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

BRENDA support

1.2.1.16: succinate-semialdehyde dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about succinate-semialdehyde dehydrogenase [NAD(P)+], go to the full flat file.

Word Map on EC 1.2.1.16

Reaction

succinate semialdehyde
+
NAD(P)+
+
H2O
=
succinate
+
NAD(P)H
+
H+

Synonyms

3-sulfopropanal dehydrogenase, ALDH, BADH, BsSSADH, cce4228, cce4228 protein, dehydrogenase, succinate semialdehyde (nicotinamide adenine dinucleotide (phosphate)), gabD, GabD dehydrogenase, GabD1, gapN-2, More, NAD(P)+-coupled 3-sulfopropanal dehydrogenase, NAD(P)+-dependent benzaldehyde dehydrogenase, NAD(P)+-dependent succinate semialdehyde dehydrogenase, NAD(P)+-dependent succinic semialdehyde dehydrogenase, NAD(P)-dependent benzaldehyde dehydrogenase, NAD+/NADP+-dependent benzaldehyde dehydrogenase, NAD+/NADP+-dependent SSADH, SpSSADH, SSA dehydrogenase, SSADH, SSADH-II, SSADHase, SSDH, SSO1842, ST0064, succinate semialdehyde dehydrogenase, succinate semialdehyde dehydrogenase (nicotinamide adenine dinucleotide (phosphate)), succinate-semialdehyde dehydrogenase, succinate-semialdehyde dehydrogenase (NAD(P)), succinate-semialdehyde dehydrogenase (NAD(P)+), succinic semialdehyde dehydrogenase, succinic semialdehyde:NAD(P)+ oxidoreductase, sulfopropanal dehydrogenase, YneI

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)+]

Engineering

Engineering on EC 1.2.1.16 - succinate-semialdehyde dehydrogenase [NAD(P)+]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K154A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
S157E
site-directed mutagenesis, the mutant shows reduced activity with NAD+/SSA and increased activity with NADP+/SSA compared to wild-type enzyme
K154A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type enzyme
-
S157E
-
site-directed mutagenesis, the mutant shows reduced activity with NAD+/SSA and increased activity with NADP+/SSA compared to wild-type enzyme
-
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
C103A
-
enzyme is inactive
C140A
C220A
C249A
D426A
E442A
F138A
K160A
K160E
N193A
R145A
R428A
S425A
W141A
D426A
-
strong decrease in activity
-
F138A
-
decrease in activity
-
K160A
-
Lys160 contributes to the enzyme preference to NAD+, strong decrease in activity
-
N193A
-
strong decrease in activity
-
S425A
-
decrease in activity
-
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