1.2.1.77: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+), go to the full flat file.
Reaction
Synonyms
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase, ALDH, ALDHC, BoxD, NADP+-dependent aldehyde dehydrogenase
ECTree
1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)Advanced search results
results (
results (Engineering
Engineering on EC 1.2.1.77 - 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C296A
same purification behavior as the native enzyme indicating that the mutation does not alter basic enzyme structure, but no catalytic activity detected consistent with a critical nucleophilic role for C296
E167A
significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 77%, likely candidate to present the catalytic water to the general base E257 that leads to deacylation and product release
E257Q
tolerated with respect to overall protein stability, but dramatic reduction in kcat value and no activity detectable, E257 serves probably as the primary general base to deprotonate the nucleophilic C296
E400A
91% reduction in kcat value, E400 plays an essential role in facilitating the acquisition of the hydride conformation
E496A
significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 90%
H485Q
completely recalcitrant to purification, H485 may be important in stabilizing the nicotinamide amide moiety of NADP+
K168A
significant reduction in enzyme activity but not perturbing the overall structure, significant reduction in activity of 92.5%, K168 likely serves to stabilize charges and tune pKa of the active site glutamate side-chains
