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Information on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+) and Organism(s) Homo sapiens and UniProt Accession P51649
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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
-
ssadhd
-
4-hydroxybutyric
- propionaldehyde
- trans-4-hydroxy-2-nonenal
- aldh4a1
-
akr7a2
-
ssadh-deficient
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
succinic semialdehyde dehydrogenase
-
dehydrogenase, succinate semialdehyde
-
-
-
-
NAD(+)-dependent succinic semialdehyde dehydrogenase
-
-
-
-
SSADH
succinate semialdehyde dehydrogenase
succinate semialdehyde:NAD+ oxidoreductase
-
-
-
-
succinic semialdehyde dehydrogenase
succinyl semialdehyde dehydrogenase
-
-
-
-
SSADH
-
-
-
-
succinate semialdehyde dehydrogenase
-
-
-
-
succinic semialdehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -
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+.
CAS REGISTRY NUMBER
COMMENTARY
9028-95-9
-
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
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
2.3% of the activity with succinate semialdehyde
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
-
13% of the activity with succinate semialdehyde
-
-
?
m-nitrobenzaldehyde + NAD+ + H2O
m-nitrobenzoate + NADH
-
4.3% of the activity with succinate semialdehyde
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
-
6.5% of the activity with succinate semialdehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
-
5% of the activity with succinate semialdehyde
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
-
20% of the activity with NAD+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
last enzyme in catabolism of 4-aminobutyric acid. Human SSADH deficiency results in 4-hydroxybutyric aciduria, an autosomal recessive disorder due to an accumulation of 4-aminobutyric acid and 4-hydroxybutyric acid in the CNS
-
-
ir
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
-
-
?
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+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH
last enzyme in catabolism of 4-aminobutyric acid. Human SSADH deficiency results in 4-hydroxybutyric aciduria, an autosomal recessive disorder due to an accumulation of 4-aminobutyric acid and 4-hydroxybutyric acid in the CNS
-
-
ir
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
NADH is a strong competitive inhibitor with respect to NAD+ and behaves as a non-competitive inhibitor with respect to succinate semialdehyde
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
succinate semialdehyde
pH and temperature not specified in the publication
125
NAD+
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C
6.3
succinate semialdehyde
-
50 microM succinate semialdehyde, 3 mM NAD+, 0.1 M sodium diphosphate pH 8.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
glioma cells, SSADH protein level differences in IDH1m and 2-HG-treated U251 wild-type cells
additional information
no expression of enzyme SSADH in U-87MG and U-373MG cells
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
brain stem, cerebellar dentate nuclei, globus pallidus, and subthalamic nuclei
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
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
malfunction
GABA addition to glioma cells increased proliferation rates. Expression of mutated IDH1 and treatment with 2-HG reduced glutamine and GABA oxidation, diminishes the pro-proliferative effect of GABA in succinic semialdehyde dehydrogenase (SSADH) expressing cells. The enzyme SSADH is overexpressed in almost all glioma cells. No significant association between SSADH expression and clinicopathological parameters (e.g. IDH mutation). IDH mutation and 2-HG production inhibit GABA oxidation in glioma cells
malfunction
succinic semialdehyde dehydrogenase deficiency (SSADHD) is a rare autosomal-recessively inherited metabolic disorder of GABA catabolism that results in the accumulation of 4-hydroxybutyrate (GHB) in tissues, cerebrospinal fluid, blood and urine. The clinical phenotype of SSADHD is highly variable, ranging from mild intellectual and developmental disabilities to severe neurological defects such as seizures, hypotonia, ataxia and behavioural problems, especially in older patients. The most common abnormalities on cerebral MRI consist of increased T2-weighted signal involving the cerebellar dentate nuclei, globus pallidus, and subthalamic nuclei symmetrically, as well as the subcortical white matter and brainstem. In SSADHD, the final step of the GABA degradation pathway shifts towards a massive reduction of SSA to gamma-hydroxybutyrate (GHB) through either specific or non-specific oxidoreductase reactions. The abnormal accumulation of GHB, eventually excreted in urine, is the pathognomonic disease marker
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
the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)
metabolism
astrocytomas and oligodendrogliomas, collectively called diffuse gliomas, are derived from astrocytes and oligodendrocytes that are in metabolic symbiosis with neurons. Astrocytes can catabolize neuron-derived glutamate and gamma-aminobutyric acid (GABA) for supporting and regulating neuronal functions. Succinic semialdehyde dehydrogenase (SSADH) expression is correlated to GABA oxidation. SSADH expression may participate in the oxidation and/or consumption of GABA in gliomas, furthermore, GABA oxidation capacity may contribute to proliferation and worse prognosis of gliomas
physiological function
enzyme SSADH is a NAD+-dependent mitochondrial homotetrameric allosteric enzyme and works with gamma-aminobutyric acid (GABA) transaminase to convert GABA to succinic semialdehyde (SSA) which is, in turn, oxidized by SSADH to succinic acid. Besides its established role in GABA catabolism, SSADH is reported to contribute to the antioxidative mitochondrial defence by oxidation of 4-hydroxynonenal, a degradation end product of peroxidated lipids
physiological function
GABA can feed the TCA cycle via the activities of GABA transaminase and succinic semialdehyde dehydrogenase (SSADH) to produce succinate. Potential role of GABA shunt and SSADH activity in the survival and the proliferation of SSADH expressing U-251 wild-type cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SSDH_HUMAN
535
0
57215
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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
each SSADH monomer comprises an N-terminal domain (for NAD+ binding), a catalytic domain (for SSA recognition), and an oligomerization beta-structured domain. In a dynamic catalytic loop, Cys340 and Glu306 are involved in SSA binding and oxidation. Analysis of the tetramer stability by in silico protein modelling analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A237S
A237S/T423S
naturally occuring mutation, the mutant shows about 70% reduced activity compared to wild-type
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
G176R/H180Y
naturally occuring mutation, the p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity
G176R/H180Y/A237S/T423S
naturally occuring mutation, an Italian SSADHD patient shows heterozygosity for four missense mutations: c.526G>A (p.G176R), c.538C>T (p.H180Y), c.709G>T (p.A237S) and c.1267A>T (p.T423S). The p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity. Clinical and cognitive evaluations, phenotype, overview
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
A273S
C223R
-
missense mutation associated with a dramatic reduction of enzyme activity
G36R
H180Y
P182L
additional information
lowest stability for the tetramer constituted by G176R/H180Y monomers and the highest stability for that constituted by A237S/T423S monomers. The combination of the two double mutant alleles produces a synergic negative effect on SSADH enzyme activity and stability, thus resulting in SSADHD phenotype
A237S
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 65% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
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
G176R
the mutant shows less than 1% activity compared to the wild type enzyme
G176R
naturally occuring mutation, the p.G176R change, alone or in combination with p.H180Y, causes the abolishment of enzyme activity. Amino acid replacements G176R and H180Y are located in the same beta-segment that is at the interface between the monomers. The introduction of the positive charges of arginines, in presence of the bulky sidechains of tyrosines, could inhibit the correct tetramer assembly, thus causing instability
G268E
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G268E
the mutant shows less than 1% activity compared to the wild type enzyme
G36R
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 87% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G409D
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G409D
the mutant shows less than 1% activity compared to the wild type enzyme
G533R
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, less than 1% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
G533R
the mutant shows less than 1% activity compared to the wild type enzyme
H180Y
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 83% of the succinate semialdehyde dehydrogenase activity of the wild-type enzyme
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
P382L
missense mutation of patient with succinate semialdehyde dehydrogenase deficiency, 2% 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
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
H180Y
naturally occuring missense variant expressed in HEK293 cells, 82.5% of the SSADH 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
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 was switched back to a reduced state
710898
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of mutant enzymes is expressed after transfection of HEK293 cells
gene ALDH5A1 gene, located in the 6p22.3 region, genotyping, recombinant epression of wild-type and mutant enzymes in HEK-293 cells, quantitative RT-PCR expression analysis
gene ALDH5A1, screening and genotyping, DNA and amino acid sequence determination and analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
GABA oxidation and SSADH activity might be additional therapeutic targets in gliomas/glioblastomas
medicine
-
succinic semialdehyde dehydrogenase deficient patients show widespread reduction in benzodiazepine receptor binding on [(11)C]-flumazenil-positron emission tomography
additional information
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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)
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 (Q8N3W7), Homo sapiens
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 (Q3MSM4), Pan paniscus, Pan troglodytes (Q6A2H0), Pan troglodytes, Pongo abelii (Q6A2H2), Pongo pygmaeus pygmaeus (Q6A2H2)
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
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
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)
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 (P51649), Homo sapiens
Knerr, I.; Gibson, K.M.; Jakobs, C.; Pearl, P.L.
Neuropsychiatric morbidity in adolescent and adult succinic semialdehyde dehydrogenase deficiency patients
CNS Spectr.
13
598-605
2008
Homo sapiens
Malaspina, P.; Picklo, M.J.; Jakobs, C.; Snead, O.C.; Gibson, K.M.
Comparative genomics of aldehyde dehydrogenase 5a1 (succinate semialdehyde dehydrogenase) and accumulation of gamma-hydroxybutyrate associated with its deficiency
Hum. Genomics
3
106-120
2009
Homo sapiens
Pearl, P.L.; Gibson, K.M.; Cortez, M.A.; Wu, Y.; Carter Snead, O.; Knerr, I.; Forester, K.; Pettiford, J.M.; Jakobs, C.; Theodore, W.H.
Succinic semialdehyde dehydrogenase deficiency: lessons from mice and men
J. Inherit. Metab. Dis.
32
343-352
2009
Homo sapiens, Mus musculus
Kratz, S.V.
Sensory integration intervention: historical concepts, treatment strategies and clinical experiences in three patients with succinic semialdehyde dehydrogenase (SSADH) deficiency
J. Inherit. Metab. Dis.
32
353-360
2009
Homo sapiens
Di Rosa, G.; Malaspina, P.; Blasi, P.; Dionisi-Vici, C.; Rizzo, C.; Tortorella, G.; Crutchfield, S.R.; Gibson, K.M.
Visual evoked potentials in succinate semialdehyde dehydrogenase (SSADH) deficiency
J. Inherit. Metab. Dis.
32
S201-S205
2009
Homo sapiens
Pearl, P.L.; Gibson, K.M.; Quezado, Z.; Dustin, I.; Taylor, J.; Trzcinski, S.; Schreiber, J.; Forester, K.; Reeves-Tyer, P.; Liew, C.; Shamim, S.; Herscovitch, P.; Carson, R.; Butman, J.; Jakobs, C.; Theodore, W.
Decreased GABA-A binding on FMZ-PET in succinic semialdehyde dehydrogenase deficiency
Neurology
73
423-429
2009
Homo sapiens
Langendorf, C.G.; Key, T.L.; Fenalti, G.; Kan, W.T.; Buckle, A.M.; Caradoc-Davies, T.; Tuck, K.L.; Law, R.H.; Whisstock, J.C.
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions
PLoS One
5
e9280
2010
Homo sapiens (P51649)
Kim, K.J.; Pearl, P.; Jensen, K.; Snead, O.C.; Malaspina, P.; Jakobs, C.; Gibson, K.M.
Succinic semialdehyde dehydrogenase (SSADH): biochemical-molecular-clinical disease mechanisms, redox regulation and functional significance
Antioxid. Redox Signal.
15
691-718
2011
Homo sapiens (P51649), Homo sapiens, Mus musculus
Puettmann, L.; Stehr, H.; Garshasbi, M.; Hu, H.; Kahrizi, K.; Lipkowitz, B.; Jamali, P.; Tzschach, A.; Najmabadi, H.; Ropers, H.H.; Musante, L.; Kuss, A.W.
A novel ALDH5A1 mutation is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability in an Iranian family
Am. J. Med. Genet. A
161A
1915-1922
2013
Homo sapiens (P51649), Homo sapiens
Tamazian, G.; Ho Chang, J.; Knyazev, S.; Stepanov, E.; Kim, K.J.; Porozov, Y.
Modeling conformational redox-switch modulation of human succinic semialdehyde dehydrogenase
Proteins
83
2217-2229
2015
Homo sapiens (P51649)
Hujber, Z.; Horvath, G.; Petoevari, G.; Krencz, I.; Danko, T.; Meszaros, K.; Rajnai, H.; Szoboszlai, N.; Leenders, W.P.J.; Jeney, A.; Tretter, L.; Sebestyen, A.
GABA, glutamine, glutamate oxidation and succinic semialdehyde dehydrogenase expression in human gliomas
J. Exp. Clin. Cancer Res.
37
271
2018
Homo sapiens (P51649)
Menduti, G.; Biamino, E.; Vittorini, R.; Vesco, S.; Puccinelli, M.P.; Porta, F.; Capo, C.; Leo, S.; Ciminelli, B.M.; Iacovelli, F.; Spada, M.; Falconi, M.; Malaspina, P.; Rossi, L.
Succinic semialdehyde dehydrogenase deficiency The combination of a novel ALDH5A1 gene mutation and a missense SNP strongly affects SSADH enzyme activity and stability
Mol. Genet. Metab.
124
210-215
2018
Homo sapiens (P51649)
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