Characterization of succinic semialdehyde dehydrogenase from aspergillus niger

Santosh Kumar, Sunil Kumar, Narayan S. Punekar

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)67-74
Number of pages8
JournalIndian Journal of Experimental Biology
Volume53
Issue number2
StatePublished - Jan 1 2015

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Succinate-Semialdehyde Dehydrogenase
Aspergillus niger
NAD
Adenosine Monophosphate
gamma-Aminobutyric Acid
Enzymes
Aminobutyrates
Mycelium
Succinic Acid
Chromatography
Fungi
succinic semialdehyde

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Molecular Biology
  • Cell Biology

Cite this

Characterization of succinic semialdehyde dehydrogenase from aspergillus niger. / Kumar, Santosh; Kumar, Sunil; Punekar, Narayan S.

In: Indian Journal of Experimental Biology, Vol. 53, No. 2, 01.01.2015, p. 67-74.

Research output: Contribution to journalArticle

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