Information on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
1.2.1.24
-
RECOMMENDED NAME
GeneOntology No.
succinate-semialdehyde dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
show the reaction diagram
compulsory-order mechanism, NAD+ is the first substrate to bind to the enzyme and NADH is the last product to dissociate from it
-
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
show the reaction diagram
compulsory ordered mechanism where NAD+ binds first followed by succinate semialdehyde
-
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation
-
4-aminobutyrate degradation IV
-
Alanine, aspartate and glutamate metabolism
-
Butanoate metabolism
-
GABA shunt
-
glutamate degradation IV
-
Metabolic pathways
-
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+.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldehyde dehydrogenase 5a1
-
-
aldehyde dehydrogenase 5a1
P51649
-
aldehyde dehydrogenase 5a1
-
-
ALDH5A1
P51649
-
ALDH5A1
Q8BUF0
-
alphaKGSA dehydrogenase
Q1JUP4
-
dehydrogenase, succinate semialdehyde
-
-
-
-
NAD(+)-dependent succinic semialdehyde dehydrogenase
-
-
-
-
SSADH
-
-
-
-
SSADH
Q6A2H1
-
SSADH
Q8N3W7
-
SSADH
Q3MSM3
-
SSADH
B0JFD4
-
SSADH
Q8BUF0
-
SSADH
Q3MSM4
-
SSADH
Q6A2H0
-
SSADH-I
Q97XS9
-
SSADH/ALDH5A1
-
-
SSO1629
Q97XS9
ordered locus name
succinate semialdehyde dehydrogenase
-
-
-
-
succinate semialdehyde dehydrogenase
-
-
succinate semialdehyde dehydrogenase
-
-
-
succinate semialdehyde dehydrogenase
-
-
succinate semialdehyde dehydrogenase
P51649
-
succinate semialdehyde dehydrogenase
-
-
succinate semialdehyde:NAD+ oxidoreductase
-
-
-
-
succinic semialdehyde dehydrogenase
-
-
-
-
succinic semialdehyde dehydrogenase
-
-
succinic semialdehyde dehydrogenase
-
-
succinic semialdehyde dehydrogenase
Q9VBP6
-
succinic semialdehyde dehydrogenase
Q6A2H1
-
succinic semialdehyde dehydrogenase
-
-
succinic semialdehyde dehydrogenase
P51649
-
succinic semialdehyde dehydrogenase
Q3MSM3
-
succinic semialdehyde dehydrogenase
B0JFD4
-
succinic semialdehyde dehydrogenase
-
-
succinic semialdehyde dehydrogenase
Q8BUF0
-
succinic semialdehyde dehydrogenase
Q3MSM4
-
succinic semialdehyde dehydrogenase
Q6A2H0
-
succinic semialdehyde dehydrogenase
Q6A2H2
-
succinic semialdehyde dehydrogenase
-
-
succinic semialdehyde dehydrogenase
-
-
succinyl semialdehyde dehydrogenase
-
-
-
-
YneI dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-95-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain BW25113
-
-
Manually annotated by BRENDA team
strain BW25113
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M5a1
M5a1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-dioxopentanoate + NAD+ + H2O
?
show the reaction diagram
Q97XS9, -
no activity in presence of NADP+
-
-
?
2-carboxybenzaldehyde + NAD+ + H2O
2-carboxybenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde
-
-
?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 3% activity compared to succinate semialdehyde
-
-
?
2-phenylacetaldehyde + NAD+ + H2O
2-phenylbenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 5% activity compared to succinate semialdehyde
-
-
?
2-tolualdehyde + NAD+ + H2O
2-carboxytoluene + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH
show the reaction diagram
-
low activity
-
-
?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
3-carboxybenzaldehyde + NAD(P)+ + H2O
3-carboxybenzoate + NAD(P)H + H+
show the reaction diagram
B0JFD4
-
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 20% activity compared to succinate semialdehyde
-
-
?
3-carboxybenzaldehyde + NAD+ + H2O
3-carboxybenzoate + NADH + H+
show the reaction diagram
-
about 35% activity compared to succinate semialdehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde, about 2% activity compared to succinate semialdehyde
-
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
show the reaction diagram
-
about 3% activity compared to succinate semialdehyde
-
-
?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
show the reaction diagram
-
about 10% activity compared to succinate semialdehyde
-
-
?
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 5% activity compared to succinate semialdehyde
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
show the reaction diagram
-
about 15% activity compared to succinate semialdehyde
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 20% activity compared to succinate semialdehyde
-
-
?
3-tolualdehyde + NAD+ + H2O
3-tolubenzoate + NADH + H+
show the reaction diagram
-
about 10% activity compared to succinate semialdehyde
-
-
?
3-tolualdehyde + NAD+ + H2O
3-tolubenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 3% activity compared to succinate semialdehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-
low activity
-
-
?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
4-carboxybenzaldehyde + NAD(P)+ + H2O
4-carboxybenzoate + NAD(P)H + H+
show the reaction diagram
B0JFD4
-
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 10% activity compared to succinate semialdehyde
-
-
?
4-carboxybenzaldehyde + NAD+ + H2O
4-carboxybenzoate + NADH + H+
show the reaction diagram
-
about 65% activity compared to succinate semialdehyde
-
-
?
4-hydroxy-trans-2-nonenal + NAD+
?
show the reaction diagram
-
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+
show the reaction diagram
-
-
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde
-
-
?
4-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
show the reaction diagram
-
about 5% activity compared to succinate semialdehyde
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 15% activity compared to succinate semialdehyde
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
show the reaction diagram
-
about 30% activity compared to succinate semialdehyde
-
-
?
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-, Q1JUP4
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
2.3% of the activity with succinate semialdehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
about 10% activity compared to succinate semialdehyde
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Q8BWF0
about 5% activity compared to succinate semialdehyde
-
-
?
alpha-ketoglutaric semialdehyde + NAD+ + H2O
alpha-ketoglutarate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH
show the reaction diagram
-, Q1JUP4
-
-
-
?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
about 30% activity compared to succinate semialdehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 5% activity compared to succinate semialdehyde
-
-
?
betaine aldehyde + NAD+ + H2O
2-trimethylammonioacetate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
butanal + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
butanaldehyde + NAD+ + H2O
butanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
show the reaction diagram
-
25% of the activity with succinate semialdehyde
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
show the reaction diagram
-
13% of the activity with succinate semialdehyde
-
-
?
glyceraldehyde + NAD+ + H2O
glycerate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
glyoxylic acid + NAD+ + H2O
2-phenylbenzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 1% activity compared to succinate semialdehyde
-
-
?
heptanaldehyde + NAD+ + H2O
heptanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
hexanaldehyde + NAD+ + H2O
hexanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
iso-butanal + NAD+ + H2O
? + NADH + H+
show the reaction diagram
Q8BWF0
less than 10% activity compared to succinate semialdehyde
-
-
?
iso-butanal + NAD+ + H2O
isobutanoate + NADH + H+
show the reaction diagram
-
less than 10% activity compared to succinate semialdehyde
-
-
?
iso-pentanal + NAD+ + H2O
? + NADH + H+
show the reaction diagram
Q8BWF0
about 2% activity compared to succinate semialdehyde
-
-
?
iso-pentanal + NAD+ + H2O
isopentanoate + NADH + H+
show the reaction diagram
-
less than 5% activity compared to succinate semialdehyde
-
-
?
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
show the reaction diagram
-, Q1JUP4
-
-
-
?
m-carboxybenzaldehyde + NAD+ + H2O
m-carboxybenzoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
m-methylcarboxybenzaldehyde + NAD+ + H2O
m-methylcarboxybenzoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
show the reaction diagram
-
4.3% of the activity with succinate semialdehyde
-
-
?
malonate semialdehyde + NAD+ + H2O
malonate + NADH + 2 H+
show the reaction diagram
-
3.8% of the activity with succinate semialdehyde
-
-
?
methyl 3-formylbenzoate + NAD+ + H2O
3-(methoxycarbonyl)benzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 20% activity compared to succinate semialdehyde
-
-
?
methyl 3-formylbenzoate + NAD+ + H2O
3-(methoxycarbonyl)benzoate + NADH + H+
show the reaction diagram
-
about 45% activity compared to succinate semialdehyde
-
-
?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
show the reaction diagram
Q8BWF0
about 15% activity compared to succinate semialdehyde
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
show the reaction diagram
Q8BWF0
about 10% activity compared to succinate semialdehyde
-
-
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
show the reaction diagram
-
less than 60% activity compared to succinate semialdehyde
-
-
?
n-butanal + NAD+ + H2O
butanoic acid + NADH + 2 H+
show the reaction diagram
-
about 11% of the rate with succinic semialdehyde
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
-
about 110% activity compared to succinate semialdehyde
-
-
?
n-hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
Q8BWF0
less than 10% activity compared to succinate semialdehyde
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
show the reaction diagram
Q8BWF0
less than 10% activity compared to succinate semialdehyde
-
-
?
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
show the reaction diagram
-
less than 80% activity compared to succinate semialdehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
show the reaction diagram
Q9VBP6
-
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
show the reaction diagram
-
100% activity
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
show the reaction diagram
Q8BWF0
less than 20% activity compared to succinate semialdehyde
-
-
?
octanaldehyde + NAD+ + H2O
octanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
show the reaction diagram
-
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
show the reaction diagram
-
6.5% of the activity with succinate semialdehyde
-
-
?
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
show the reaction diagram
B0JFD4
-
-
-
?
pentanaldehyde + NAD+ + H2O
pentanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
propanal + NAD(P)+ + H2O
propanoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
Q8BWF0
less than 10% activity compared to succinate semialdehyde
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
-
less than 20% activity compared to succinate semialdehyde
-
-
?
propanaldehyde + NAD+ + H2O
propanoate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
-
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
5% of the activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
show the reaction diagram
B0JFD4
-
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
show the reaction diagram
Q9VBP6
cysteine 311 and glutamic acid 277 are likely candidates for the active site residues directly involved in catalysis
-
-
?
succinate semialdehyde + NAD+
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
-
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
Q8N3W7
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-, Q1JUP4
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
reverse reaction proceeds at 1/1230 of the rate of the forward eaction
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme of agmatine degradation
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme is involved in the catabolism of the neurotransmitter 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
induced by pyridine, the enzyme is involved in the degradation of pyridine
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
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
show the reaction diagram
Klebsiella pneumoniae M5a1
-
-, 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 + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
Q9SAK4
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
Q8BUF0
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
enzyme of the gamma-aminobutyrate shunt required to restrict levels of reactive oxygen intermediates in plants
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
Q8BWF0
100% activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
100% activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
show the reaction diagram
Q97XS9, -
no activity in presence of NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
Q8BWF0
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
activity with NAD+ is 10times higher than with NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
activity with NAD+ is about 7fold higher than activity with NADP+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
activity with NAD+ is about 7fold higher than activity with NADP+
-
-
ir
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
20% of the activity with NAD+
-
-
-
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
reaction with NADP+ is 13% of the activity with NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
-
reduction rate is only a few percent of that of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
Klebsiella pneumoniae M5a1
-
activity with NAD+ is 10times higher than with NADP+
-
-
?
trans-2-hexenal + NAD+ + H2O
trans-2-hexenoate + NADH + H+
show the reaction diagram
-
-
-
-
?
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
show the reaction diagram
-
about 30% activity compared to succinate semialdehyde
-
-
?
additional information
?
-
-
no activity with NADP+
-
-
-
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
?
-
Q9VBP6
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
?
-
-
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, 2-nitrobenzaldehyde, 2-carboxybenzaldehyde, 2-tolualdehyde, 4-tolualdehyde, 2-hydroxybenzaldehyde, 4-hydroxybenzaldehyde, 2-phenylacetaldedyde, and glyoxylic acid
-
-
-
additional information
?
-
Q8BWF0
no activity towards 2-methoxybenzaldehyde, and 4-tolualdehyde
-
-
-
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
?
-
Q97XS9, -
formaldehyde, betaine aldehyde and benzaldehyde can not serve as substrates
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxy-trans-2-nonenal + NAD+
?
show the reaction diagram
-
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
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme of agmatine degradation
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme is induced by growth on gamma-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
enzyme is involved in the catabolism of the neurotransmitter 4-aminobutyrate
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
-
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
show the reaction diagram
-
induced by pyridine, the enzyme is involved in the degradation of pyridine
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
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 + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
ir
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
Q9SAK4
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
enzyme of the gamma-aminobutyrate shunt required to restrict levels of reactive oxygen intermediates in plants
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
Klebsiella pneumoniae M5a1
-
enzyme is induced by succinate semialdehyde, functions in the oxidation of succinate semialdehyde during growth on both 4-hydroxyphenylacetate and 4-aminobutyrate
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
show the reaction diagram
-
-
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
-
-
3-acetylpyridine adenine dinucleotide
-
reduced at nearly the same rate as NAD+
NAD+
-
required
NAD+
Q8BWF0
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive
NAD+
Q97XS9, -
no activity in presence of NADP+
NADP+
-
cofactor; reduction rate is only a few percent of that of NAD+
NADP+
-
activity with NAD+ is 10times higher than with NADP+; cofactor
NADP+
-
cofactor
NADP+
-
cofactor
NADP+
Q9VBP6
is also accepted as coenzyme substrate but leads to 7fold lower reaction rates compared to NAD+ at saturating succinate semialdehyde concentrations
deamino-NAD+
-
reduced at nearly the same rate as NAD+
additional information
-
no activity with NADP+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
5 mM, 84% activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutaric semialdehyde
Q97XS9, -
substrate inhibition
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+
4-hydroxy-trans-2-nonenal
-
IC50: 0.11 mM
4-hydroxybenzaldehyde
-
-
4-hydroxybenzaldehyde
-
-
4-hydroxybenzaldehyde
-
-
4-hydroxybenzaldehyde
-
-
4-hydroxybenzaldehyde
-
-
4-hydroxybenzaldehyde
-
10 mM, 82% inhibition
4-hydroxybenzaldehyde
Q8BWF0
more than 95% inhibition at 0.05 mM
4-hydroxybenzaldehyde
-
more than 95% inhibition at 0.05 mM
4-Methoxybenzaldehyde
Q8BWF0
-
4-Methoxybenzaldehyde
-
-
4-tolualdehyde
Q8BWF0
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.01 mM, 66% residual activity
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
acetaldehyde
-
1 mM, 40% inhibition
acetaldehyde
-
above 1 mM
acrolein
-
irreversible, noncompetitive, IC50: 0.015 mM
AMP
-
1 mM, 17% inhibition
arsenite
-
-
benzaldehyde
-
-
Chloral hydrate
-
-
Disulfiram
-
-
Disulfiram
-
0.01 mM
Dithionitrobenzoate
-
-
glyoxylate
-
1 mM, 33% inhibition
iodoacetamide
-
-
m-hydroxybenzaldehyde
-
-
m-hydroxybenzaldehyde
-
-
N-ethylmaleimide
-
0.1 mM, complete loss of activity
N-Formylglycine
-
4 mM, 40% inhibition, reversible, competitive with respect to succinate semialdehyde, uncompetitive with respect to NAD+
NAD+
Q97XS9, -
substrate inhibition
NADH
-
competitive with respect to NAD+; mixed with respect to succinate semialdehyde
NADH
-
competitive with NAD+
NADH
-
competitive with respect to NAD+
NADH
-
NADH is a strong competitive inhibitor with respect to NAD+ and behaves as a non-competitive inhibitor with respect to succinate semialdehyde
o-phthalaldehyde
-
binding of 10 mol per mol of enzyme results in irreversible loss of activity
p-bromobenzaldehyde
-
1 mM, 38% inhibition
p-chlorobenzaldehyde
-
1 mM, 38% inhibition
p-Chloromercuriphenyl sulfonate
-
-
p-ethoxybenzaldehyde
-
1 mM, 19% inhibition
p-ethylbenzaldehyde
-
1 mM, 51% inhibition
p-fluorobenzaldehyde
-
1 mM, 19% inhibition
p-hydroxymercuribenzoate
-
-
p-iodobenzaldehyde
-
1 mM, 52% inhibition
p-isopropylbenzaldehyde
-
1 mM, 19% inhibition
p-Methoxybenzaldehyde
-
1 mM, 19% inhibition
p-methylbenzaldehyde
-
1 mM, 64% inhibition
p-nitrobenzaldehyde
-
1 mM, 20% inhibition
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
pyridoxal 5'-phosphate
-
NAD+ protects
pyridoxal 5'-phosphate
-
10 mM, 25% inhibition
Succinate semialdehyde
-
substrate inhibition above 2 mM
Succinate semialdehyde
-
substrate inhibition, uncompetitive with respect to NAD+
Succinate semialdehyde
-
-
Succinate semialdehyde
-
-
Succinate semialdehyde
-
substrate inhibition above 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
B0JFD4
inhibition by the succinate semialdehyde substrate is starting already at a concentration as low as 0.02 mM
Succinate semialdehyde
Q8BWF0
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
-
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
Q97XS9, -
substrate inhibition
Valeraldehyde
-
-
Zn2+
-
1 mM, 43% inhibition
additional information
-
no inhibition by 0.1 mM trans-2-hexenal and 0.1 mM crotonaldehyde
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activates
2-mercaptoethanol
-
strongly dependent on presence of
2-mercaptoethanol
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
2-mercaptoethanol
-
loss of about 50% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol
dithiothreitol
-
1 mM, 17% activation
dithiothreitol
-
activates
dithiothreitol
-
requirement of sulfhydryl protective reagent, maximal activity with 10 mM to 0.1 M dithiothreitol or mercaptoethanol
glutathione
-
activates
sodium lauryl sulfate
-
low concentrations activate to a small extent
L-Cys
-
activates
additional information
-
gene yneI is responsible for NAD+/NADP+-SSADH activity. The gene is induced by succinate semialdehyde
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
2,5-dioxopentanoate
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
0.1035
-
3-(methoxycarbonyl)benzoate
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.05
-
3-acetylpyridine adenine dinucleotide
-
-
0.017
-
3-carboxybenzaldehyde
-
-
0.0331
-
3-carboxybenzaldehyde
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.112
-
3-carboxybenzaldehyde
B0JFD4
-
0.1418
-
3-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0502
-
3-Nitrobenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.287
-
3-Nitrobenzaldehyde
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0121
-
4-carboxybenzaldehyde
-
-
0.0151
-
4-carboxybenzaldehyde
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0312
-
4-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0776
-
4-carboxybenzaldehyde
B0JFD4
-
0.115
-
4-carboxybenzaldehyde
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.1668
-
4-carboxybenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0503
-
4-hydroxy-trans-2-nonenal
-
recombinant enzyme
0.156
-
4-Nitrobenzaldehyde
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.1612
-
4-Nitrobenzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.875
-
acetaldehyde
-
-
0.9
-
acetaldehyde
-
-
2.797
-
acetaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
3.16
-
acetaldehyde
-
mutant enzyme R166K, at 37C, in 40 mM sodium phosphate, pH 7.4
4.076
-
acetaldehyde
-
-
4.3
-
acetaldehyde
-
wild type enzyme, at 37C, in 40 mM sodium phosphate, pH 7.4
4.5
-
acetaldehyde
-
mutant enzyme R166H, at 37C, in 40 mM sodium phosphate, pH 7.4
4.82
-
acetaldehyde
-
mutant enzyme R166E, at 37C, in 40 mM sodium phosphate, pH 7.4
0.011
-
alpha-Ketoglutaric semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
0.0159
-
alpha-Ketoglutaric semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25C
0.019
-
benzaldehyde
-
-
0.167
-
benzaldehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.241
-
benzaldehyde
-
-
0.105
-
Butanal
-
-
0.0163
-
Glutaraldehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
0.0034
-
Glutaric semialdehyde
-
-
0.061
-
n-Butanal
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.106
-
n-Butanal
Q9VBP6
-
0.323
-
n-Butanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0253
-
n-Hexanal
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.051
-
n-Hexanal
Q9VBP6
-
0.107
-
n-Hexanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0514
-
n-octanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.137
-
n-octanal
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0287
-
n-Pentanal
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.057
-
n-Pentanal
Q9VBP6
-
0.096
-
n-Pentanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0025
-
NAD+
-
-
0.021
-
NAD+
-
wild type enzyme, at 37C, in 40 mM sodium phosphate, pH 7.4
0.031
-
NAD+
-
-
0.035
-
NAD+
-
mutant enzyme R166E, at 37C, in 40 mM sodium phosphate, pH 7.4
0.038
-
NAD+
-
pH 9.0, 37C
0.04
-
NAD+
-
-
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 22C
0.044
-
NAD+
-
mutant enzyme R166A, at 37C, in 40 mM sodium phosphate, pH 7.4
0.063
-
NAD+
-
mutant enzyme R166H, at 37C, in 40 mM sodium phosphate, pH 7.4
0.0667
-
NAD+
-
-
0.071
-
NAD+
-
pH 8.3, 35C
0.081
-
NAD+
-
mutant enzyme R166K, at 37C, in 40 mM sodium phosphate, pH 7.4
0.0909
-
NAD+
Q9VBP6
-
0.13
-
NAD+
-
-
0.2
-
NAD+
-
-
0.227
-
NAD+
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.227
-
NAD+
-
pH and temperature not specified in the publication
0.31
-
NAD+
-
-
0.348
-
NAD+
B0JFD4
-
9.1
-
NAD+
Q97XS9, -
pH 6.5, 70C
125
-
NAD+
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25C
0.552
-
NADP+
B0JFD4
-
0.616
-
NADP+
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
1.2
-
NADP+
Q9VBP6
-
0.033
-
p-nitrobenzaldehyde
-
-
0.025
-
Pentanal
-
-
0.0827
-
Pentanal
B0JFD4
-
1.212
-
propanal
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
1.606
-
propanal
-
-
1.622
-
propanal
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.58
-
propionaldehyde
-
-
0.85
-
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
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.00256
-
Succinate semialdehyde
-
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.0027
0.0029
Succinate semialdehyde
-
-
0.0027
-
Succinate semialdehyde
B0JFD4
-
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
Q9VBP6
-
0.0074
-
Succinate semialdehyde
-
-
0.01053
-
Succinate semialdehyde
-
-
0.0109
-
Succinate semialdehyde
-
mutant enzyme R166K, at 37C, in 40 mM sodium phosphate, pH 7.4
0.013
-
Succinate semialdehyde
-
wild type enzyme, at 37C, in 40 mM sodium phosphate, pH 7.4
0.015
-
Succinate semialdehyde
-
-
0.0159
-
Succinate semialdehyde
-
-
0.03
-
Succinate semialdehyde
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
0.0385
-
Succinate semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
0.047
-
Succinate semialdehyde
-
pH 9.0, 37C
0.1
-
Succinate semialdehyde
-
-
0.16
-
Succinate semialdehyde
-
pH 8.3, 35C
0.62
-
Succinate semialdehyde
-
mutant enzyme R166E, at 37C, in 40 mM sodium phosphate, pH 7.4
1.13
-
Succinate semialdehyde
-
mutant enzyme R166H, at 37C, in 40 mM sodium phosphate, pH 7.4
1.6
-
Succinate semialdehyde
-
mutant enzyme R166A, at 37C, 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, 25C
0.0589
-
trans-2-hexenal
-
recombinant enzyme
0.218
-
methyl 3-formylbenzoate
Q8BWF0
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.1
-
2,5-dioxopentanoate
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
12.3
-
alpha-Ketoglutaric semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NADP+. 25C
51.2
-
alpha-Ketoglutaric semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
12.3
-
Glutaraldehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
69
-
NAD+
Q97XS9, -
pH 6.5, 70C
22.6
-
Succinate semialdehyde
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
31.7
-
Succinate semialdehyde
-, Q1JUP4
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
21.4
-
2,5-dioxopentanoate
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
1964
7.6
-
NAD+
Q97XS9, -
pH 6.5, 70C
14330
842
-
Succinate semialdehyde
Q97XS9, -
pH 6.5, 70C, cofactor NAD+
16755
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
NADH
-
succinate semialdehyde as varied substrate
0.128
-
NADH
-
NAD+ as varied substrate
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.11
-
4-hydroxy-trans-2-nonenal
-
IC50: 0.11 mM
0.1
-
4-Methoxybenzaldehyde
-
-
2
-
4-Methoxybenzaldehyde
Q8BWF0
-
0.1
-
4-tolualdehyde
-
-
1
-
4-tolualdehyde
Q8BWF0
-
0.015
-
acrolein
-
irreversible, noncompetitive, IC50: 0.015 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.25
-
-
pH 8.3, 35C
5.3
-
-
-
33.2
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
Q97XS9, -
assay at
8
9.5
-
-
8
-
B0JFD4
-
8.5
-
-
-
8.6
-
-
-
8.7
9.1
-
-
9.5
-
-
-
10.5
-
-
activity with succinate semialdehyde and 3-aminopropanal
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.5
Q9VBP6
at pH 8.5 MalE-DmSSADH is 10fold more active than at pH 6.0
7
10
-
pH 7.0: about 40% of maximal activity, pH 10.0: about 35% of maximal activity
7
10
-
about 50% of maximal activity at pH 7.0 and at pH 10.0
8
10
-
pH 8.0: about 40% of maximal activity, pH 10.0: about 55% of maximal activity
8
9
-
at least 80% of its optimal 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
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
Q9VBP6
optimal expression of pMalc2x-DmSSADH in Escherichia coli TB1
37
-
-
assay at
70
-
Q97XS9, -
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.66
-
-
computer prediction
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
low mRNA expression compared to other tissues
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
mRNA expression
Manually annotated by BRENDA team
-
fetal kidney
Manually annotated by BRENDA team
-
highest mRNA expression
Manually annotated by BRENDA team
-
mRNA expression
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
YneI protein
52000
-
-
gel filtration
52000
-
B0JFD4
deduced protein without the mitochondria import sequence
52100
-
-
deduced protein without the mitochondria import sequence
52230
-
-
calculated from sequence, SDS-PAGE
55000
-
-, Q1JUP4
SDS-PAGE
55400
-
-
deduced protein with the mitochondria import sequence
55400
-
B0JFD4
deduced protein with the mitochondria import sequence
98000
-
Q8BWF0
SDS-PAGE
98000
-
-
SDS-PAGE
120000
-
-
gel filtration
130000
-
-
gel filtration
140000
-
-
gel filtration
145000
-
-
gel filtration
145000
-
-
gel filtration
150000
-
-
gel filtration
157000
-
Q97XS9, -
gel filtration
160000
-
-
non-denaturing PAGE, gel filtration
164000
-
-
gel filtration
191000
-
-
-
200000
-
-
gel filtration
220000
-
-, Q1JUP4
gel-filtration
225000
-
-
gel filtration
232000
245000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 61000 + x * 63000, SDS-PAGE
?
-
x * 53000, SDS-PAGE
?
-
x * 50000, SDS-PAGE; x * 54430, MALDI-MS
?
Q9VBP6
x * 98200, SDS-PAGE
dimer
-
2 * 69000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
homotetramer
-
4 * 58000
homotetramer
-
-
tetramer
-
4 * 35000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-, Q1JUP4
4 * 55000, gel-filtration, SDS-PAGE
tetramer
-
4 * 52000, gel-filtration
trimer
-
3 * 54500, SDS-PAGE
homotrimer
Q97XS9, -
3 * 50000, SDS-PAGE; 3 * 51500, calculated from sequence
additional information
-
4-aminobutyrate aminotransferase and succinate semialdehyde dehydrogenase form a stable enzymatic complex under in vivo conditions
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
18C, 1 h, about 20% loss of activity
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
6
9
-
18C, 1 h, stable
7
9
-
4C, 18 h, stable
8
-
-
rapid decrease in stability above
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
40
-
pH 8.9, 10 min, stable
18
-
-
14 h, 93% residual activity
37
-
-
14 h, 92% residual activity
40
-
-
stable up to
50
-
-
pH 7.4, 8 min, complete inactivation. Mercaptoethanol stabilizes for 20 min or longer
60
-
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
denaturation by sodium lauryl sulfate
-
NAD+ and mercaptoethanol effectively protect from auto-oxidation. NAD+ does not prevent auto-oxidation in presence of urea
-
freezing in absence of glycerol results in inactivation
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
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
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, 100 mM sodium phosphate, pH 8.5, 1mM DTT, 43% glycerol, 3 years
Q9VBP6
-15C, 14 h, 95% residual activity
-
18C, 14 h, 93% residual activity
-
5C, unstable unless 30% glycerol is added
-
-20C, in presence of 10% v/v glycerol, stable for several months
-
-20C, 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
-
0-2C, 24 h, 50% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni-affinity chromatography
-, Q1JUP4
by Ni2+-NTA agarose chromatography
Q9VBP6
His-tagged YneI dehydrogenase purified from cell extracts with HiTrap affinity columns
-
2 isoenzymes
-
Ni-affinity chromatography
-
Ni2+-NTA agarose column chromatography
Q8BWF0
Ni2+-NTA agarose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli as His-tag fusion protein
-, Q1JUP4
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
Q9VBP6
overexpressed as His-tagged YneI
-
expression in Escherichia coli as His-tag fusion protein
-
expression of mutant enzymes is expressed after transfection of HEK293 cells
-
transfection of HEK 293 cells
Q8N3W7
into vectors pQE30 and into pMalc2x. Expression in Escherichia coli strains M15 and TB1
B0JFD4
expressed in Escherichia coli M15 cells
Q8BWF0
expressed in Escherichia coli Rosetta 2 (DE3) cells
-
expressed in Escherichia coli M15 cells
-
expression in Escherichia coli
Q97XS9, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
induced by growth of cells on gamma-aminobutanoate
-
induction by growth on glutamate
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C196A
Q9VBP6
loss in specific activity of 55%
C196S
Q9VBP6
loss in specific activity of 74%
C243S
Q9VBP6
loss in specific activity of 70%
C311A
Q9VBP6
decreased SSADH activity to undetectable levels
C311S
Q9VBP6
decreased SSADH activity to undetectable levels
C502S
Q9VBP6
loss in specific activity of 93%
E277D
Q9VBP6
leads to a product with similar specific activity
E277K
Q9VBP6
charge inversion, which results in recombinant protein totally devoid of detectable SSADH activity
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
Q8N3W7
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
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
-
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
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
Q8N3W7
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
G46R
-
the mutant shows 87% 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
Q8N3W7
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
-
the mutant shows 83% activity compared to the wild type enzyme
H180Y
-
mutant with activity reduction
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
Q8N3W7
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
-
the mutant shows 48% activity compared to the wild type enzyme
P182L
-
mutant with significant activity reduction
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
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
E277Q
Q9VBP6
concomitant loss of the negative charge, which results in recombinant protein totally devoid of detectable SSADH activity
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
-
T233M
-
the mutant shows 4% activity compared to the wild type enzyme
additional information
Q8BUF0
Aldh5a1-/- mice show abnormalities of respiratory chain function. Hippocampus and cortex are primary targets for neurodegeneration
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q8BUF0
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
additional information
-
genomic copy of the SSADH gene is devoid of 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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medicine
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succinic semialdehyde dehydrogenase deficient patients show widespread reduction in benzodiazepine receptor binding on [(11)C]-flumazenil-positron emission tomography
additional information
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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
B0JFD4
genomic copy of the SSADH gene contains two introns. Multiple SSADH gene copies are present in the genome