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Literature summary for 1.2.1.24 extracted from

  • Rothacker, B.; Ilg, T.
    Functional characterization of a Drosophila melanogaster succinic semialdehyde dehydrogenase and a non-specific aldehyde dehydrogenase (2008), Insect Biochem. Mol. Biol., 38, 354-366.
    View publication on PubMed
Search for more literature for 1.2.1.24

Cloned(Commentary)

Cloned (Comment) Organism
PCR product cloned into pCR2.1-Topo. Open reading frame ligated into vector QE30. Overexpressed in Escherichia coli M15. Subcloned into pMALc2x and expressed in Escherichia coli TB1 Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
C196A loss in specific activity of 55% Drosophila melanogaster
C196S loss in specific activity of 74% Drosophila melanogaster
C243S loss in specific activity of 70% Drosophila melanogaster
C311A decreased SSADH activity to undetectable levels Drosophila melanogaster
C311S decreased SSADH activity to undetectable levels Drosophila melanogaster
C502S loss in specific activity of 93% Drosophila melanogaster
E277D leads to a product with similar specific activity Drosophila melanogaster
E277K charge inversion, which results in recombinant protein totally devoid of detectable SSADH activity Drosophila melanogaster
E277Q concomitant loss of the negative charge, which results in recombinant protein totally devoid of detectable SSADH activity Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0047
-
 succinate semialdehyde
-
 Drosophila melanogaster
0.051
-
 n-hexanal
-
 Drosophila melanogaster
0.057
-
 n-Pentanal
-
 Drosophila melanogaster
0.0909
-
 NAD+
-
 Drosophila melanogaster
0.106
-
 n-Butanal
-
 Drosophila melanogaster
1.2
-
 NADP+
-
 Drosophila melanogaster

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
98200
-
 x * 98200, SDS-PAGE Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q9VBP6
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni2+-NTA agarose chromatography Drosophila melanogaster

Storage Stability

Storage Stability Organism
0°C, 100 mM sodium phosphate, pH 8.5, 1mM DTT, 43% glycerol, 3 years Drosophila melanogaster

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
m-carboxybenzaldehyde + NAD+ + H2O
-
 Drosophila melanogaster m-carboxybenzoate + NADH + H+
-
 ?
m-methylcarboxybenzaldehyde + NAD+ + H2O
-
 Drosophila melanogaster m-methylcarboxybenzoate + NADH + H+
-
 ?
additional information no activity with formaldehyde, o-nitrobenzaldehyde, o-carboxybenzaldehyde, o-tolualdehyde, p-tolualdehyde, o-methoxybenzaldehyde, p-methoxybenzaldehyde o-hydroxybenzaldehyde, m-hydroxybenzaldehyde, phenylacetaldehyde and glyoxylic acid Drosophila melanogaster ?
-
 ?
n-butanal + NAD+ + H2O
-
 Drosophila melanogaster butanoate + NADH + H+
-
 ?
n-hexanal + NAD+ + H2O
-
 Drosophila melanogaster hexanoate + NADH + H+
-
 ?
n-octanal + NAD+ + H2O
-
 Drosophila melanogaster n-octanoate + NADH + H+
-
 ?
n-pentanal + NAD+ + H2O
-
 Drosophila melanogaster n-pentanoate + NADH + H+
-
 ?
succinate semialdehyde + NAD(P)+ + H2O cysteine 311 and glutamic acid 277 are likely candidates for the active site residues directly involved in catalysis Drosophila melanogaster succinate + NAD(P)H + H+
-
 ?

Subunits

Subunits Comment Organism
? x * 98200, SDS-PAGE Drosophila melanogaster

Synonyms

Synonyms Comment Organism
SSADH
-
 Drosophila melanogaster
succinic semialdehyde dehydrogenase
-
 Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 optimal expression of pMalc2x-DmSSADH in Escherichia coli TB1 Drosophila melanogaster

pH Range

pH Minimum pH Maximum Comment Organism
6 8.5 at pH 8.5 MalE-DmSSADH is 10fold more active than at pH 6.0 Drosophila melanogaster

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Drosophila melanogaster
NADP+ is also accepted as coenzyme substrate but leads to 7fold lower reaction rates compared to NAD+ at saturating succinate semialdehyde concentrations Drosophila melanogaster