Information on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+):
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EC NUMBERCOMMENTARY
1.2.1.79-

RECOMMENDED NAMEGeneOntology No.
succinate-semialdehyde dehydrogenase (NADP+)GO:0036243

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
succinate semialdehyde + NADP+ + H2O = succinate + NADPH + 2 H+
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
4-aminobutyrate degradation II-PWY-6537
4-hydroxyphenylacetate degradation-3-HYDROXYPHENYLACETATE-DEGRADATION-PWY
nicotine degradation I-P181-PWY
nicotine degradation II-PWY-6993
TCA cycle IV (2-oxoglutarate decarboxylase)-P105-PWY

SYSTEMATIC NAMEIUBMB Comments
succinate-semialdehyde:NADP+ oxidoreductaseThis enzyme participates in the degradation of glutamate and 4-aminobutyrate. It is similar to EC 1.2.1.24 [succinate-semialdehyde dehydrogenase (NAD+)], and EC 1.2.1.16 [succinate-semialdehyde dehydrogenase (NAD(P)+)], but is specific for NADP+. The enzyme from Escherichia coli is 20-fold more active with NADP+ than NAD+ [2].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
gabDEscherichia coli K-12P25526gene name710394
SSADHEscherichia coli--710394
SSADHEscherichia coli K-12P25526-710394
succinic semialdehyde dehydrogenaseEscherichia coli--710394
succinic semialdehyde dehydrogenaseEscherichia coli K-12P25526-710394

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Cupriavidus necator-288054Q9RBF6UniProtManually annotated by BRENDA team
Escherichia coli-690736, 710394P25526UniProtManually annotated by BRENDA team
Escherichia coli-707392, 708907--Manually annotated by BRENDA team
Escherichia coli K-12-707580--Manually annotated by BRENDA team
Escherichia coli K-12-710394P25526UniProtManually annotated by BRENDA team
Escherichia coli MC1061-710394P25526UniProtManually annotated by BRENDA team
Euglena gracilis-288042--Manually annotated by BRENDA team
Klebsiella pneumoniae-288038--Manually annotated by BRENDA team
Pseudomonas putida-707583--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismEscherichia coli-SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid710394
physiological functionCupriavidus necatorQ9RBF6gene is disrupted in a transposon-induced mutant of Ralstonia eutropha exhibiting the phenotype 4-hydroxybutyric acid-leaky288054

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
3-carboxybenzaldehyde + NADP+ + H2O3-carboxybenzoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
3-nitrobenzaldehyde + NADP+ + H2O3-nitrobenzoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
4-carboxybenzaldehyde + NADP+ + H2O4-carboxybenzoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
benzaldehyde + NADP+ + H2Obenzoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
n-butanal + NADP+ + H2Obutanoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
n-hexanal + NADP+ + H2Ohexanoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
n-pentanal + NADP+ + H2Opentanoate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
succinate semialdehyde + NAD+ + H2Osuccinate + NADH + H+
show the reaction diagram		Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394--?
succinate semialdehyde + NAD+ + H2Osuccinate + NADH + 2 H+
show the reaction diagram		Cupriavidus necatorQ9RBF6about 11% of the activity with NADP+288054--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + H+
show the reaction diagram		Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Escherichia coli--708907--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Euglena gracilis--288042--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Pseudomonas putida--707583--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Klebsiella pneumoniae--288038--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Escherichia coli K-12--707580--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Escherichia coliP25526-690736--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Escherichia coli K-12P25526-710394--?
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + 2 H+
show the reaction diagram		Cupriavidus necatorQ9RBF6-288054--?
malonate semialdehyde + NADP+ + H2Omalonate + NADPH + 2 H+
show the reaction diagram		Euglena gracilis-8.7% of the activity with succinate semialdehyde288042--?
additional information?-Euglena gracilis-no substrate: glyoxylic acid, formic acid, formaldehyde, acetaldehyde, glyoxal, furfural and acrolein288042---
additional information?-Escherichia coli K-12-no substrate: n-butanal, formaldehyde, acetaldehyde, glyoxal, glyoxalate, propanal, glutaraldehyde, benzaldehyde, and anisaldehyde707580---
additional information?-Escherichia coliP25526only 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 enzyme690736---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
succinate semialdehyde + NAD+ + H2Osuccinate + NADH + H+
show the reaction diagram		Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394--
succinate semialdehyde + NADP+ + H2Osuccinate + NADPH + H+
show the reaction diagram		Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
NAD+Cupriavidus necatorQ9RBF6about 11% of the activity with NADP+288054 2D-image
NAD+Escherichia coli-NAD+ acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+690736 2D-image
NAD+Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394 2D-image
NADP+Klebsiella pneumoniae-specific for NADP+288038 2D-image
NADP+Euglena gracilis--288042 2D-image
NADP+Cupriavidus necatorQ9RBF6-288054 2D-image
NADP+Escherichia coli-NAD+ also acts as cosubstrate, but the reaction rates are more than 20fold lower than those with NADP+690736 2D-image
NADP+Pseudomonas putida-specific for NADP+707583 2D-image
NADP+Escherichia coli-enzyme is specific for NADP+ as a cofactor708907 2D-image
NADP+Escherichia coli-the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394 2D-image
NADP+Escherichia coli K-12P25526electron density analysis of binding site. The enzyme activity measured in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+710394 2D-image
additional informationEscherichia coli K-12P25526no cofactor: NAD+710394-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
K+Euglena gracilis-5 mM, 10% activation288042

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3-tolualdehydeEscherichia coli-only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme690736 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Euglena gracilis-0.01 mM, 29% residual activity288042 2D-image
Ca2+Euglena gracilis--288042 2D-image
Mg2+Euglena gracilis--288042 2D-image
N-ethylmaleiimideEuglena gracilis-0.1 mM, complete loss of activity288042-
NADPHKlebsiella pneumoniae--288038 2D-image
NADPHPseudomonas putida--707583 2D-image
Ni2+Euglena gracilis--288042 2D-image
Succinate semialdehydeEuglena gracilis-substrate inhibition above 1 mM288042 2D-image
Zn2+Euglena gracilis-1 mM, complete inhibition288042 2D-image
Mn2+Euglena gracilis--288042 2D-image
additional informationKlebsiella pneumoniae-not inhibitory: succinate, pyruvate288038-
additional informationPseudomonas putida-not inhibitory: succinate, pyruvate707583-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-mercaptoethanolEscherichia coli K-12-loss of about 80% of original acitivity after exhaustive dialysis, renaturation in presence of 2-mercaptoethanol707580 2D-image
2-mercaptoethanolPseudomonas putida--707583 2D-image
dithiothreitolEuglena gracilis-1 mM, 78% activation288042 2D-image
dithiothreitolPseudomonas putida--707583 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.038-NADP+Euglena gracilis-pH 8.7, 35°C288042 2D-image
0.04-NADP+Escherichia coli K-12-pH 9.0, 37°C707580 2D-image
0.0446-NADP+Escherichia coli-pH 8.5, 22°C690736 2D-image
0.135-NADP+Pseudomonas putida-pH 8.0, 30°C707583 2D-image
0.25-NADP+Klebsiella pneumoniae-pH 7.8, 30°C288038 2D-image
0.0078-Succinate semialdehydeEscherichia coli-pH 8.5, 22°C690736 2D-image
0.01-Succinate semialdehydeEscherichia coli K-12-pH 9.0, 37°C707580 2D-image
0.01694-Succinate semialdehydeEscherichia coli-in 100 mM sodium phosphate buffer, pH 8.0, 30°C710394 2D-image
0.01694-Succinate semialdehydeEscherichia coli K-12P25526pH 8.0, 30°C710394 2D-image
0.0199-Succinate semialdehydePseudomonas putida-pH 8.0, 30°C707583 2D-image
0.04-Succinate semialdehydeKlebsiella pneumoniae-pH 7.8, 30°C288038 2D-image
1.06-Succinate semialdehydeEuglena gracilis-pH 8.7, 35°C288042 2D-image
additional information-additional informationCupriavidus necatorQ9RBF6enzyme does not obey Michaelis-Menten kinetics288054-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.08-3-tolualdehydeEscherichia coli-pH 8.5, 22°C690736 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4.1-Klebsiella pneumoniae-pH 7.8, 30°C288038
7.9-Euglena gracilis-pH 8.7, 35°C288042
14.9-Cupriavidus necatorQ9RBF6cosubstrate NAD+, pH 11.0, 30°C288054
34-Escherichia coli-pH 8.5, 22°C690736
132.1-Cupriavidus necatorQ9RBF6cosubstrate NADP+, pH 11.0, 30°C288054

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.57.8Klebsiella pneumoniae--288038
8.5-Escherichia coli--690736
8.7-Euglena gracilis--288042
9-Escherichia coli K-12--707580
11-Cupriavidus necatorQ9RBF6-288054

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
7.4-Escherichia coli-75% of maximum activity690736

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Escherichia coli-assay at690736
30-Klebsiella pneumoniae-assay at288038
31-Cupriavidus necatorQ9RBF6-288054
3545Euglena gracilis--288042
37-Escherichia coli K-12-assay at707580

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytosolEscherichia coli--5829707392Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
200000-Pseudomonas putida-gel filtration707583
300000-Klebsiella pneumoniae-gel filtration288038

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Cupriavidus necatorQ9RBF6x * 5022, calculated, x * 51000, SDS-PAGE288054
?Escherichia coli-x * 60000, calculated708907
tetramerEscherichia coli K-12P25526crystallographic data710394
tetramerEscherichia coli-x-ray crystallography710394

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
in complex with NADP+, hanging drop vapour diffusion method, using 0.2 M ammonium tartrate, 26-31% polyethylene glycol 3350, 10 mM beta-mercaptoethanol and 0.1 M Tris (pH 7.2-7.5)Escherichia coli-710394
to 1.4 A resolution. The overall structure of SSADH shares the general fold of ALDH classes 1 and 2. The SSADH monomer is composed of three domains; an N-terminal NAD(P)-binding domain of residues 1–125, 148–256, and 457–472, a catalytic domain of residues 257–456, and an oligomerization domain of residues 126–147 and 473–482. The catalytic loop of Escherichia coli SSADH, unlike that of human SSADH, does not undergo disulfide bond-mediated structural changes upon changes of environmental redox status. The protein is not regulated via redox-switch modulation. A difference in the conformation of the connecting loop beta15–beta16 causes the formation of a water molecule-mediated hydrogen bond network between the connecting loop and the catalytic loop in Escherichia coli SSADHEscherichia coli-707392
comparison to human enzyme, analysis of NADP+ binding site. Enzyme is a homotetramer with the 4 monomers related by a non-crystallographic 222 symmetry. The conserved catalytic site residues and active site residues correspond to C288 and E254 as well as R164, R282 and S445, respectivelyEscherichia coli K-12P25526710394

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
8-Escherichia coli K-12-rapid decrease in stability above707580

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
18-Escherichia coli K-12-14 h, 78% residual activity707580
37-Escherichia coli K-12-14 h, 69% residual activity707580
50-Cupriavidus necatorQ9RBF610 min, stable288054
60-Euglena gracilis-stable up to288042

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-15C, 14 h, 81% residual activityEscherichia coli K-12-707580
18C, 14 h, 78% residual activityEscherichia coli K-12-707580
5°C, unstable unless 30% glycerol is addedEuglena gracilis-288042

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
nickel chelating Sepharose column chromatography and S200 16/60 gel filtrationEscherichia coli-710394
recombinant enzymeEscherichia coli K-12P25526710394

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliCupriavidus necatorQ9RBF6288054
-Escherichia coli-690736, 708907
expressed in Escherichia coli BL21(DE3) cellsEscherichia coli-710394
expression in Escherichia coliEscherichia coli-707392
-Escherichia coli K-12P25526710394

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
the expression of gabD is not specifically induced by either 4-hydroxybutanoic acid or gamma-aminobutanoateCupriavidus necatorQ9RBF6288054
the genes gabT, coding for glutamate:succinic semialdehyde transaminase, and gabD, encoding succinic semialdehyde dehydrogenase, are cotranscribed from a promoter located upstream of gabDEscherichia coli-708907
decrease by growth of cells on gamma-aminobutanoateEscherichia coli K-12-707580
induction by growth on glutamateEuglena gracilis-288042
induction is highly coordinated with putrescine:2-oxoglutarate transaminase, gamma-aminobutyraldehyde dehydrogenase and gamma-aminobutyrate:2-oxoglutarate transaminase activitiesPseudomonas putida-707583

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
medicineEscherichia coli K-12P25526analysis of Escherichia coli SSADH structure with respect to human disease-linked mutations710394

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
288038Sanchez, M.; Fernandez, J.; Martin, M.; Gibello, A.; Garrido-Pertierra, A.Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniaeBiochim. Biophys. Acta990225-2311989Klebsiella pneumoniae PubMed
288042Tokunaga, M.; Nakano, Y.; Kitaoka, S.Separation and properties of the NAD-linked and NADP-linked isozymes of succinic semialdehyde dehydrogenase in Euglena gracilis zBiochim. Biophys. Acta42955-621976Euglena gracilis PubMed
288054Lutke-Eversloh, T.; Steinbuchel, A.Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutrophaFEMS Microbiol. Lett.18163-711999Cupriavidus necator PubMed
690736Jaeger, M.; Rothacker, B.; Ilg, T.Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenasesBiochem. Biophys. Res. Commun.372400-4062008Escherichia coli PubMed
707392Ahn, J.-W.; Kim, Y.-G.; Kim, K.-J.Crystal structure of non-redox regulated SSADH from Escherichia coliBiochem. Biophys. Res. Commun.392106-1112010Escherichia coli PubMed
707580Cozzani, I.; Fazio, A.M.; Felici, E.; Barletta, G.Separation and characterization of NAD- and NADP-specific succinate-semialdehyde dehydrogenase from Escherichia coli K-12 3300Biochim. Biophys. Acta613309-3171980Escherichia coli K-12 PubMed
707583Sanchez, M.; Alvarez, M.A.; Balana, R.; Garrido-Pertierra, A.Properties and functions of two succinic-semialdehyde dehydrogenases from Pseudomonas putidaBiochim. Biophys. Acta953249-2571988Pseudomonas putida PubMed
708907Bartsch, K.; von Johnn-Marteville, A.; Schulz, A.Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)J. Bacteriol.1727035-70421990Escherichia coli PubMed
710394Langendorf, 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 interactionsPLoS One5e92802010Escherichia coli, Escherichia coli K-12 PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.79)
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NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)