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2,5-dioxopentanoate + NAD+ + H2O
?
no activity in presence of NADP+
-
-
?
2-carboxybenzaldehyde + NAD+ + H2O
2-carboxybenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + H+
about 3% activity compared to succinate semialdehyde
-
-
?
2-phenylacetaldehyde + NAD+ + H2O
2-phenylbenzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
-
-
?
2-tolualdehyde + NAD+ + H2O
2-carboxytoluene + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
low activity
-
-
?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH
-
low activity
-
-
?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
4-hydroxy-trans-2-nonenal + NAD+
?
-
elevated levels of 4-hydroxy-trans-2-nonenal are implicated in the pathogenesis of numerous neurodegenerative disorders. Succinate-semialdehyde dehydrogenase is the predominant oxidizing enzyme for 4-hydroxy-trans-2-nonenal but only contributes a portion of the total oxidizing activity in liver mitochondria
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
alpha-ketoglutaric semialdehyde + NAD+ + H2O
alpha-ketoglutarate + NADH
-
-
-
?
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH
-
-
-
?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
betaine aldehyde + NAD+ + H2O
2-trimethylammonioacetate + NADH
-
-
-
?
butanal + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
-
-
-
-
?
butanaldehyde + NAD+ + H2O
butanoate + NADH
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH
-
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
glyceraldehyde + NAD+ + H2O
glycerate + NADH
-
-
-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH
-
-
-
?
glyoxylic acid + NAD+ + H2O
2-phenylbenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
heptanaldehyde + NAD+ + H2O
heptanoate + NADH
-
-
-
?
hexanaldehyde + NAD+ + H2O
hexanoate + NADH
-
-
-
?
iso-butanal + NAD+ + H2O
? + NADH + H+
less than 10% activity compared to succinate semialdehyde
-
-
?
iso-butanal + NAD+ + H2O
isobutanoate + NADH + H+
-
less than 10% activity compared to succinate semialdehyde
-
-
?
iso-pentanal + NAD+ + H2O
? + NADH + H+
about 2% activity compared to succinate semialdehyde
-
-
?
iso-pentanal + NAD+ + H2O
isopentanoate + NADH + H+
-
less than 5% activity compared to succinate semialdehyde
-
-
?
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
-
-
-
?
m-carboxybenzaldehyde + NAD+ + H2O
m-carboxybenzoate + NADH + H+
-
-
-
?
m-methylcarboxybenzaldehyde + NAD+ + H2O
m-methylcarboxybenzoate + NADH + H+
-
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
-
4.3% of the activity with succinate semialdehyde
-
-
?
malonate semialdehyde + NAD+ + H2O
malonate + NADH + 2 H+
-
3.8% of the activity with succinate semialdehyde
-
-
?
methyl 3-formylbenzoate + NAD+ + H2O
3-(methoxycarbonyl)benzoate + NADH + H+
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
n-butanal + NAD+ + H2O
butanoate + NADH + H+
n-butanal + NAD+ + H2O
butanoic acid + NADH + 2 H+
-
about 11% of the rate with succinic semialdehyde
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
octanaldehyde + NAD+ + H2O
octanoate + NADH
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
pentanaldehyde + NAD+ + H2O
pentanoate + NADH
-
-
-
?
propanal + NAD(P)+ + H2O
propanoate + NAD(P)H + H+
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
propanaldehyde + NAD+ + H2O
propanoate + NADH
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
succinate semialdehyde + 3-acetylpyridine adenine dinucleotide + H2O
succinate + reduced 3-acetylpyridine adenine dinucleotide + H+
-
-
-
-
r
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
succinate semialdehyde + NAD+
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
trans-2-hexenal + NAD+ + H2O
trans-2-hexenoate + NADH + H+
-
-
-
-
?
additional information
?
-
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
-
-
-
-
?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
-
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
about 20% activity compared to succinate semialdehyde
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
-
about 35% activity compared to succinate semialdehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
about 2% activity compared to succinate semialdehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
about 3% activity compared to succinate semialdehyde
-
-
?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
-
-
?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
-
about 10% activity compared to succinate semialdehyde
-
-
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
about 3% activity compared to succinate semialdehyde
-
-
?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
-
about 10% activity compared to succinate semialdehyde
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
about 20% activity compared to succinate semialdehyde
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
-
about 15% activity compared to succinate semialdehyde
-
-
?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
-
-
-
-
?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
-
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
about 10% activity compared to succinate semialdehyde
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
-
about 65% activity compared to succinate semialdehyde
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
-
?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
-
-
?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
-
about 5% activity compared to succinate semialdehyde
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
about 15% activity compared to succinate semialdehyde
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
-
about 30% activity compared to succinate semialdehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
2.3% of the activity with succinate semialdehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
about 5% activity compared to succinate semialdehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
about 10% activity compared to succinate semialdehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
about 30% activity compared to succinate semialdehyde
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
-
13% of the activity with succinate semialdehyde
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
-
25% of the activity with succinate semialdehyde
-
-
?
methyl 3-formylbenzoate + NAD+ + H2O
3-(methoxycarbonyl)benzoate + NADH + H+
about 20% activity compared to succinate semialdehyde
-
-
?
methyl 3-formylbenzoate + NAD+ + H2O
3-(methoxycarbonyl)benzoate + NADH + H+
-
about 45% activity compared to succinate semialdehyde
-
-
?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
about 15% activity compared to succinate semialdehyde
-
-
?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
-
about 30% activity compared to succinate semialdehyde
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
about 10% activity compared to succinate semialdehyde
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
less than 60% activity compared to succinate semialdehyde
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
less than 10% activity compared to succinate semialdehyde
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
about 110% activity compared to succinate semialdehyde
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
-
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
less than 10% activity compared to succinate semialdehyde
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
-
less than 80% activity compared to succinate semialdehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
less than 20% activity compared to succinate semialdehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
100% activity
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
6.5% of the activity with succinate semialdehyde
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
-
-
-
?
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
-
-
-
-
?
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
less than 10% activity compared to succinate semialdehyde
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
less than 20% activity compared to succinate semialdehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
5% of the activity with succinate semialdehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
-
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
cysteine 311 and glutamic acid 277 are likely candidates for the active site residues directly involved in catalysis
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
last enzyme in catabolism of 4-aminobutyric acid. Human SSADH deficiency results in 4-hydroxybutyric aciduria, an autosomal recessive disorder due to an accumulation of 4-aminobutyric acid and 4-hydroxybutyric acid in the CNS
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme of agmatine degradation
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by succinate semialdehyde, functions in the oxidation of succinate semialdehyde during growth on both 4-hydroxyphenylacetate and 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by succinate semialdehyde, functions in the oxidation of succinate semialdehyde during growth on both 4-hydroxyphenylacetate and 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme may play an important role, not only in metabolizing succinate semialdehyde but also in oxidation of aromatic aldehydes in the soil environment
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
induced by pyridine, the enzyme is involved in the degradation of pyridine
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
reverse reaction proceeds at 1/1230 of the rate of the forward eaction
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is involved in the catabolism of the neurotransmitter 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
the enzyme is specific for the substrates
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
the enzyme is specific for the substrates
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
no activity in presence of NADP+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
enzyme of the gamma-aminobutyrate shunt required to restrict levels of reactive oxygen intermediates in plants
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
r
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
100% activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
100% activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
20% of the activity with NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
reduction rate is only a few percent of that of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
activity with NAD+ is 10times higher than with NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
activity with NAD+ is 10times higher than with NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
reaction with NADP+ is 13% of the activity with NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
activity with NAD+ is about 7fold higher than activity with NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
activity with NAD+ is about 7fold higher than activity with NADP+
-
-
ir
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive
-
-
?
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
-
-
?
additional information
?
-
-
no substrate: formaldehyde, acetaldehyde, glyoxal, glyoxalate, propanal, glutaraldehyde, benzaldehyde, and anisaldehyde
-
-
?
additional information
?
-
-
no substrate: glyoxylic acid, formic acid, formaldehyde, acetaldehyde, glyoxal, furfural and acrolein
-
-
?
additional information
?
-
deficiency of succinate semialdehyde dehydrogenase is a rare autosomal recessively inherited metabolic disorder that results in acumulation of 4-hydroxybutyrate. Functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency
-
-
?
additional information
?
-
-
ALDH5A1 plays an important role as a gamma-aminobutyric acid catabolic enzyme and potentially as a detoxifying enzyme involved in aldehyde scavenging
-
-
?
additional information
?
-
no activity towards 2-methoxybenzaldehyde, and 4-tolualdehyde
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
?
additional information
?
-
-
no activity towards 2-methoxybenzaldehyde, 2-nitrobenzaldehyde, 2-carboxybenzaldehyde, 2-tolualdehyde, 4-tolualdehyde, 2-hydroxybenzaldehyde, 4-hydroxybenzaldehyde, 2-phenylacetaldedyde, and glyoxylic acid
-
-
?
additional information
?
-
formaldehyde, betaine aldehyde and benzaldehyde can not serve as substrates
-
-
?
additional information
?
-
-
formaldehyde, betaine aldehyde and benzaldehyde can not serve as substrates
-
-
?
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4-aminobutyrate-2-oxoglutarate transaminase deficiency
4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency.
alcohol dehydrogenase deficiency
A boy with a severe phenotype of succinic semialdehyde dehydrogenase deficiency.
alcohol dehydrogenase deficiency
Circadian distribution of generalized tonic-clonic seizures associated with murine succinic semialdehyde dehydrogenase deficiency, a disorder of GABA metabolism.
alcohol dehydrogenase deficiency
Clinical diagnosis and mutation analysis of four Chinese families with succinic semialdehyde dehydrogenase deficiency.
alcohol dehydrogenase deficiency
Inherited disorders of gamma-aminobutyric acid metabolism and advances in ALDH5A1 mutation identification.
alcohol dehydrogenase deficiency
Metabolic Stroke: A Novel Presentation in a Child with Succinic Semialdehyde Dehydrogenase Deficiency.
alcohol dehydrogenase deficiency
Mutation analysis and prenatal diagnosis in a Chinese family with succinic semialdehyde dehydrogenase and a systematic review of the literature of reported ALDH5A1 mutations.
alcohol dehydrogenase deficiency
Novel ALDH5A1 variants and genotype: Phenotype correlation in SSADH deficiency.
alcohol dehydrogenase deficiency
SSADH deficiency in an Italian family: a novel ALDH5A1 gene mutation affecting the succinic semialdehyde substrate binding site.
Carcinoma, Intraductal, Noninfiltrating
RNA-Seq of human breast ductal carcinoma in situ models reveals aldehyde dehydrogenase isoform 5A1 as a novel potential target.
Cerebral Palsy
Bi-allelic Mutations in ALDH5A1 is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability.
Epilepsy
Polymorphisms of ABAT, SCN2A and ALDH5A1 may affect valproic acid responses in the treatment of epilepsy in Chinese.
Epilepsy, Generalized
Candidate gene analysis of the succinic semialdehyde dehydrogenase gene (ALDH5A1) in patients with idiopathic generalized epilepsy and photosensitivity.
Intellectual Disability
A novel ALDH5A1 mutation is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability in an Iranian family.
Intellectual Disability
Bi-allelic Mutations in ALDH5A1 is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability.
Ischemic Stroke
Metabolic Or Ischemic Stroke in Succinic Semi-Aldehyde Dehydrogenase Deficiency Due to the Homozygous Variant c. 1343 + 1_1343 + 3delGTAinsTT in ALDH5A1.
Ischemic Stroke
Metabolic or Ischemic Stroke in Succinic Semi-aldehyde Dehydrogenase Deficiency Due to the Homozygous Variant c. 1343 + 1_1343 + 3delGTAinsTT in ALDH5A1.
Metabolic Diseases
Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease.
Muscle Hypotonia
Novel mutations in a Chinese family with two patients with succinic semialdehyde dehydrogenase deficiency.
Neoplasm Metastasis
ALDH5A1 acts as a tumour promoter and has a prognostic impact in papillary thyroid carcinoma.
Neoplasms
Aldehyde dehydrogenases and cell proliferation.
Neoplasms
ALDH5A1 acts as a tumour promoter and has a prognostic impact in papillary thyroid carcinoma.
Neurodegenerative Diseases
Bi-allelic Mutations in ALDH5A1 is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability.
Ovarian Neoplasms
Decreased expression of ALDH5A1 predicts prognosis in patients with ovarian cancer.
Rett Syndrome
Rett syndrome (MECP2) and succinic semialdehyde dehydrogenase (ALDH5A1) deficiency in a developmentally delayed female.
Seizures
4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency.
Seizures
Circadian distribution of generalized tonic-clonic seizures associated with murine succinic semialdehyde dehydrogenase deficiency, a disorder of GABA metabolism.
Seizures
Gene expression analysis in epileptic hippocampi reveals a promoter haplotype conferring reduced aldehyde dehydrogenase 5a1 expression and responsiveness.
Seizures
Liver-directed adenoviral gene transfer in murine succinate semialdehyde dehydrogenase deficiency.
Seizures
Novel mutations in a Chinese family with two patients with succinic semialdehyde dehydrogenase deficiency.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
A Missense Variant in ALDH5A1 Associated with Canine Succinic Semialdehyde Dehydrogenase Deficiency (SSADHD) in the Saluki Dog.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
A novel ALDH5A1 mutation in a patient with succinic semialdehyde dehydrogenase deficiency.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
A novel ALDH5A1 mutation is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability in an Iranian family.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
A novel mutation of ALDH5A1 gene associated with succinic semialdehyde dehydrogenase deficiency.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Bi-allelic Mutations in ALDH5A1 is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Enzyme Replacement Therapy for Succinic Semialdehyde Dehydrogenase Deficiency: Relevance in ?-Aminobutyric Acid Plasticity.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Functional analysis of thirty-four suspected pathogenic missense variants in ALDH5A1 gene associated with succinic semialdehyde dehydrogenase deficiency.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency: a compound heterozygote with 103-121del and 1460T > A of the ALDH5A1 gene.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Rett syndrome (MECP2) and succinic semialdehyde dehydrogenase (ALDH5A1) deficiency in a developmentally delayed female.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Succinic Semialdehyde Dehydrogenase Deficiency in a Chinese Boy: A Novel ALDH5A1 Mutation With Severe Phenotype.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Succinic Semialdehyde Dehydrogenase Deficiency: In Vitro and In Silico Characterization of a Novel Pathogenic Missense Variant and Analysis of the Mutational Spectrum of ALDH5A1.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
Succinic semialdehyde dehydrogenase deficiency: The combination of a novel ALDH5A1 gene mutation and a missense SNP strongly affects SSADH enzyme activity and stability.
succinate-semialdehyde dehydrogenase [nad(p)+] deficiency
[Analysis of ALDH5A1 gene mutation in a Chinese Han family with succinic semialdehyde dehydrogenase deficiency].
Thyroid Cancer, Papillary
ALDH5A1 acts as a tumour promoter and has a prognostic impact in papillary thyroid carcinoma.
Zika Virus Infection
Determination of system level alterations in host transcriptome due to Zika virus (ZIKV) Infection in retinal pigment epithelium.
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0.3
2,5-dioxopentanoate
pH 6.5, 70°C, cofactor NAD+
0.1035
3-(methoxycarbonyl)benzoate
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.05
3-acetylpyridine adenine dinucleotide
-
-
0.017 - 0.1418
3-carboxybenzaldehyde
0.0502 - 0.287
3-Nitrobenzaldehyde
0.0121 - 0.1668
4-carboxybenzaldehyde
0.0503
4-hydroxy-trans-2-nonenal
-
recombinant enzyme
0.156 - 0.1612
4-nitrobenzaldehyde
0.875 - 4.82
acetaldehyde
0.011 - 0.0159
alpha-Ketoglutaric semialdehyde
0.019 - 0.241
benzaldehyde
0.0163
Glutaraldehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
0.0034
Glutaric semialdehyde
-
-
0.218
methyl 3-formylbenzoate
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0287 - 0.096
n-Pentanal
0.033
p-nitrobenzaldehyde
-
-
0.58 - 0.85
propionaldehyde
0.0007 - 6.3
succinate semialdehyde
0.0589
trans-2-hexenal
-
recombinant enzyme
additional information
additional information
-
0.017
3-carboxybenzaldehyde
-
-
0.0331
3-carboxybenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.112
3-carboxybenzaldehyde
-
0.1418
3-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0502
3-Nitrobenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.287
3-Nitrobenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0121
4-carboxybenzaldehyde
-
-
0.0151
4-carboxybenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0312
4-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0776
4-carboxybenzaldehyde
-
0.115
4-carboxybenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.1668
4-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.156
4-nitrobenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.1612
4-nitrobenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.875
acetaldehyde
-
-
2.797
acetaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
3.16
acetaldehyde
-
mutant enzyme R166K, at 37°C, in 40 mM sodium phosphate, pH 7.4
4.3
acetaldehyde
-
wild type enzyme, at 37°C, in 40 mM sodium phosphate, pH 7.4
4.5
acetaldehyde
-
mutant enzyme R166H, at 37°C, in 40 mM sodium phosphate, pH 7.4
4.82
acetaldehyde
-
mutant enzyme R166E, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.011
alpha-Ketoglutaric semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
0.0159
alpha-Ketoglutaric semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25°C
0.019
benzaldehyde
-
-
0.167
benzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.061
n-Butanal
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.323
n-Butanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0253
n-hexanal
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.107
n-hexanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0514
n-octanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.137
n-octanal
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0287
n-Pentanal
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.096
n-Pentanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0025
NAD+
-
-
0.021
NAD+
-
wild type enzyme, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.035
NAD+
-
mutant enzyme R166E, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.038
NAD+
-
pH 9.0, 37°C
0.04
NAD+
pH and temperature not specified in the publication
0.0433
NAD+
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.044
NAD+
-
mutant enzyme R166A, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.063
NAD+
-
mutant enzyme R166H, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.071
NAD+
-
pH 8.3, 35°C
0.081
NAD+
-
mutant enzyme R166K, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.227
NAD+
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.227
NAD+
-
pH and temperature not specified in the publication
125
NAD+
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C
0.552
NADP+
-
0.616
NADP+
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.025
pentanal
-
-
1.212
propanal
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
1.622
propanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.58
propionaldehyde
-
-
0.0007 - 0.002
succinate semialdehyde
-
-
0.001
succinate semialdehyde
-
-
0.001
succinate semialdehyde
-
-
0.001
succinate semialdehyde
pH and temperature not specified in the publication
0.00247
succinate semialdehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.00256
succinate semialdehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0027
succinate semialdehyde
-
0.0027 - 0.0029
succinate semialdehyde
-
-
0.003
succinate semialdehyde
-
pH and temperature not specified in the publication
0.0035
succinate semialdehyde
-
recombinant enzyme
0.0039
succinate semialdehyde
-
-
0.0046
succinate semialdehyde
-
-
0.0047
succinate semialdehyde
-
0.0074
succinate semialdehyde
-
-
0.01053
succinate semialdehyde
-
-
0.0109
succinate semialdehyde
-
mutant enzyme R166K, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.013
succinate semialdehyde
-
wild type enzyme, at 37°C, in 40 mM sodium phosphate, pH 7.4
0.015
succinate semialdehyde
-
-
0.0159
succinate semialdehyde
-
-
0.028
succinate semialdehyde
pH 9.0 37°C
0.03
succinate semialdehyde
pH 6.5, 70°C, cofactor NAD+
0.0385
succinate semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
0.047
succinate semialdehyde
-
pH 9.0, 37°C
0.1
succinate semialdehyde
-
-
0.16
succinate semialdehyde
-
pH 8.3, 35°C
0.62
succinate semialdehyde
-
mutant enzyme R166E, at 37°C, in 40 mM sodium phosphate, pH 7.4
1.13
succinate semialdehyde
-
mutant enzyme R166H, at 37°C, in 40 mM sodium phosphate, pH 7.4
1.6
succinate semialdehyde
-
mutant enzyme R166A, at 37°C, in 40 mM sodium phosphate, pH 7.4
6.3
succinate semialdehyde
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
kinetics and kinetic mechanism, overview
-
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C196A
loss in specific activity of 55%
C196S
loss in specific activity of 74%
C243S
loss in specific activity of 70%
C311A
decreased SSADH activity to undetectable levels
C311S
decreased SSADH activity to undetectable levels
C502S
loss in specific activity of 93%
E277D
leads to a product with similar specific activity
E277K
charge inversion, which results in recombinant protein totally devoid of detectable SSADH activity
E277Q
concomitant loss of the negative charge, which results in recombinant protein totally devoid of detectable SSADH activity
A237S/T423S
naturally occuring mutation, the mutant shows about 70% reduced activity compared to wild-type
C340A
inactive mutant that cannot form a disulfide bond even under strong reducing conditions
C342A
catalytically functional mutant that cannot form a disulfide bond even under strong reducing conditions
G176R/H180Y
naturally occuring mutation, the p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity
G176R/H180Y/A237S/T423S
naturally occuring mutation, an Italian SSADHD patient shows heterozygosity for four missense mutations: c.526G>A (p.G176R), c.538C>T (p.H180Y), c.709G>T (p.A237S) and c.1267A>T (p.T423S). The p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity. Clinical and cognitive evaluations, phenotype, overview
G46R
the mutant shows 87% activity compared to the wild type enzyme
K301E
naturally occuring homozygous missense mutation c.901A>G, inactive mutant, the mutation leads to semialdehyde dehydrogenase (SSADH) deficiency disorder, phenotype overview. Mutation K301E most likely leads to a loss of NAD+ binding and a predicted decrease in the free energy by 6.67 kcal/mol suggesting a severe destabilization of the protein. Structure-based in silico modeling of the mutant protein
T233M
the mutant shows 4% activity compared to the wild type enzyme
R166A
-
the mutant enzyme shows no activity towards acetaldehyde and decreased activity and higher KM for succinate semiacetaldehyde
R166E
-
the mutant enzyme shows almost no activity towards acetaldehyde and decreased activity and higher KM for succinate semiacetaldehyde
R166H
-
the mutant has KM for succinate semiacetaldehyde of 800fold greater than the wild type enzyme, while the VMAX for this mutant is 11.3fold less than wild type for succinate semiacetaldehyde
R166K
-
the mutant has KM for succinate semiacetaldehyde of 8fold greater than the wild type enzyme, while the VMAX for this mutant is 2.5fold less than wild type for succinate semiacetaldehyde
A237S
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 65% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
A237S
the mutant shows 65% activity compared to the wild type enzyme
A273S
naturally occuring missense variant expressed in HEK293 cells, 65.1% of the SSADH activity of the wild-type enzyme
A273S
-
the mutant shows enzyme activity reduction
A273S
mutant with activity reduction
C223R
-
missense mutation associated with a dramatic reduction of enzyme activity
C223R
the mutation is associated with gamma-hydroxybutyric aciduria
C223Y
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 5% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
C223Y
the mutant shows 5% activity compared to the wild type enzyme
C93F
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 3% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
C93F
the mutant shows 3% activity compared to the wild type enzyme
G176R
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G176R
the mutant shows less than 1% activity compared to the wild type enzyme
G176R
naturally occuring mutation, the p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity. Amino acid replacements G176R and H180Y are located in the same beta-segment that is at the interface between the monomers. The introduction of the positive charges of arginines, in presence of the bulky sidechains of tyrosines, could inhibit the correct tetramer assembly, thus causing instability
G268E
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G268E
the mutant shows less than 1% activity compared to the wild type enzyme
G36R
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 87% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G36R
naturally occuring missense variant expressed in HEK293 cells, 86.7% of the SSADH activity of the wild-type enzyme
G36R
-
the slight activity reduction displayed by the G36R variant can be attributed to altered mitochondrial targeting, as the amino acid change lies within the mitochondrial leader sequence
G36R
mutant with activity reduction
G409D
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G409D
the mutant shows less than 1% activity compared to the wild type enzyme
G533R
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G533R
the mutant shows less than 1% activity compared to the wild type enzyme
H180Y
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 83% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
H180Y
naturally occuring missense variant expressed in HEK293 cells, 82.5% of the SSADH activity of the wild-type enzyme
H180Y
-
the mutant shows enzyme activity reduction
H180Y
mutant with activity reduction
H180Y
the mutant shows 83% activity compared to the wild type enzyme
N255S
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 17% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
N255S
the mutant shows 17% activity compared to the wild type enzyme
N335K
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
N335K
the mutant shows 1% activity compared to the wild type enzyme
P182L
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 5% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
P182L
naturally occuring missense variant expressed in HEK293 cells, 47.6% of the SSADH activity of the wild-type enzyme
P182L
-
a significant activity reduction is observed for P182L
P182L
mutant with significant activity reduction
P182L
the mutant shows 48% activity compared to the wild type enzyme
P382L
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 2% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
P382L
the mutant shows 2% activity compared to the wild type enzyme
additional information
-
yneI knockout mutant shows strongly inhibited growth compared to the wild-type
additional information
-
yneI knockout mutant shows strongly inhibited growth compared to the wild-type
-
additional information
lowest stability for the tetramer constituted by G176R/H180Y monomers and the highest stability for that constituted by A237S/T423S monomers. The combination of the two double mutant alleles produces a synergic negative effect on SSADH enzyme activity and stability, thus resulting in SSADHD phenotype
additional information
Aldh5a1-/- mice show abnormalities of respiratory chain function. Hippocampus and cortex are primary targets for neurodegeneration
additional information
aldh5a1-/- (SSADHD) mice and their genetic controls (aldh5a1+/+) are exposed to either a 4% (w/w) glutamine-containing diet or a glutamine-free diet from conception until postnatal day 30. The test diet increases hepatic glutamate in both genotypes, decreases glutamine in aldh5a1+/+ but not in aldh5a1-/-, but has no effect on GABA. Dried bloodspot analyses show significantly elevated GABA in mutants (approximately 800% above controls) and decreased glutamate (approximately 25%), but no glutamine difference with controls. Glutamine supplementation does not impact blood GABA but significantly increased glutamine and glutamate in both genotypes indicating systemic exposure to dietary glutamine. Ataxia and pronounced hyperactivity are observed in aldh5a1-/- mice but remain unchanged by the diet intervention. Glutamine supplementation improves peripheral but not central glutamine deficiency in experimental SSADHD. Murine SSADHD presents with dramatic changes in amino acid levels including a significant elevation in brain GABA, one of the major inhibitory neurotransmitters, a moderate increase in excitatory neurotransmitter glutamate, and a very significant decrease in brain glutamine, the metabolic precursor of glutamate. Phenotype, overview
additional information
-
aldh5a1-/- (SSADHD) mice and their genetic controls (aldh5a1+/+) are exposed to either a 4% (w/w) glutamine-containing diet or a glutamine-free diet from conception until postnatal day 30. The test diet increases hepatic glutamate in both genotypes, decreases glutamine in aldh5a1+/+ but not in aldh5a1-/-, but has no effect on GABA. Dried bloodspot analyses show significantly elevated GABA in mutants (approximately 800% above controls) and decreased glutamate (approximately 25%), but no glutamine difference with controls. Glutamine supplementation does not impact blood GABA but significantly increased glutamine and glutamate in both genotypes indicating systemic exposure to dietary glutamine. Ataxia and pronounced hyperactivity are observed in aldh5a1-/- mice but remain unchanged by the diet intervention. Glutamine supplementation improves peripheral but not central glutamine deficiency in experimental SSADHD. Murine SSADHD presents with dramatic changes in amino acid levels including a significant elevation in brain GABA, one of the major inhibitory neurotransmitters, a moderate increase in excitatory neurotransmitter glutamate, and a very significant decrease in brain glutamine, the metabolic precursor of glutamate. Phenotype, overview
-
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