Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+) and Organism(s) Escherichia coli and UniProt Accession P25526

for references in articles please use BRENDA:EC1.2.1.79
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This 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+ .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P25526
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
aldh21, sp2771, syssadh, abssadh, apssadh, all3556, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
succinic semialdehyde dehydrogenase
-
SYSTEMATIC NAME
IUBMB Comments
succinate-semialdehyde:NADP+ oxidoreductase
This 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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-carboxybenzaldehyde + NADP+ + H2O
3-carboxybenzoate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
3-nitrobenzaldehyde + NADP+ + H2O
3-nitrobenzoate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
4-carboxybenzaldehyde + NADP+ + H2O
4-carboxybenzoate + NADPH + H+
show the reaction diagram
-
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
n-butanal + NADP+ + H2O
butanoate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
n-hexanal + NADP+ + H2O
hexanoate + NADPH + H+
show the reaction diagram
-
-
-
?
n-pentanal + NADP+ + H2O
n-pentanoate + NADPH + H+
show the reaction diagram
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + H+
show the reaction diagram
the enzyme activity in the presence of NADP+ is approximately 20fold higher than that measured in the presence of NAD+
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADP+
-
enzyme is specific for NADP+ as a cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-tolualdehyde
only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0446
NADP+
pH 8.5, 22°C
0.0078 - 0.01694
succinate semialdehyde
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
3-tolualdehyde
Escherichia coli
pH 8.5, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34
pH 8.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
75% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
x * 60000, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
x-ray crystallography
?
-
x * 60000, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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)
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 SSADH
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel chelating Sepharose column chromatography and S200 16/60 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the genes gabT, coding for glutamate:succinic semialdehyde transaminase, and gabD, encoding succinic semialdehyde dehydrogenase, are cotranscribed from a promoter located upstream of gabD
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli (P25526)
Manually annotated by BRENDA team
Ahn, J.-W.; Kim, Y.-G.; Kim, K.-J.
Crystal structure of non-redox regulated SSADH from Escherichia coli
Biochem. Biophys. Res. Commun.
392
106-111
2010
Escherichia coli
Manually annotated by BRENDA team
Bartsch, 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.
172
7035-7042
1990
Escherichia coli
Manually annotated by BRENDA team
Langendorf, C.G.; Key, T.L.; Fenalti, G.; Kan, W.T.; Buckle, A.M.; Caradoc-Davies, T.; Tuck, K.L.; Law, R.H.; Whisstock, J.C.
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions
PLoS One
5
e9280
2010
Escherichia coli (P25526), Escherichia coli K-12 (P25526), Escherichia coli MC1061 (P25526)
Manually annotated by BRENDA team