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Information on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)
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1.2.1.24 succinate-semialdehyde dehydrogenase (NAD+)IUBMB Comments
This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.79 [succinate-semialdehyde dehydrogenase (NADP+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NAD+.
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Word Map
- 1.2.1.24
-
aldhs
-
gamma-hydroxybutyric
-
4-hydroxybutyric
-
ssadhd
- propionaldehyde
- trans-4-hydroxy-2-nonenal
- aldh4a1
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
aldh5a1, aldh5a, aldehyde dehydrogenase 5a1, nad(+)-dependent succinic semialdehyde dehydrogenase, alphakgsa dehydrogenase, ssaldh, sso1629, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde dehydrogenase 5a1
ALDH5A1
dehydrogenase, succinate semialdehyde
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NAD(+)-dependent succinic semialdehyde dehydrogenase
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SSADH
succinate semialdehyde dehydrogenase
succinate semialdehyde:NAD+ oxidoreductase
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succinic semialdehyde dehydrogenase
succinyl semialdehyde dehydrogenase
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SSADH
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succinate semialdehyde dehydrogenase
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succinic semialdehyde dehydrogenase
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succinic semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
compulsory-order mechanism, NAD+ is the first substrate to bind to the enzyme and NADH is the last product to dissociate from it
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succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
compulsory ordered mechanism where NAD+ binds first followed by succinate semialdehyde
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succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
sequential ordered Bi-Bi reaction mechanism
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
sequential ordered Bi-Bi reaction mechanism
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succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
succinate-semialdehyde:NAD+ oxidoreductase
This enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.79 [succinate-semialdehyde dehydrogenase (NADP+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NAD+.
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CAS REGISTRY NUMBER
COMMENTARY
9028-95-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
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?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + H+
about 3% activity compared to succinate semialdehyde
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?
2-phenylacetaldehyde + NAD+ + H2O
2-phenylbenzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
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?
2-tolualdehyde + NAD+ + H2O
2-carboxytoluene + NADH + H+
about 1% activity compared to succinate semialdehyde
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-
?
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
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?
alpha-ketoglutaric semialdehyde + NAD+ + H2O
alpha-ketoglutarate + NADH
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?
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH
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-
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?
betaine aldehyde + NAD+ + H2O
2-trimethylammonioacetate + NADH
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?
glyoxylic acid + NAD+ + H2O
2-phenylbenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
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?
iso-butanal + NAD+ + H2O
? + NADH + H+
less than 10% activity compared to succinate semialdehyde
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?
iso-butanal + NAD+ + H2O
isobutanoate + NADH + H+
-
less than 10% activity compared to succinate semialdehyde
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-
?
iso-pentanal + NAD+ + H2O
? + NADH + H+
about 2% activity compared to succinate semialdehyde
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-
?
iso-pentanal + NAD+ + H2O
isopentanoate + NADH + H+
-
less than 5% activity compared to succinate semialdehyde
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-
?
m-carboxybenzaldehyde + NAD+ + H2O
m-carboxybenzoate + NADH + H+
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?
m-methylcarboxybenzaldehyde + NAD+ + H2O
m-methylcarboxybenzoate + NADH + H+
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?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
-
4.3% of the activity with succinate semialdehyde
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?
malonate semialdehyde + NAD+ + H2O
malonate + NADH + 2 H+
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3.8% of the activity with succinate semialdehyde
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?
n-butanal + NAD+ + H2O
butanoic acid + NADH + 2 H+
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about 11% of the rate with succinic semialdehyde
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?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
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?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
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?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
about 20% activity compared to succinate semialdehyde
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?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
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about 35% activity compared to succinate semialdehyde
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?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
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?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
about 2% activity compared to succinate semialdehyde
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?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
about 3% activity compared to succinate semialdehyde
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?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
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?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
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about 10% activity compared to succinate semialdehyde
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?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
about 3% activity compared to succinate semialdehyde
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?
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
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about 10% activity compared to succinate semialdehyde
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?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
about 20% activity compared to succinate semialdehyde
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?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
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about 15% activity compared to succinate semialdehyde
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?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
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?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
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?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
about 10% activity compared to succinate semialdehyde
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?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
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about 65% activity compared to succinate semialdehyde
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?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
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?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
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?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
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?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
about 1% activity compared to succinate semialdehyde
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?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
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about 5% activity compared to succinate semialdehyde
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?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
about 15% activity compared to succinate semialdehyde
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?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
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about 30% activity compared to succinate semialdehyde
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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2.3% of the activity with succinate semialdehyde
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
about 5% activity compared to succinate semialdehyde
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
about 10% activity compared to succinate semialdehyde
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?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
about 5% activity compared to succinate semialdehyde
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?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
about 30% activity compared to succinate semialdehyde
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?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
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13% of the activity with succinate semialdehyde
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?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
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25% of the activity with succinate semialdehyde
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?
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
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?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
about 15% activity compared to succinate semialdehyde
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?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
-
about 30% activity compared to succinate semialdehyde
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?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
about 10% activity compared to succinate semialdehyde
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?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
less than 60% activity compared to succinate semialdehyde
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-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
less than 10% activity compared to succinate semialdehyde
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?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
about 110% activity compared to succinate semialdehyde
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-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
less than 10% activity compared to succinate semialdehyde
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?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
-
less than 80% activity compared to succinate semialdehyde
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?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
less than 20% activity compared to succinate semialdehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
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100% activity
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?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
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6.5% of the activity with succinate semialdehyde
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?
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
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?
propionaldehyde + NAD+ + H2O
propionate + NADH
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5% of the activity with succinate semialdehyde
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-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
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-
-
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?
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
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?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
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enzyme is induced by growth on gamma-aminobutyrate
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?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
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?
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
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ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
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-
-
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?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme of agmatine degradation
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-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by growth on gamma-aminobutyrate
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-
?
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
-
enzyme is induced by succinate semialdehyde, functions in the oxidation of succinate semialdehyde during growth on both 4-hydroxyphenylacetate and 4-aminobutyrate
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?
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
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-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
induced by pyridine, the enzyme is involved in the degradation of pyridine
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-
?
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
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ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is involved in the catabolism of the neurotransmitter 4-aminobutyrate
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-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
-
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
the enzyme is specific for the substrates
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-
?
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+
no activity in presence of NADP+
-
-
?
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+
-
-
-
-
?
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+
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ir
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
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-
-
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
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-
-
additional information
?
-
no activity towards 2-methoxybenzaldehyde, and 4-tolualdehyde
-
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
Q8N3W7
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
-
enzyme of agmatine degradation
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
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
-
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
-
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
-
induced by pyridine, the enzyme is involved in the degradation of pyridine
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
enzyme is involved in the catabolism of the neurotransmitter 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
A2R4V5
-
-
-
?
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+
Q9SAK4
-
-
-
?
additional information
?
-
P51649
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive
NAD+
-
-
NADP+
-
cofactor; reduction rate is only a few percent of that of NAD+
NADP+
is also accepted as coenzyme substrate but leads to 7fold lower reaction rates compared to NAD+ at saturating succinate semialdehyde concentrations
additional information
-
human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-dimethylaminoazobenzene-4-iodoacetamide
-
time-dependent loss of activity, pseudo first-order kinetics. The inhibitor binds to a cysteine residue or near its active site. Inactivation is prevented by preincubation with succinate semialdehyde, but not by preincubation with coenzyme NAD+
o-phthalaldehyde
-
binding of 10 mol per mol of enzyme results in irreversible loss of activity
4-hydroxybenzaldehyde
linear dead-end inhibition, competitive versus succinate semialdehyde, uncompetitive versus NAD+
N-formylglycine
-
4 mM, 40% inhibition, reversible, competitive with respect to succinate semialdehyde, uncompetitive with respect to NAD+
NADH
product inhibition, competitive versus NAD+, uncompetitive versus succinate semialdehyde
NADH
-
NADH is a strong competitive inhibitor with respect to NAD+ and behaves as a non-competitive inhibitor with respect to succinate semialdehyde
NADH
-
competitive with respect to NAD+; mixed with respect to succinate semialdehyde
pyridoxal 5'-phosphate
-
catalytic function is modulated by binding of pyridoxal-5'-phosphate to specific Lys347 residue at or near the coenzyme-binding site of the protein, NAD+ protects from inactivation
succinate semialdehyde
substrate inhibition, uncompetitive versus NAD+
succinate semialdehyde
-
inhibition by the succinate semialdehyde substrate is starting already at a concentration as low as 0.02 mM
succinate semialdehyde
inhibition by the succinate semialdehyde substrate is starting already at a concentration as low as 0.02 mM
succinate semialdehyde
the enzyme loses more than 80% of its enzymatic potential at 0.5 mM and shows 8% residual activity at 3 mM succinate semialdehyde
succinate semialdehyde
-
substrate inhibition, uncompetitive with respect to NAD+
succinate semialdehyde
-
the enzyme loses more than 80% of its enzymatic potential at 0.5 mM and shows 8% residual activity at 3 mM succinate semialdehyde
additional information
-
no inhibition by 0.1 mM trans-2-hexenal and 0.1 mM crotonaldehyde
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
gene yneI is responsible for NAD+/NADP+-SSADH activity. The gene is induced by succinate semialdehyde
-
2-mercaptoethanol
-
loss of about 50% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
2-mercaptoethanol
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
dithiothreitol
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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
Inherited disorders of gamma-aminobutyric acid metabolism and advances in ALDH5A1 mutation identification.
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
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.
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.
Metabolic Diseases
Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease.
Ovarian Neoplasms
Decreased expression of ALDH5A1 predicts prognosis in patients with ovarian cancer.
Seizures
Circadian distribution of generalized tonic-clonic seizures associated with murine succinic semialdehyde dehydrogenase deficiency, a disorder of GABA metabolism.
Seizures
Liver-directed adenoviral gene transfer in murine succinate semialdehyde dehydrogenase deficiency.
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
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
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: 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].
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1035
3-(methoxycarbonyl)benzoate
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0163
Glutaraldehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
0.218
methyl 3-formylbenzoate
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
0.0331
3-carboxybenzaldehyde
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
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
0.0151
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
0.115
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
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
0.167
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
0.035
NAD+
-
mutant enzyme R166E, at 37°C, in 40 mM sodium phosphate, pH 7.4
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
0.081
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
125
NAD+
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C
0.616
NADP+
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C
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
0.001
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
0.003
succinate semialdehyde
-
pH and temperature not specified in the publication
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
0.0385
succinate semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
0.62
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
kinetics and kinetic mechanism, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.3
Glutaraldehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
12.3
alpha-Ketoglutaric semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25°C
51.2
alpha-Ketoglutaric semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
31.7
succinate semialdehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.37
4-hydroxybenzaldehyde
pH 9.0, 37°C, versus succinate semmialdehyde
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.6
9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
at pH 8.5 MalE-DmSSADH is 10fold more active than at pH 6.0
7 - 10
8 - 9
8 - 10
-
pH 8.0: about 40% of maximal activity, pH 10.0: about 55% of maximal activity
8.5 - 10
-
pH 8.5: about 45% of maximal activity, pH 10.0: about 70% of maximal activity
8.7 - 10.5
-
pH 8.7: about 50% of maximal activity, pH 10.5: about 75% of maximal activity
7 - 10
-
pH 7.0: about 40% of maximal activity, pH 10.0: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
optimal expression of pMalc2x-DmSSADH in Escherichia coli TB1
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
complete sequence of cDNA clone H46643 with C538/transition; naturally occuring missense variants, which may significantly contribute to inter-individual variation of SSADH activity, possibly influencing endogenous level of 4-aminobutyric acid and 4-hydroxybutyric acid
SwissProt
brenda
single nucleotide polymorphism in the coding sequence as well as in the exons and the 5'-regulatory region of the succinic semialdehyde dehydrogenase gene can not be related to idiopathic generalized epilepsy or abnormal photoparoxysomal response
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SSADH is widely expressed throughout most brain regions, although a particularly strong expression is observed in the primary and secondary motor cortex, the amygdala, and the basal ganglia
brenda
-
SSADH is widely expressed throughout most brain regions, although a particularly strong expression is observed in the primary and secondary motor cortex, the amygdala, and the basal ganglia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
additional information
-
human SSADH intrinsic regulatory mechanism, redox-switch modulation, by which large conformational changes are brought about in the catalytic loop through disulfide bonding, enzyme molecular structure, overview
malfunction
-
SSADH enzyme activity is deficient in patients with gamma-hydroxybutyric aciduria
malfunction
-
at approximately postnatal day 16-22 SSADH-deficient mice display ataxia and loss of motor control, and develop generalized seizures leading to rapid death by the fourth week of life. D-2-hydroxyglutarate and 4,5-dihydroxyhexanoic acid are elevated in SSADH-deficient mice. SSADH-deficient mice demonstrate a 20% reduction in the ethanolamine glycerophospholipid content as compared to wild type littermates while other brain phospholipids (choline glycerophospholipid, phosphatidylserine and phosphatidylinositol) are not affected
malfunction
-
mutation of gene ALDH5A1 with amino acid exchange K301E is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability in an Iranian family. Succinic semialdehyde dehydrogenase (SSADH) deficiency is a rare autosomal recessive inherited metabolic disorder of the catabolism of the neurotransmitter gamma-aminobutyric acid (GABA) with a very variable clinical phenotype ranging from mild intellectual disability to severe neurological defects. The disorder results in the accumulation of gamma-hydroxybutyrate in the brain, 30fold increased level compared to wild-type. No SSADH enzyme activity is detected in the patient's lymphoblasts
metabolism
-
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid
metabolism
-
under normal physiological conditions, SSADH works in tandem with GABA transaminase to convert the carbon backbone of gamma-aminobutyric acid to succinate, the latter a source of energy within the tricarboxylic acid cycle. SSADH, in brain, is the major aldehyde dehydrogenase responsible for 4-hydroxy-trans-2-nonenal disposition, but only a minor contributor to its metabolism in liver
metabolism
-
under normal physiological conditions, SSADH works in tandem with GABA transaminase to convert the carbon backbone of gamma-aminobutyric acid to succinate, the latter a source of energy within the tricarboxylic acid cycle. SSADH, in brain, is the major aldehyde dehydrogenase responsible for 4-hydroxy-trans-2-nonenal disposition, but only a minor contributor to its metabolism in liver
metabolism
-
the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)
Show AA Sequence and Transmembrane Helices (745 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
52000
55400
98000
145000
160000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
homotrimer
3 * 50000, SDS-PAGE; 3 * 51500, calculated from sequence
tetramer
additional information
additional information
-
human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding. Human SSADH activity is regulated by redox-switch modulation, which depends on reversible intra-disulfide binding to the dynamic catalytic loop. Simulations, and protein transformation and configuration modelling to explain the dynamic redox modulation, method optimization, detailed overview
additional information
-
4-aminobutyrate aminotransferase and succinate semialdehyde dehydrogenase form a stable enzymatic complex under in vivo conditions
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
A273S
C223R
C223Y
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
C93F
G176R
G268E
G36R
G409D
G533R
H180Y
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
N255S
N335K
P182L
P382L
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
additional information
A237S
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 65% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
A273S
naturally occuring missense variant expressed in HEK293 cells, 65.1% of the SSADH activity of the wild-type enzyme
C223R
-
missense mutation associated with a dramatic reduction of enzyme activity
C223Y
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 5% of the succinate semialdehyde dehydrogenase activity of 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
G176R
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G268E
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of 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
G409D
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of 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
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
N255S
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 17% of the succinate semialdehyde dehydrogenase activity of 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
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
P382L
-
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 2% of the succinate semialdehyde dehydrogenase activity of 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
Aldh5a1-/- mice show abnormalities of respiratory chain function. Hippocampus and cortex are primary targets for neurodegeneration
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.2
-
with wild type enzyme, similar activity is observed with pH 7.4 and 8.2, only 10% of the pH 7.4 activity is observed when the pH is reduced to pH 6.0, substitution with a lysine removes the pH sensitivity whereas the R166H mutant enzyme has higher activity at pH 6.0 than at pH 8.0
697282
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
pH 7.4, 8 min, complete inactivation. Mercaptoethanol stabilizes for 20 min or longer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NAD+ and mercaptoethanol effectively protect from auto-oxidation. NAD+ does not prevent auto-oxidation in presence of urea
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
when reduced wild type SSADH is treated with hydrogen peroxide, the protein is almost completely inactivated and recovers its activity when the environment is switched back to a reduced state
-
710898
when reduced wild type SSADH is treated with hydrogen peroxide, the protein is almost completely inactivated and recovers its activity when the environment was switched back to a reduced state
-
710898
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM sodium diphosphate buffer, pH 7.2, 14 mM 2-mercaptoethanol, 25% v/v glycerol, 2-3 months, retains 80-85% of the activity
-
-20°C, purified native enzyme, 100 mM diphosphate, pH 8.0, 14 mM 2-mercaptoethanol, 20% glycerol, loss of 50% activity witin 5 days
0°C, 100 mM sodium phosphate, pH 8.5, 1mM DTT, 43% glycerol, 3 years
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
His-tagged YneI dehydrogenase purified from cell extracts with HiTrap affinity columns
-
native enzyme 9fold from mycelia by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography
Ni-affinity chromatography
Ni2+-NTA agarose column chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
expression in Escherichia coli as His-tag fusion protein
gene ALDH5A1, screening and genotyping, DNA and amino acid sequence determination and analysis
-
into vectors pQE30 and into pMalc2x. Expression in Escherichia coli strains M15 and TB1
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
into vectors pQE30 and into pMalc2x. Expression in Escherichia coli strains M15 and TB1
-
into vectors pQE30 and into pMalc2x. Expression in Escherichia coli strains M15 and TB1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
SSADH (Aldh5a1) deficiency is a rare autosomal recessive disease. Hippocampal and cortical dysfunction in Aldh5a1-/- brain, but no evidence that accumulating key metabolites of SSADH deficiency directly induce impairment of energy metabolism
medicine
-
succinic semialdehyde dehydrogenase deficient patients show widespread reduction in benzodiazepine receptor binding on [(11)C]-flumazenil-positron emission tomography
additional information
-
in the world population, the c.538C variant of SSADH is proceeding to replace the ancestral c.538T, shared with primates. A significant correlation between the frequencies of the derived alleles in SSADH and microcephalin, which show concerted changes worldwide and, at least in Asian populations, also on a restricted geographical scale
additional information
-
genomic copy of the SSADH gene is devoid of introns. Multiple SSADH gene copies are present in the genome
additional information
genomic copy of the SSADH gene contains two introns. Multiple SSADH gene copies are present in the genome
additional information
-
yneI, responsible for NAD+/NADP+-dependent SSADH activity, plays a unique physiological role in the general nitrogen metabolism of Escherichia coli. The yneI gene has an important, but not essential, role during growth on arginine and probably has an essential function during growth on putrescine as the nitrogen source. The yneI-encoded activity functions primarily as a valve to prevent toxic accumulation of succinate semialdehyde
additional information
-
yneI, responsible for NAD+/NADP+-dependent SSADH activity, plays a unique physiological role in the general nitrogen metabolism of Escherichia coli. The yneI gene has an important, but not essential, role during growth on arginine and probably has an essential function during growth on putrescine as the nitrogen source. The yneI-encoded activity functions primarily as a valve to prevent toxic accumulation of succinate semialdehyde
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Friedrich, B.; Magasanik, B.
Enzymes of agmatine degradation and the control of their synthesis in Klebsiella aerogenes
J. Bacteriol.
137
1127-1133
1979
Klebsiella aerogenes
brenda
Tokunaga, M.; Nakano, Y.; Kitaoka, S.
Separation and properties of the NAD-linked and NADP-linked isozymes of succinic semialdehyde dehydrogenase in Euglena gracilis z
Biochim. Biophys. Acta
429
55-62
1976
Euglena gracilis
brenda
Choi, S.Y.; Bahn, J.H.; Lee, B.R.; Jeon, S.G.; Jang, J.S.; Kim, C.K.; Jin, L.H.; Kim, K.H.; Park, J.S.; Park, J.; Cho, S.W.
Brain succinic semialdehyde dehydrogenase: identification of reactive lysyl residues labeled with pyridoxal-5'-phosphate
J. Neurochem.
76
919-925
2001
Bos taurus
brenda
Satya Narayan, V.; Madhusudanan Nair, P.
Potato tuber succinate semialdehyde dehydrogenase: purification and characterization
Arch. Biochem. Biophys.
275
469-477
1989
Solanum tuberosum
brenda
Yamaura, I.; Matsumoto, T.; Funatsu, M.; Shinohara, T.
Purification and some properties of succinic semialdehyde dehydrogenase from barley seeds
Agric. Biol. Chem.
52
2929-2930
1988
Hordeum vulgare subsp. vulgare
-
brenda
Ryzlak, M.T.; Pietruszko, R.
Human brain high Km aldehyde dehydrogenase: purification, characterization, and identification as NAD+-dependent succinic semialdehyde dehydrogenase
Arch. Biochem. Biophys.
266
386-396
1988
Homo sapiens
brenda
Ferrer, E.; Cooper, R.A.
a single succinic semialdehyde dehydrogenase is involved in 4-hydroxyphenylacetate and 4-aminobutyrate catabolism in Klebsiella pneumoniae M5a1
FEMS Microbiol. Lett.
52
161-164
1988
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
-
brenda
Marek, L.E.; Henson, J.M.
Cloning and expression of the Escherichia coli K-12 sad gene
J. Bacteriol.
170
991-994
1988
Escherichia coli
brenda
Sims, G.K.; Sommers, L.E.; Konopka, A.
Degradation of pyridine by Micrococcus luteus isolated from soil
Appl. Environ. Microbiol.
51
963-968
1986
Micrococcus luteus
brenda
Hearl, W.G.; Churchich, J.E.
Interactions between 4-aminobutyrate aminotransferase and succinic semialdehyde dehydrogenase, two mitochondrial enzymes
J. Biol. Chem.
259
11459-11463
1984
Sus scrofa
brenda
Galleschi, L.; Nocchi, C.; Floris, C.; Bedini, G.; Anguillesi, M.C.; Grilli, I.
Succinic semialdehyde dehydrogenase in higher plants: purification and properties of the enzyme from Triticum durum embryos
Biochem. Physiol. Pflanz.
178
645-651
1983
Triticum turgidum subsp. durum
-
brenda
Rivett, A.J.; Tipton, K.F.
Kinetic studies with rat-brain succinic-semialdehyde dehydrogenase
Eur. J. Biochem.
117
187-193
1981
Rattus norvegicus
brenda
Donnelly, M.I.; Cooper, R.A.
Two succinic semialdehyde dehydrogenases are induced when Escherichia coli K-12 is grown on gamma-aminobutyrate
J. Bacteriol.
145
1425-1427
1981
Escherichia coli
brenda
Blaner, W.S.; Churchich, J.E.
The binding of NADH to succinic semialdehyde dehydrogenase
Eur. J. Biochem.
109
431-437
1980
Sus scrofa
brenda
Lai, J.C.K.; Clark, J.B.
Preparation of synaptic and nonsynaptic mitochondria from mammalian brain
Methods Enzymol.
55
51-60
1979
Rattus norvegicus
brenda
Blaner, W.S.; Churchich, J.
Succinic semialdehyde dehydrogenase. Reactivity of lysyl residues
J. Biol. Chem.
254
1794-1798
1979
Sus scrofa
brenda
Galleschi, L.; Tozzi, M.G.; Cozzani, I.; Floris, C.
Succinic semialdehyde dehydrogenase of wheat grain
Planta
142
175-180
1978
Triticum turgidum subsp. durum
brenda
Cash, C.D.; Maitre, M.; Ossola, L.; Mandel, P.
Purification and properties of two succinate semialdehyde dehydrogenases from human brain
Biochim. Biophys. Acta
524
26-36
1978
Homo sapiens
brenda
Cash, C.; Ciesielski, L.; Maitre, M.; Mandel, P.
Purification and properties of rat brain succinic semialdehyde dehydrogenase
Biochimie
59
257-268
1977
Rattus norvegicus
brenda
Callewaert, D.M.; Rosemblatt, M.S.; Suzuki, K.; Tchen, T.T.
Succinic semialdehyde dehydrogenase from a Pseudomonas species. I. Purification and chemical properties
J. Biol. Chem.
248
6009-6013
1973
Pseudomonas sp.
brenda
Rosemblatt, M.S.; Callewaert, D.M.; Tchen, T.T.
Succinic semialdehyde dehydrogenase from a Pseudomonas species. II. Physical and immunochemical properties of the enzyme
J. Biol. Chem.
248
6014-6018
1973
Pseudomonas sp.
brenda
Kumar, S.; Punekar, N.S.
Inhibition of succinic semialdehyde dehydrogenase by N-formylglycine
J. Enzyme Inhib.
13
369-376
1998
Aspergillus niger, Solanum tuberosum
brenda
Albers, R.W.; Koval, G.J.
Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain
Biochim. Biophys. Acta
52
29-35
1961
Platyrrhini
brenda
Koh, Y.S.; Joo, C.N.; Choi, S.Y.; Kim, D.S.
Purification and properties of succinic semialdehyde dehydrogenase from Lumbricus rubellus
Korean Biochem. J.
27
75-79
1994
Lumbricus rubellus
-
brenda
Chambliss, K.L.; Caudle, D.L.; Hinson, D.D.; Moomaw, C.R.; Slaughter, C.A.; Jakobs, C.; Gibson, K.M.
Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression
J. Biol. Chem.
270
461-467
1995
Homo sapiens, Rattus norvegicus
brenda
Busch, K.B.; Fromm, H.
Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides
Plant Physiol.
121
589-597
1999
Arabidopsis sp.
brenda
Chambliss, K.L.; Zhang, Y.A.; Rossier, E.; Vollmer, B.; Gibson, K.M.
Enzymatic and immunologic identification of succinic semialdehyde dehydrogenase in rat and human neural and nonneural tissues
J. Neurochem.
65
851-855
1995
Homo sapiens, Rattus norvegicus
brenda
Nguyen, E.; Picklo, M.J., Sr.
Inhibition of succinic semialdehyde dehydrogenase activity by alkenal products of lipid peroxidation
Biochim. Biophys. Acta
1637
107-112
2003
Rattus norvegicus
brenda
Lee, B.R.; Kim, D.W.; Hong, J.W.; Eum, W.S.; Choi, H.S.; Choi, S.H.; Kim, S.Y.; An, J.J.; Ahn, J.Y.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Brain succinic semialdehyde dehydrogenase. Reactions of sulfhydryl residues connected with catalytic activity
Eur. J. Biochem.
271
4903-4908
2004
Bos taurus
brenda
Akaboshi, S.; Hogema, B.M.; Novelletto, A.; Malaspina, P.; Salomons, G.S.; Maropoulos, G.D.; Jakobs, C.; Grompe, M.; Gibson, K.M.
Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency
Hum. Mutat.
22
442-450
2003
Homo sapiens (P51649)
brenda
Murphy, T.C.; Amarnath, V.; Gibson, K.M.; Picklo, M.J., Sr.
Oxidation of 4-hydroxy-2-nonenal by succinic semialdehyde dehydrogenase (ALDH5A)
J. Neurochem.
86
298-305
2003
Rattus norvegicus
brenda
Blasi, P.; Boyl, P.P.; Ledda, M.; Novelletto, A.; Gibson, K.M.; Jakobs, C.; Hogema, B.; Akaboshi, S.; Loreni, F.; Malaspina, P.
Structure of human succinic semialdehyde dehydrogenase gene: identification of promoter region and alternatively processed isoforms
Mol. Genet. Metab.
76
348-362
2002
Homo sapiens, Homo sapiens (Q8N3W7)
brenda
Bouche, N.; Fait, A.; Bouchez, D.; Moller, S.G.; Fromm, H.
Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
Proc. Natl. Acad. Sci. USA
100
6843-6848
2003
Arabidopsis sp.
brenda
Watanabe, S.; Kodaki, T.; Makino, K.
A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism
J. Biol. Chem.
281
28876-28888
2006
Azospirillum brasilense, Azospirillum brasilense (Q1JUP4)
brenda
Blasi, P.; Palmerio, F.; Aiello, A.; Rocchi, M.; Malaspina, P.; Novelletto, A.
SSADH variation in primates: intra- and interspecific data on a gene with a potential role in human cognitive functions
J. Mol. Evol.
63
54-68
2006
Gorilla gorilla (Q6A2H1), Homo sapiens, Hylobates lar (Q3MSM3), Pan paniscus, Pan paniscus (Q3MSM4), Pan troglodytes, Pan troglodytes (Q6A2H0), Pongo abelii (Q6A2H2), Pongo pygmaeus pygmaeus (Q6A2H2)
brenda
Lorenz, S.; Heils, A.; Taylor, K.P.; Gehrmann, A.; Muhle, H.; Gresch, M.; Becker, T.; Tauer, U.; Stephani, U.; Sander, T.
Candidate gene analysis of the succinic semialdehyde dehydrogenase gene (ALDH5A1) in patients with idiopathic generalized epilepsy and photosensitivity
Neurosci. Lett.
397
234-239
2006
Homo sapiens
brenda
Kang, J.H.; Park, Y.B.; Huh, T.L.; Lee, W.H.; Choi, M.S.; Kwon, O.S.
High-level expression and characterization of the recombinant enzyme, and tissue distribution of human succinic semialdehyde dehydrogenase
Protein Expr. Purif.
44
16-22
2005
Homo sapiens
brenda
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens (P51649)
brenda
Leone, O.; Blasi, P.; Palmerio, F.; Kozlov, A.I.; Malaspina, P.; Novelletto, A.
A human derived SSADH coding variant is replacing the ancestral allele shared with primates
Ann. Hum. Biol.
33
593-603
2007
Homo sapiens, Homo sapiens (P51649)
brenda
Rothacker, B.; Ilg, T.
Functional characterization of a Drosophila melanogaster succinic semialdehyde dehydrogenase and a non-specific aldehyde dehydrogenase
Insect Biochem. Mol. Biol.
38
354-366
2008
Drosophila melanogaster (Q9VBP6)
brenda
Rothacker, B.; Werr, M.; Ilg, T.
Molecular cloning, partial genomic structure and functional characterization of succinic semialdehyde dehydrogenase genes from the parasitic insects Lucilia cuprina and Ctenocephalides felis
Insect Mol. Biol.
17
279-291
2008
Ctenocephalides felis, Lucilia cuprina (B0JFD4)
brenda
Fuhrer, T.; Chen, L.; Sauer, U.; Vitkup, D.
Computational prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in Escherichia coli
J. Bacteriol.
189
8073-8078
2007
Escherichia coli, Escherichia coli BW25113
brenda
Sauer, S.W.; Koelker, S.; Hoffmann, G.F.; Ten Brink, H.J.; Jakobs, C.; Gibson, K.M.; Okun, J.G.
Enzymatic and metabolic evidence for a region specific mitochondrial dysfunction in brains of murine succinic semialdehyde dehydrogenase deficiency (Aldh5a1-/- mice)
Neurochem. Int.
50
653-659
2007
Mus musculus (Q8BUF0)
brenda
Jansen, E.E.; Struys, E.; Jakobs, C.; Hager, E.; Snead, O.C.; Gibson, K.M.
Neurotransmitter alterations in embryonic succinate semialdehyde dehydrogenase (SSADH) deficiency suggest a heightened