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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.16 - succinate-semialdehyde dehydrogenase [NAD(P)+] and Organism(s) Bacillus subtilis and UniProt Accession P94428

for references in articles please use BRENDA:EC1.2.1.16
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: P94428 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
succinic semialdehyde dehydrogenase, ssdh, succinate semialdehyde dehydrogenase, succinate-semialdehyde dehydrogenase, spssadh, gabd1, ssa dehydrogenase, cce4228 protein, cce4228, st0064, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, succinate semialdehyde (nicotinamide adenine dinucleotide (phosphate))
-
-
-
-
NAD(P)+-dependent succinic semialdehyde dehydrogenase
-
-
SSDH
-
-
-
-
succinate semialdehyde dehydrogenase (nicotinamide adenine dinucleotide (phosphate))
-
-
-
-
succinate-semialdehyde dehydrogenase (NAD(P))
-
-
-
-
succinate-semialdehyde dehydrogenase (NAD(P)+)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
succinate-semialdehyde:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-88-7
-
SUBSTRATE
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 + 2 H+
show the reaction diagram
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
-
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + 2 H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
-
-
-
-
?
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 + 2 H+
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + NADP+ + H2O
succinate + NADPH + 2 H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
similar values of the catalytic efficiency (kcat/Km) with both NAD+ and NADP+ as cofactors
NADP+
similar values of the catalytic efficiency (kcat/Km) with both NAD+ and NADP+ as cofactors
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+
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Succinic semialdehyde
complete uncompetitive substrate inhibition
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
NAD+
pH not specified in the publication, 30°C
0.39
NADP+
pH not specified in the publication, 30°C
10.36 - 20.5
succinate semialdehyde
0.21
NAD+
-
pH and temperature not specified in the publication
0.39
NADP+
-
pH and temperature not specified in the publication
10.36 - 20.5
succinate semialdehyde
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.26
NAD+
pH not specified in the publication, 30°C
9.93
NADP+
pH not specified in the publication, 30°C
5.61 - 7.24
succinate semialdehyde
5.26
NAD+
-
pH and temperature not specified in the publication
9.93
NADP+
-
pH and temperature not specified in the publication
5.61 - 7.24
succinate semialdehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.1
NAD+
pH not specified in the publication, 30°C
25.4
NADP+
pH not specified in the publication, 30°C
0.36 - 0.6
succinate semialdehyde
25.1
NAD+
-
pH and temperature not specified in the publication
25.4
NADP+
-
pH and temperature not specified in the publication
0.362 - 0.598
succinate semialdehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28.3 - 470.6
succinate semialdehyde
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
succinic semialdehyde dehydrogenase (SSADH) catalyzes the oxidation of succinic semialdehyde (SSA) into succinic acid in the final step of gamma-aminobutyric acid degradation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team