1.2.1.79: succinate-semialdehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about succinate-semialdehyde dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.2.1.79
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1.2.1.79
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ssadhs
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nad+
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dehydrogenases
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tricarboxylic
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cyanobacterium
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2-oxoglutarate
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adduct
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moss
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tca
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syntrichia
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shunt
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synechococcus
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medicine
- 1.2.1.79
- ssadhs
- nad+
- dehydrogenases
-
tricarboxylic
- cyanobacterium
- 2-oxoglutarate
- adduct
-
moss
- tca
-
syntrichia
-
shunt
- synechococcus
- medicine
Reaction
Synonyms
AbSSADH, ALDH21, all3556, ApSSADH, gabD, GabD1, NADP+-dependent SSADH, NADP+-dependent succinic semialdehyde dehydrogenase, NADP-dependent succinic semialdehyde dehydrogenase, PpSSALDH, slr0370, Sp2771, SpSSADH, SSADH, SSADH-II, SSALDH, SSO1842, succinic semialdehy de dehydrogenase, succinic semialdehyde dehydrogenase, SYNPCC7002_A2771, SySSADH
ECTree
1.2.1.79 succinate-semialdehyde dehydrogenase (NADP+)Advanced search results
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results (Inhibitors
Inhibitors on EC 1.2.1.79 - succinate-semialdehyde dehydrogenase (NADP+)
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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
H2O2
50 microM H2O2 sharply reduces activity to 31% of the H2O2-free enzyme and activity further decreases to 3% at 1 mM H2O2
Succinic semialdehyde
partial substrate inhibition because velocity decreases to a non-zero value at saturating concentrations of Mg2+ and succinic semialdehyde
succinate semialdehyde
substrate inhhibition at 2 mM, not at 0.1 mM
succinate semialdehyde
uncompetitive substrate inhibition above 0.02 mM, in the presence of NADP+. Substrate inhibition is induced by the binding of inhibitory succinate semialdehyde in the cofactor-binding site, instead of NADP+
succinate semialdehyde
complete uncompetitive substrate inhibition. Structural comparison of the tertiary enzyme-succinate semialdehyde-NADP+-complex with a binary complex of SpSSADH with NADP indicates that the substrate inhibition is induced by the binding of inhibitory succinate semialdehyde in the cofactor-binding site, instead of NADP+
additional information
no product inhibition by succinate
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additional information
analysis of the kinetic inhibitory parameters revealed significant substrate inhibition in the presence of NADP+ at concentrations of succinate semialdehyde higher than 0.02 mM, which exhibits complete uncompetitive substrate inhibition, structure-based molecular insights into the substrate inhibition mechanism of SpSSADH, overview
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