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Information on EC 1.2.1.16 - succinate-semialdehyde dehydrogenase [NAD(P)+]
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1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)+]Specify your search results
Word Map
- 1.2.1.16
-
gamma-aminobutyric
- seizure
-
neurotransmitter
- transaminase
-
4-hydroxybutyric
-
gamma-hydroxybutyric
- aciduria
- aldh5a1
-
shunt
- epilepsy
-
subdural
- hematoma
-
gabaergic
- hypotonia
- gaba-transaminase
- 4-aminobutyrate
-
neurometabolic
-
ssadhd
-
tonic-clonic
- vigabatrin
-
globus
-
gabab
-
2.6.1.19
-
pallidi
-
evacuation
The enzyme appears in viruses and cellular organisms
Synonyms
succinic semialdehyde dehydrogenase, ssdh, succinate semialdehyde dehydrogenase, succinate-semialdehyde dehydrogenase, spssadh, gabd1, st0064, bsssadh, succinate-semialdehyde dehydrogenase [nad(p)+], nad(p)+-dependent benzaldehyde dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BsSSADH
GabD dehydrogenase
GabD1
gapN-2
NAD(P)+-dependent succinate semialdehyde dehydrogenase
NAD(P)+-dependent succinic semialdehyde dehydrogenase
NAD+/NADP+-dependent benzaldehyde dehydrogenase
SSADH
SSADH-II
SSO1842
ST0064
succinate semialdehyde dehydrogenase
succinic semialdehyde dehydrogenase
YneI
NAD(P)+-dependent succinate semialdehyde dehydrogenase
-
NAD(P)+-dependent succinate semialdehyde dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + 2 H+
-
-
-
-
succinate semialdehyde + NAD(P)+ + H2O = succinate + NAD(P)H + 2 H+
mechanism is sequential, consistent with rapid-equilibrium ordered bi-bi system and a steady-state ordered bi-bi system
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
succinate-semialdehyde:NAD(P)+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-88-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
low dehydrogenase activity
-
?
3-chlorobenzaldehyde + NAD+ + H2O
3-chlorobenzoate + NADH + 2 H+
-
-
-
?
3-hydroxy-benzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + H+
-
good substrate
-
?
3-hydroxybenzaldehyde + NAD+ + H2O
3-hydroxybenzoate + NADH + 2 H+
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
-
-
?
4-chloro-benzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + H+
-
good substrate
-
?
4-chlorobenzaldehyde + NAD+ + H2O
4-chlorobenzoate + NADH + 2 H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
-
mandelate pathway
-
ir
beta-hydroxysuccinic semialdehyde + NADP+ + H2O
beta-hydroxysuccinate + NADPH + H+
-
-
-
?
cyclohexanal + NAD+ + H2O
cyclohexanecarboxylic acid + NADH + H+
-
good substrate
-
?
decanal + NADP+ + H2O
decanoate + NADPH + H+
low dehydrogenase activity
-
?
malonic semialdehyde + NADP+ + H2O
malonate + NADPH + H+
-
hydrolyzed at 8.7% the rate of succinate semialdehyde
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
-
-
?
succinic semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
weaker reaction compared to NAD+
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
weaker reaction compared to NAD+
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
ir
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
at 9% of the rate with NAD+
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
pathway for utilization of 4-aminobutyric acid as nitrogen source for Saccharomyces cerevisiae
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
additional information
?
-
-
only the aldehyde forms and not the gem-diol forms of the specific substrate succinic semialdehyde , of selected aldehyde substrates, and of the inhibitor 3-tolualdehyde bind to the enzyme. Residue cysteine311 is crucial for their discrimination
-
?
additional information
?
-
-
almost no activity with DL-glyceraldehyde, DL-glyceraldehyde 3-phosphate, and glycoaldehyde
-
?
additional information
?
-
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates
-
?
additional information
?
-
-
no activity with 2-chlorobenzaldehyde, 3-chlorobenzaldehyde, and acetaldehyde
-
?
additional information
?
-
-
no activity is observed with 2-chlorobenzaldehyde
-
?
additional information
?
-
-
the 3- and 4-chloro substituents as well as the 3-hydroxy substituent are all electron withdrawing. All these compounds show a reduction in reaction velocity from that of the unsubstituted benzaldehyde
-
?
additional information
?
-
-
almost no activity with D,L-glyceraldehyde, D,L-glyceraldehyde-3-phosphate, and D,L-glycolaldehyde
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
?
additional information
?
-
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
?
additional information
?
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
?
additional information
?
-
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
?
additional information
?
-
neither propionaldehyde nor phthalaldehyde seves as substrate
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-naphthaldehyde + NADP+ + H2O
2-naphthoate + NADPH + H+
low dehydrogenase activity
-
-
?
2-oxoglutarate semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
-
?
2-oxoglutarate semialdehyde + NADP+ + H2O
2-oxoglutarate + NADPH + H+
-
-
-
-
?
3-sulfopropanal + NAD(P)+ + H2O
3-sulfopropanoate + NAD(P)H + 2 H+
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
-
mandelate pathway
-
-
ir
decanal + NADP+ + H2O
decanoate + NADPH + H+
low dehydrogenase activity
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
succinate + NAD(P)H + 2 H+
-
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
-
?
2-naphthaldehyde + NAD+ + H2O
2-naphthoate + NADH + H+
low dehydrogenase activity
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
low dehydrogenase activity
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
degradation of 3,4-dihydroxyphenylacetate in Arthrobacter sp.
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
implicated in 4-hydroxyphenylacetic acid and gamma-aminobutyric acid catabolism
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
involved in the degradation of gamma-aminobutyrate
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
pathway for utilization of 4-aminobutyric acid as nitrogen source for Saccharomyces cerevisiae
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
-
-
-
?
additional information
?
-
-
almost no activity with DL-glyceraldehyde, DL-glyceraldehyde 3-phosphate, and glycoaldehyde
-
-
?
additional information
?
-
-
other aldehydes, such as formaldehyde, acetaldehyde and glutaraldehyde, are very poor substrates
-
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
additional information
?
-
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
additional information
?
-
the enzyme shows no detectable activity with hexanal or benzaldehyde
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
NAD(P)+-dependent succinic semialdehyde dehydrogenase, BsSSADH shows similar values of the catalytic efficiency (kcat/Km) in both NAD+ and NADP+ as cofactors. The affinity of enzyme BsSSADH to NAD+ is approximately 2fold higher than that to NADP+, but the values of kcat are almost 2fold higher in the presence of NADP+ than NAD+
-
NAD+
-
enzyme is active both with NADP+ and NAD+, Vmax with NAD+ is considerably larger than that obtained with NADP+
NAD+
-
2.5fold better activity than with NADP+ at 0.2 mM concentration
NAD+
-
higher activity in the presence of NAD+ than in the presence of NADP+
NAD+
kcat/Km-value is comparable for succinate semialdehyde with NADP+ and for succinate semialdehyde with NAD+
NAD+
-
long incubations lead to a modest utilization of NAD+ as substrate
NAD+
the enzyme can use both NAD+ and NADP+ although affinity to NAD+ is 10times higher
NAD+
affinity to NAD+ is 10 times higher than to NADP+
NAD+
similar values of the catalytic efficiency (kcat/Km) with both NAD+ and NADP+ as cofactors
NADP+
-
enzyme is active both with NADP+ and NAD+, Vmax with NAD+ is considerably larger than that obtained with NADP+
NADP+
-
higher activity in the presence of NAD+ than in the presence of NADP+
NADP+
-
although long incubations lead to a modest utilization of NAD+ as substrate, NADP+ is the preferred substrate
NADP+
kcat/Km-value is comparable for succinate semialdehyde with NADP+ and for succinate semialdehyde with NAD+
NADP+
the enzyme can use both NAD+ and NADP+ although affinity to NAD+ is 10times higher
NADP+
affinity to NAD+ is 10 times higher than to NADP+
NADP+
similar values of the catalytic efficiency (kcat/Km) with both NAD+ and NADP+ as cofactors
NADP+
SpSSADH prefers NADP+ over NAD+ as a hydride acceptor, structural basis of the cofactor preference of SpSSADH, overview. Residues Ser158 and Tyr188 in SpSSADH participate in the stabilization of the 2'-phosphate group of adenine-side ribose in NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
100% activity at 10 mM Mg2+. With Mg2+ there is a 4fold decrease in the Km value for succinate semialdehyde and a 6fold decrease in the Km value for NADP+
additional information
additional information
-
bivalent kations such as Mg2+, Mn2+, Ca2+ or Fe2+ are not required
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-tolualdehyde
-
only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme
succinate semialdehyde
-
enzyme BsSSADH shows the substrate inhibition phenomenon in the presence of both NAD+ and NADP+ as cofactors at the concentration of succinate semialdehyde higher than 0.05 and 0.02 mM, respectively
succinate semialdehyde
substrate inhibition at concentrations higher than 0.1 mM
Succinic semialdehyde
substrate inhibition above 0.1 mM
additional information
-
the enzyme is not influenced by 5 mM EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-aminobutyrate
induction during growth with 4-aminobutyrate (GABA)
dithiothreitol
-
activation and stabilization, maximum activity at 25 mM
dithiothreitol
-
necessary both to maintain the activity of BADH and to prevent oligimerization of the enzyme
dithiothreitol
the enzyme is stimulated (up to 40%) by the addition of dithiothreitol (0.1-0.2 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
0.2
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
0.011
benzaldehyde
-
recombinant wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C
0.013
benzaldehyde
-
native wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C
0.033
benzaldehyde
-
native wild type enzyme, in the presence of NAD+, TAPS buffer, at pH 8.5, at 30°C
0.035
benzaldehyde
-
recombinant wild type enzyme, in the presence of NAD+, TAPS buffer, at pH 8.5, at 30°C
0.043
NAD+
wild-type, pH 8.0, 37°C
0.043
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.111
NAD+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.15
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
0.15
NAD+
mutant N193A, pH 8.0, 37°C
0.48
NAD+
wild-type, pH 8.0, 37°C
10
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
10
NAD+
mutant K160A , pH 8.0, 37°C
11
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
11
NAD+
mutant K160E , pH 8.0, 37°C
0.287
NADP+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
0.482
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
2.4
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
2.4
NADP+
mutant N193A, pH 8.0, 37°C
26
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
26
NADP+
mutant K160A , pH 8.0, 37°C
27
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
27
NADP+
mutant K160E , pH 8.0, 37°C
0.0029
succinate semialdehyde
pH 8.0, 60°C, cosubstrate: NADP+
0.003
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
0.0133
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
0.022
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.022
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
0.027
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.027
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
0.047
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.047
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
0.12
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.12
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
0.14
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.14
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
0.22
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.22
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
0.23
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.23
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
0.77
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.77
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
2.49
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2.49
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
2.6
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2.6
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
10.36
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
10.36
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
20.5
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
20.5
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
0.0011
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
0.004
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.2
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
27.3
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
14
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
14
NAD+
mutant N193A, pH 8.0, 37°C
38
NAD+
wild-type, pH 8.0, 37°C
38
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
39
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
39
NAD+
mutant K160A , pH 8.0, 37°C
46
NAD+
wild-type, pH 8.0, 37°C
66
NAD+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
80
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
80
NAD+
mutant K160E , pH 8.0, 37°C
2.1
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
2.1
NADP+
mutant K160E , pH 8.0, 37°C
2.6
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
2.6
NADP+
mutant K160A , pH 8.0, 37°C
21
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
21
NADP+
mutant N193A, pH 8.0, 37°C
21.1
NADP+
-
recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C
46
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.3
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
0.3
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
1.9
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
2 - 8
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
2 - 8
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
4.7
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
5.61
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
5.61
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
7.24
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
7.24
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
26
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
26
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
45
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
45
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
55
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
55
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
66
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
66
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
68
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
68
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
73
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
73
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
83
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
83
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
164
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
164
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
16.8
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
18.4
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
134.1
2-oxoglutarate semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
215.3
2-oxoglutarate semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
3.8
NAD+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
3.8
NAD+
mutant K160A , pH 8.0, 37°C
7.3
NAD+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
7.3
NAD+
mutant K160E , pH 8.0, 37°C
95
NAD+
wild-type, pH 8.0, 37°C
97
NAD+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
97
NAD+
mutant N193A, pH 8.0, 37°C
880
NAD+
wild-type, pH 8.0, 37°C
880
NAD+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.077
NADP+
mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C
0.1
NADP+
mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C
0.1
NADP+
mutant K160A , pH 8.0, 37°C
0.77
NADP+
mutant K160E , pH 8.0, 37°C
8.6
NADP+
mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C
8.6
NADP+
mutant N193A, pH 8.0, 37°C
95
NADP+
wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C
0.36
succinate semialdehyde
cofactor NADP+, pH not specified in the publication, 30°C
0.362
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
0.598
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
0.6
succinate semialdehyde
cofactor NAD+, pH not specified in the publication, 30°C
1.3
succinate semialdehyde
mutant D426A , cofactor NAD+, pH 8.0, 37°C
18
succinate semialdehyde
mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
18
succinate semialdehyde
mutant R145A , cofactor NAD+, pH 8.0, 37°C
28
succinate semialdehyde
mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
28
succinate semialdehyde
mutant K92A, cofactor NAD+, pH 8.0, 37°C
86
succinate semialdehyde
mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
86
succinate semialdehyde
mutant W141A , cofactor NAD+, pH 8.0, 37°C
110
succinate semialdehyde
mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
130
succinate semialdehyde
mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
130
succinate semialdehyde
mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
140
succinate semialdehyde
-
with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C
180
succinate semialdehyde
wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
200
succinate semialdehyde
wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
210
succinate semialdehyde
mutant enzyme F138A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
210
succinate semialdehyde
mutant F138A , cofactor NAD+, pH 8.0, 37°C
310
succinate semialdehyde
mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C
310
succinate semialdehyde
mutant S425A , cofactor NAD+, pH 8.0, 37°C
1100
succinate semialdehyde
mutant E442A, cofactor NAD+, pH 8.0, 37°C
1300
succinate semialdehyde
mutant R428A , cofactor NAD+, pH 8.0, 37°C
1600
succinate semialdehyde
-
with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C
1800
succinate semialdehyde
wild-type, cofactor NADP+, pH 8.0, 37°C
2000
succinate semialdehyde
wild-type, cofactor NAD+, pH 8.0, 37°C
1789
Succinic semialdehyde
-
with NAD+ as cosubstrate, at pH 6.5 and 70°C
3454
Succinic semialdehyde
-
with NADP+ as cosubstrate, at pH 6.5 and 70°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0628
succinate semialdehyde
-
in the absence of Mg2+, at pH 7.5 and 37°C
28.3
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NADP+
470.6
succinate semialdehyde
-
pH and temperature not specified in the publication, in presence of NAD+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0017
-
wild type, value below, NH4+ used as N-source or uga2 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.0033
-
uga3 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.021
-
wild type, succinate used as C-source, gamma-aminobutyrate and NH3 used as N-source
0.023
0.026
0.03
-
bis(3-aminopropyl)-amine and glucose, glucose and NH3 or ribose and NH3 used as C-source and N-source
0.034
-
wild type, 4-hydroxyphenylacetate used as C-source and NH3 used as N-source
0.06
-
4-hydroxyphenylacetic acid and glucose used as carbon source, NH3 used as N-source
0.075
0.078
-
glycerol used as carbon source, 4-aminobutyric acid used as N-source
0.08
-
4-hydroxyphenylacetic acid used as carbon source, NH3 used as N-source
0.085
-
4-aminobutyric acid used as carbon source, NH3 used as N-source
0.091
-
4-hydroxyphenylacetic acid, glucose and cAMP used as carbon source, NH3 used as N-source
0.105
-
wild type, succinate used as C-source and gamma-aminobutyrate used as N-source
0.125
-
uga1 mutant unable to grow on 4-aminobutyric acid, glutamate and 4-aminobutyric acid used as N-source
0.13
-
4-hydroxyphenylacetic acid and cAMP used as carbon source, NH3 used as N-source
0.319
-
mutant, gamma-aminobutyrate used as C-source and NH3 used as N-source
0.351
-
mutant, succinate used as C-source and gamma-aminobutyrate used as N-source
0.38
-
wild type, glutamate and 4-aminobutyric acid used as N-source
0.395
-
mutant, glucose used as C-source and gamma-aminobutyrate used as N-source
8.5
additional information
additional information
specific activity of 0.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 0.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 0.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 0.6 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 0.6 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 0.7 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 0.7 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 10 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 10 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 2.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
-
specific activity of 2.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NADP+
additional information
specific activity of 3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
-
specific activity of 5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is sulfopropanal and NAD+
additional information
specific activity of 5.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 5.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
specific activity of 7.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
-
specific activity of 7.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NADP+
additional information
specific activity of 7.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
specific activity of 7.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinale semialdehyde and NAD+
additional information
-
Good activity with several alternate substrates including the aromatic substrates, 4-chloro- and 3-hydroxy-benzaldehyde, as well as cyclohexanal. BADH is most active with medium chain aliphatic substrates such as pentanal and hexanal.The level of activity with aliphatic substrates drops off rapidly as the chain length decreased with very little activity (<0.1%) being observed with acetaldehyde.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
KM value for NAD+ increases from 0.3 to 1 mM as the pH changes from pH 5 to 10. The pH profile data are obtained at a NAD+ concentration of 5 mM, essentially saturating across the entire pH range. Similarly, data for the NADP+ pH profile are obtained at 10 mM NADP+
5.5 - 10
-
the enzyme cannot be assayed below pH 5.5, due to precipitation and loss of activity
8.7 - 10.6
-
with NAD+, at pH 8.7: 45% of activity maximum, at pH 10.6: about 50% of activity maximum
8.7 - 10.9
-
with NADP+, at pH 8.7: about 30% of activity maximum, at pH 10.9: about 65% of activity maximum
additional information
-
The pH profiles are bell-shaped indicating that two ionizable groups are involved in the catalytic mechanism.
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type strain B and mutant able to grow on gamma-aminobutyrate as sole C- and N-source
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation
metabolism
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde to succinic acid in the final step of GABA catabolism
metabolism
-
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation
Show AA Sequence and Transmembrane Helices (7923 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49000
51600
52000
90000
49000
2 * 49000 , predicted from amino acid sequence
90000
-
Dimer is determined by gel filtration whereas the molecular mass of the enzyme is calculated by comparison to the relative mobility of the standard proteins.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
additional information
homodimer
2 * 49000 , predicted from amino acid sequence
homodimer
-
2 * 49000 , predicted from amino acid sequence
homodimer
enzyme SpSSADH shows a dimeric conformation, containing a single cysteine residue in the catalytic loop of each subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-form and in complex with NAD+, hanging drop vapor diffusion method, using 2 M sodium formate and 0.1 M sodium acetate (pH 4.6), at 22°C
structures of apoenzyme and in complex with NAD+, to 1.85 and 1.9 A resolution. Two domain protein with the active site located in the interdomain interface. The NAD+ molecule is bound in the long channel with its nicotinamide ring positioned close to the side chain of the catalytic Cys268
apoenzyme and in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M MES monohydrate pH 5.8-6.1 and 18-23% (w/v) polyethylene glycol 4000
-
purified recombinant SpSSADH in apo-form and in a binary complex with NADP+, hanging drop vapor diffusion method, for the apoform crystals: mixing 0.001 ml of protein solution with 0.001 ml of reservoir solution containing 0.1 M MES monohydrate, pH 5.8-6.1, and 18-23% w/v PEG 4000, and equilibration over 0.5 ml reservoir solution, for the binary complex crystals: mixing of protein solution with NADP+ in a 1:10 molar ratio with reservoir solution containing 0.1 M sodium acetate trihydrate, pH 4.6, and 2 M ammonium sulfate, 22°C, X-ray diffraction structure determination and analysis at 1.6 A and 2.1 A resolutions, respectively, molecular replacement method using the structure of Escherichia coli SSADH, PDB ID 3JZ4, as search model
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C311A
-
mutant is still soluble but unable to catalyze succinate semialdehyde oxidation. Mutation leads to an inactive product binding both succinate semialdehyde aldehyde and gem-diol
C102A
-
mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
C140A
C220A
C249A
D426A
E442A
F138A
K160A
K160E
K92A
N193A
R145A
R428A
S425A
W141A
D426A
-
strong decrease in activity
K160A
-
Lys160 contributes to the enzyme preference to NAD+, strong decrease in activity
N193A
-
strong decrease in activity
D426A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F138A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N193A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S425A
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S434A
kinetic data show no significant difference from wild-type enzyme
S434D
kinetic data show no significant difference from wild-type enzyme
S434E
kinetic data show no significant difference from wild-type enzyme
S434A
-
kinetic data show no significant difference from wild-type enzyme
S434D
-
kinetic data show no significant difference from wild-type enzyme
S434E
-
kinetic data show no significant difference from wild-type enzyme
additional information
C140A
-
mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
C220A
-
mutant exhibits BADH activity between 50 and 75% that of the wild type enzyme
D426A
strong decrease in activity
D426A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
E442A
strong decrease in activity
E442A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
F138A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160A
Lys160 contributes to the enzyme preference to NAD+, strong decrease in activity
K160E
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K160E
Lys160 contributes to the enzyme preference to NAD+, strong decrease in activity
K92A
strong decrease in activity
K92A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N193A
strong decrease in activity
N193A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R145A
strong decrease in activity
R145A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R428A
activity similar to wild-type
R428A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S425A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
W141A
strong decrease in activity
W141A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information
-
gabD knockout mutant has a limited capacity to metabolize gamma-aminobutyrate
additional information
-
gabD knockout mutant has a limited capacity to metabolize gamma-aminobutyrate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
the Km value for NAD+ increases from 0.3 to 1 mM as the pH changes from pH 5 to 10
685387
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol is necessary both to maintain the activity of BADH and to prevent oligimerization of the enzyme
-
enzyme is labile (50% loss of activity overnight) but can be largely stabilized (in crude extract only) by the addition of 10 mM dithiothreitol 1.2.1.16
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
there is no significant loss of catalytic activity, after up to 40 min of incubation of isoform GabD1 with 1 mM H2O2 at pH 7.4
-
724115
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Addition of 2 mM DTT to both stacking and resolving gels results in a decrease in the protein laddering effect, and both BADH and BADH-His are present as near-homogeneous species.
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
-
by ammonium sulfate precipitation and anion exchange chromatography and gel filtration
column chromatography on DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex
-
His-tagged GabD dehydrogenase purified from cell extracts with HiTrap affinity columns
-
Ni-NTA resin column chromatography and Superdex 75 gel filtration
Purification of his-tagged proteins by using a standard Ni2+-agarose chromatography protocol.
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
expression in Escherichia coli
gene ssadh, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Protein expression in Escherichia coli strain JM109. Single colonies are picked and the DNA is isolated and screened for the desired mutation either by restriction analysis (C103A and C249A) or by sequencing (C140A and C220A). The overall fidelity of the PCR amplification and the presence of the desired mutations are confirmed by sequencing. The plasmids containing the mutated genes are then transformed into Escherichia coli strain BL21(DE3)pLysS for protein expression.
-
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcript is detected inducibly in both homotaurine and GABA-grown cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the NADP+-dependent succinate semialdehyde dehydrogenase activity encoded by gabD appears to be important for nitrogen metabolism under N limitation conditions
additional information
-
the NADP+-dependent succinate semialdehyde dehydrogenase activity encoded by gabD appears to be important for nitrogen metabolism under N limitation conditions
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Enzymatic utilization of gamma-hydroxybutyric acid
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Mutations affecting the enzymes involved in the utilization of 4-aminobutyric acid as nitrogen source by the yeast Saccharomyces cerevisiae
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1985
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Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniae
Biochim. Biophys. Acta
990
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1989
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Donelly, M.I.; Cooper, R.A.
Succinic semialdehyde dehydrogenases of Escherichia coli: their role in the degradation of p-hydroxyphenylacetate and gamma-aminobutyrate
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The catabolism of L-tyrosine by an Arthrobacter sp.
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Enzymes of gamma-aminobutyrate metabolism (bacterial)
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5
765-778
1962
Pseudomonas fluorescens
-
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Separation and properties of the NAD-linked and NADP-linked isozymes of succinic semialdehyde dehydrogenase in Euglena gracilis z
Biochim. Biophys. Acta
429
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1976
Euglena gracilis
brenda
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Novel type of catabolite repression in the pathway of gamma-aminobutyrate breakdown in Escherichia coli K-12
FEBS Lett.
37
207-211
1973
Escherichia coli
brenda
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Succinate semialdehyde dehydrogenase of Rhodopseudomonas spheroides which is active with both NADP+ and NAD+
J. Biochem.
70
243-247
1971
Rhodobacter sphaeroides
brenda
Padmanabhan, R.; Tchen, T.T.
Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate-linked succinic semialdehyde dehydrogenases in a Pseudonomas species
J. Bacteriol.
100
398-402
1969
Pseudomonas sp.
brenda
Jakoby, W.B.; Scott, E.M.
Aldehyde oxidation III. Succinic semialdehyde dehydrogenase
J. Biol. Chem.
234
937-940
1959
Pseudomonas fluorescens
brenda
Sims, K.L.; Davis, G.A.
Subcellular distribution of succinate-semialdehyde dehydrogenase in rat brain
Eur. J. Biochem.
35
450-453
1973
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Maitre, M.; Ossola, L.; Mandel, P.
In vitro studies into the effect of inhibition of rat brain succinic semialdehyde dehydrogenase on GABA synthesis and degradation
FEBS Lett.
72(1)
53-57
1976
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Walsh, J.M.; Clark, J.B.
Studies on the control of 4-aminobutyrate metabolism in synaptosomal and free rat brain mitochondria
Biochem. J.
160
147-157
1976
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Metzer, E.; Levitz, R.; Halpern, Y.S.
Isolation and properties of Escherichia coli K-12 mutants impaired in the utilization of gamma-aminobutyrate
J. Bacteriol.
137
111-1118
1979
Escherichia coli
-
brenda
Vissers, S.; Andre, B.; Muyldermans, F.; Grenson, M.
Positive and negative regulatory elements control the expression of the UGA4 gene coding for the inducible 4-aminobutyric-acid-specific permease in Saccharomyces cerevisiae
Eur. J. Biochem.
181
357-361
1989
Saccharomyces cerevisiae
brenda
Vissers, S.; Andre, B.; Muyldermans, F.; Grenson, M.
Induction of the 4-aminobutyrate and urea-catabolic pathways in Saccharomyces cerevisiae
Eur. J. Biochem.
187
611-616
1990
Saccharomyces cerevisiae
brenda
Lutke-Eversloh, T.; Steinbuchel, A.
Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha
FEMS Microbiol. Lett.
181
63-71
1999
Cupriavidus necator (Q9RBF6), Cupriavidus necator
brenda
Saehuan, C.; Rojanarata, T.; Wiyakrutta, S.; McLeish, M.J.; Meevootisom, V.
Isolation and characterization of a benzoylformate decarboxylase and a NAD+/NADP+-dependent benzaldehyde dehydrogenase involved in D-phenylglycine metabolism in Pseudomonas stutzeri ST-201
Biochim. Biophys. Acta
1770
1585-1592
2007
Pseudomonas stutzeri, Pseudomonas stutzeri ST-201
brenda
Yeung, C.K.; Yep, A.; Kenyon, G.L.; McLeish, M.J.
Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633
Biochim. Biophys. Acta
1784
1248-1255
2008
Pseudomonas putida
brenda
Jaeger, M.; Rothacker, B.; Ilg, T.
Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases
Biochem. Biophys. Res. Commun.
372
400-406
2008
Drosophila melanogaster
brenda
Fuhrer, T.; Chen, L.; Sauer, U.; Vitkup, D.
Computational prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in Escherichia coli
J. Bacteriol.
189
8073-8078
2007
Escherichia coli, Escherichia coli BW25113
brenda
Mayer, J.; Cook, A.M.
Homotaurine metabolized to 3-sulfopropanoate in Cupriavidus necator H16: enzymes and genes in a patchwork pathway
J. Bacteriol.
191
6052-6058
2009
Cupriavidus necator (Q0K2K1), Cupriavidus necator
brenda
Sanchez, M.; Alvarez, M.A.; Balana, R.; Garrido-Pertierra, A.
Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putida
Biochim. Biophys. Acta
953
249-257
1988
Pseudomonas putida
brenda
Esser, D.; Kouril, T.; Talfournier, F.; Polkowska, J.; Schrader, T.; Bräsen, C.; Siebers, B.
Unraveling the function of paralogs of the aldehyde dehydrogenase super family from Sulfolobus solfataricus
Extremophiles
17
205-216
2013
Escherichia coli, Saccharolobus solfataricus
brenda
Jang, E.H.; Lim, J.E.; Chi, Y.M.; Lee, K.S.
Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes
Acta Crystallogr. Sect. F
68
288-291
2012
Streptococcus pyogenes
brenda
de Carvalho, L.P.; Ling, Y.; Shen, C.; Warren, J.D.; Rhee, K.Y.
On the chemical mechanism of succinic semialdehyde dehydrogenase (GabD1) from Mycobacterium tuberculosis
Arch. Biochem. Biophys.
509
90-99
2011
Mycobacterium tuberculosis
brenda
Ito, F.; Chishiki, H.; Fushinobu, S.; Wakagi, T.
Archaeal aldehyde dehydrogenase ST0064 from Sulfolobus tokodaii, a paralog of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, is a succinate semialdehyde dehydrogenase
Biosci. Biotechnol. Biochem.
77
1344-1348
2013
Sulfurisphaera tokodaii (Q976X5), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q976X5)
brenda
Zheng, H.; Beliavsky, A.; Tchigvintsev, A.; Brunzelle, J.S.; Brown, G.; Flick, R.; Evdokimova, E.; Wawrzak, Z.; Mahadevan, R.; Anderson, W.F.; Savchenko, A.; Yakunin, A.F.
Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium
Proteins
81
1031-1041
2013
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZPI3), Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2 (Q8ZPI3)
brenda
Park, S.A.; Park, Y.S.; Lee, K.S.
Kinetic characterization and molecular modeling of NAD(P)(+)-dependent succinic semialdehyde dehydrogenase from Bacillus subtilis as an ortholog YneI
J. Microbiol. Biotechnol.
24
954-958
2014
Bacillus subtilis (P94428), Bacillus subtilis, Bacillus subtilis 168 (P94428)
brenda
Zheng, H.; Beliavsky, A.; Tchigvintsev, A.; Brunzelle, J.; Brown, G.; Flick, R.; Evdokimova, E.; Wawrzak, Z.; Mahadevan, R.; Anderson, W.; Savchenko, A.; Yakunin, A.
Structure and activity of the NAD(P)+-dependent succinate semialdehyde dehydrogenase YneI from Salmonella typhimurium
Proteins Struct. Funct. Bioinform.
81
1031-1041
2013
Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZPI3), Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (Q8ZPI3)
brenda
Park, S.A.; Park, Y.S.; Lee, K.S.
Kinetic characterization and molecular modeling of NAD(P)+-dependent succinic semialdehyde dehydrogenase from Bacillus subtilis as an ortholog YneI
J. Microbiol. Biotechnol.
24
954-958
2014
Bacillus subtilis, Bacillus subtilis 168
brenda
Jang, E.H.; Park, S.A.; Chi, Y.M.; Lee, K.S.
Kinetic and structural characterization for cofactor preference of succinic semialdehyde dehydrogenase from Streptococcus pyogenes
Mol. Cells
37
719-726
2014
Streptococcus pyogenes (A0A0J9X1M8), Streptococcus pyogenes
brenda
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