this enzyme.
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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Protein Binding / Aspergillus niger / Substrate Specificity / Benzaldehydes / Binding, Competitive / Fungal Proteins / Kinetics / Adenosine Monophosphate / Mycelium / Succinate-Semialdehyde Dehydrogenase Language: English Journal: Indian J Exp Biol Year: 2015 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Protein Binding / Aspergillus niger / Substrate Specificity / Benzaldehydes / Binding, Competitive / Fungal Proteins / Kinetics / Adenosine Monophosphate / Mycelium / Succinate-Semialdehyde Dehydrogenase Language: English Journal: Indian J Exp Biol Year: 2015 Type: Article