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 hide
1.2.1.24
-
RECOMMENDED NAME
GeneOntology No.
succinate-semialdehyde dehydrogenase (NAD+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation I
-
-
4-aminobutanoate degradation IV
-
-
Alanine, aspartate and glutamate metabolism
-
-
Butanoate metabolism
-
-
GABA shunt
-
-
glutamate and glutamine metabolism
-
-
L-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+.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-95-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BW25113
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
M5a1
-
-
Manually annotated by BRENDA team
M5a1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-dioxopentanoate + NAD+ + H2O
?
show the reaction diagram
no activity in presence of NADP+
-
-
?
2-carboxybenzaldehyde + NAD+ + H2O
2-carboxybenzoate + NADH + H+
show the reaction diagram
about 1% activity compared to succinate semialdehyde
-
-
?
2-hydroxybenzaldehyde + NAD+ + H2O
2-hydroxybenzoate + NADH + H+
show the reaction diagram
about 1% activity compared to succinate semialdehyde
-
-
?
2-nitrobenzaldehyde + NAD+ + H2O
2-nitrobenzoate + NADH + H+
show the reaction diagram
about 3% activity compared to succinate semialdehyde
-
-
?
2-phenylacetaldehyde + NAD+ + H2O
2-phenylbenzoate + NADH + H+
show the reaction diagram
about 5% activity compared to succinate semialdehyde
-
-
?
2-tolualdehyde + NAD+ + H2O
2-carboxytoluene + NADH + H+
show the reaction diagram
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+ + H2O
3-carboxybenzoate + NADH + H+
show the reaction diagram
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
show the reaction diagram
3-methoxy-benzaldehyde + NAD+ + H2O
3-methoxy-benzoate + NADH + H+
show the reaction diagram
3-methylbenzaldehyde + NAD+ + H2O
3-methylbenzoate + NADH + H+
show the reaction diagram
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
show the reaction diagram
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+ + H2O
4-carboxybenzoate + NADH + H+
show the reaction diagram
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-methoxy-benzaldehyde + NAD+ + H2O
4-methoxy-benzoate + NADH + H+
show the reaction diagram
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
show the reaction diagram
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
alpha-ketoglutaric semialdehyde + NAD+ + H2O
alpha-ketoglutarate + NADH
show the reaction diagram
-
-
-
?
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH
show the reaction diagram
-
-
-
?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
2-trimethylammonioacetate + NADH
show the reaction diagram
-
-
-
?
butanal + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
butanaldehyde + NAD+ + H2O
butanoate + NADH
show the reaction diagram
-
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
-
-
?
glutaraldehyde + NAD+ + H2O
glutarate + NADH
show the reaction diagram
-
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH
show the reaction diagram
glyceraldehyde + NAD+ + H2O
glycerate + NADH
show the reaction diagram
-
-
-
?
glycoaldehyde + NAD+ + H2O
glycolate + NADH
show the reaction diagram
-
-
-
?
glyoxylic acid + NAD+ + H2O
2-phenylbenzoate + NADH + H+
show the reaction diagram
about 1% activity compared to succinate semialdehyde
-
-
?
heptanaldehyde + NAD+ + H2O
heptanoate + NADH
show the reaction diagram
-
-
-
?
hexanaldehyde + NAD+ + H2O
hexanoate + NADH
show the reaction diagram
-
-
-
?
iso-butanal + NAD+ + H2O
? + NADH + H+
show the reaction diagram
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
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
-
-
-
?
m-carboxybenzaldehyde + NAD+ + H2O
m-carboxybenzoate + NADH + H+
show the reaction diagram
-
-
-
?
m-methylcarboxybenzaldehyde + NAD+ + H2O
m-methylcarboxybenzoate + NADH + H+
show the reaction diagram
-
-
-
?
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
methyl 4-formylbenzoate + NAD+ + H2O
4-(methoxycarbonyl)benzoate + NADH + H+
show the reaction diagram
n-butanal + NAD+ + H2O
butanoate + NADH + H+
show the reaction diagram
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
n-octanal + NAD+ + H2O
n-octanoate + NADH + H+
show the reaction diagram
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
show the reaction diagram
octanaldehyde + NAD+ + H2O
octanoate + NADH
show the reaction diagram
-
-
-
?
p-nitrobenzaldehyde + NAD+ + H2O
p-nitrobenzoate + NADH
show the reaction diagram
pentanal + NAD(P)+ + H2O
pentanoate + NAD(P)H + H+
show the reaction diagram
pentanaldehyde + NAD+ + H2O
pentanoate + NADH
show the reaction diagram
-
-
-
?
propanal + NAD(P)+ + H2O
propanoate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
propanaldehyde + NAD+ + H2O
propanoate + NADH
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH
show the reaction diagram
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + H+
show the reaction diagram
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 + 2 H+
show the reaction diagram
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
succinate semialdehyde + NADP+ + H2O
succinate + NADPH
show the reaction diagram
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
trans-2-hexenal + NAD+ + H2O
trans-2-hexenoate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
?
4-hydroxy-trans-2-nonenal + NAD+ + H2O
4-hydroxy-trans-2-nonenoate + NADH + H+
show the reaction diagram
succinate semialdehyde + NAD+ + H2O
succinate + NADH
show the reaction diagram
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
deamino-NAD+
-
reduced at nearly the same rate as NAD+
additional information
-
no activity with NADP+
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
5 mM, 84% activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutaric semialdehyde
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-Methoxybenzaldehyde
4-tolualdehyde
5,5'-dithiobis(2-nitrobenzoic acid)
acetaldehyde
acrolein
-
irreversible, noncompetitive, IC50: 0.015 mM
arsenite
benzaldehyde
-
-
Chloral hydrate
-
-
Disulfiram
Dithionitrobenzoate
-
-
glyoxylate
-
1 mM, 33% inhibition
iodoacetamide
-
-
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+
substrate inhibition
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
succinate semialdehyde
Valeraldehyde
-
-
additional information
-
no inhibition by 0.1 mM trans-2-hexenal and 0.1 mM crotonaldehyde
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
dithiothreitol
glutathione
-
activates
L-Cys
-
activates
sodium lauryl sulfate
-
low concentrations activate to a small extent
additional information
-
gene yneI is responsible for NAD+/NADP+-SSADH activity. The gene is induced by succinate semialdehyde
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
2,5-dioxopentanoate
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 - 0.1418
3-carboxybenzaldehyde
0.0502 - 0.287
3-Nitrobenzaldehyde
0.0121 - 0.1668
4-carboxybenzaldehyde
0.0503
4-hydroxy-trans-2-nonenal
-
recombinant enzyme
0.156 - 0.1612
4-Nitrobenzaldehyde
0.875 - 4.82
acetaldehyde
0.011 - 0.0159
alpha-Ketoglutaric semialdehyde
0.019 - 0.241
benzaldehyde
0.105
Butanal
-
-
0.0163
Glutaraldehyde
1 mM EDTA, 1 mM 2-mercaptoethanol, 66.7 mM potassium phosphate pH 7.2, 1.5 mM NAD+. 25C
0.0034
Glutaric semialdehyde
-
-
0.218
methyl 3-formylbenzoate
in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22C
0.061 - 0.323
n-Butanal
0.0253 - 0.107
n-Hexanal
0.0514 - 0.137
n-octanal
0.0287 - 0.096
n-Pentanal
0.0025 - 125
NAD+
0.552 - 4.4
NADP+
0.033
p-nitrobenzaldehyde
-
-
0.025 - 0.0827
pentanal
1.212 - 1.622
propanal
0.58 - 0.85
propionaldehyde
0.0007 - 6.3
succinate semialdehyde
0.0589
trans-2-hexenal
-
recombinant enzyme
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.1
2,5-dioxopentanoate
Sulfolobus solfataricus
Q97XS9
pH 6.5, 70C, cofactor NAD+
12.3 - 51.2
alpha-Ketoglutaric semialdehyde
69
NAD+
Sulfolobus solfataricus
Q97XS9
pH 6.5, 70C
22.6 - 31.7
succinate semialdehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.4
2,5-dioxopentanoate
Sulfolobus solfataricus
Q97XS9
pH 6.5, 70C, cofactor NAD+
3305
7.6
NAD+
Sulfolobus solfataricus
Q97XS9
pH 6.5, 70C
7
842
succinate semialdehyde
Sulfolobus solfataricus
Q97XS9
pH 6.5, 70C, cofactor NAD+
528
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 0.128
NADH
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
4-hydroxy-trans-2-nonenal
Rattus norvegicus
-
IC50: 0.11 mM
0.1 - 2
4-Methoxybenzaldehyde
1
4-tolualdehyde
Mus musculus
Q8BWF0
-
0.015
acrolein
Rattus norvegicus
-
irreversible, noncompetitive, IC50: 0.015 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.25
-
pH 8.3, 35C
5.3
-
-
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
at pH 8.5 MalE-DmSSADH is 10fold more active than at pH 6.0
7 - 10
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
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
optimal expression of pMalc2x-DmSSADH in Escherichia coli TB1
35 - 45
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.66
-
computer prediction
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mRNA expression
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
YneI protein
52100
-
deduced protein without the mitochondria import sequence
52230
-
calculated from sequence, SDS-PAGE
120000
-
gel filtration
130000
-
gel filtration
140000
-
gel filtration
145000
150000
-
gel filtration
157000
gel filtration
160000
-
non-denaturing PAGE, gel filtration
164000
-
gel filtration
191000
-
-
200000
-
gel filtration
220000
gel-filtration
225000
-
gel filtration
232000 - 245000
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
homotrimer
3 * 50000, SDS-PAGE; 3 * 51500, calculated from sequence
tetramer
trimer
-
3 * 54500, SDS-PAGE
additional information
-
4-aminobutyrate aminotransferase and succinate semialdehyde dehydrogenase form a stable enzymatic complex under in vivo conditions
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
18C, 1 h, about 20% loss of activity
288164
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
6 - 9
-
18C, 1 h, stable
288164
7 - 9
-
4C, 18 h, stable
288151
8
-
rapid decrease in stability above
707580
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
-
pH 8.9, 10 min, stable
18
-
14 h, 93% residual activity
37
-
14 h, 92% residual activity
50
-
pH 7.4, 8 min, complete inactivation. Mercaptoethanol stabilizes for 20 min or longer
60
-
stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
denaturation by sodium lauryl sulfate
-
freezing in absence of glycerol results in inactivation
-
NAD+ and mercaptoethanol effectively protect from auto-oxidation. NAD+ does not prevent auto-oxidation in presence of urea
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 14 h, 95% residual activity
-
-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
-
-20C, in presence of 10% v/v glycerol, stable for several months
-
0-2C, 24 h, 50% loss of activity
-
0C, 100 mM sodium phosphate, pH 8.5, 1mM DTT, 43% glycerol, 3 years
18C, 14 h, 93% residual activity
-
5C, unstable unless 30% glycerol is added
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes
-
by Ni2+-NTA agarose chromatography
His-tagged YneI dehydrogenase purified from cell extracts with HiTrap affinity columns
-
Ni-affinity chromatography
Ni2+-NTA agarose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 cells
expressed in Escherichia coli Rosetta 2 (DE3) cells
-
expression in Escherichia coli
expression in Escherichia coli as His-tag fusion protein
expression of mutant enzymes is expressed after transfection of HEK293 cells
-
into vectors pQE30 and into pMalc2x. Expression in Escherichia coli strains M15 and TB1
overexpressed as His-tagged YneI
-
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
transfection of HEK 293 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by growth of cells on gamma-aminobutanoate
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induction by growth on glutamate
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C196A
loss in specific activity of 55%
C196S
loss in specific activity of 74%
C243S
loss in specific activity of 70%
C311A
decreased SSADH activity to undetectable levels
C311S
decreased SSADH activity to undetectable levels
C502S
loss in specific activity of 93%
E277D
leads to a product with similar specific activity
E277K
charge inversion, which results in recombinant protein totally devoid of detectable SSADH activity
E277Q
concomitant loss of the negative charge, which results in recombinant protein totally devoid of detectable SSADH activity
C340A
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inactive mutant that cannot form a disulfide bond even under strong reducing conditions
C342A
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catalytically functional mutant that cannot form a disulfide bond even under strong reducing conditions
G46R
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the mutant shows 87% activity compared to the wild type enzyme
T233M
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the mutant shows 4% activity compared to the wild type enzyme
R166A
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the mutant enzyme shows no activity towards acetaldehyde and decreased activity and higher KM for succinate semiacetaldehyde
R166E
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the mutant enzyme shows almost no activity towards acetaldehyde and decreased activity and higher KM for succinate semiacetaldehyde
R166H
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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
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information
Show AA Sequence (428 entries)
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