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

BRENDA support

1.5.1.10: saccharopine dehydrogenase (NADP+, L-glutamate-forming)

This is an abbreviated version!
For detailed information about saccharopine dehydrogenase (NADP+, L-glutamate-forming), go to the full flat file.

Word Map on EC 1.5.1.10

Reaction

N6-(L-1,3-dicarboxypropyl)-L-lysine
+
NADP+
+
H2O
=
L-glutamate
+
(S)-2-amino-6-oxohexanoate
+
NADPH
+
H+

Synonyms

aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamic reductase, ASS, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide phosphate, glutamate-forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase (L-2-aminoadipate-semialdehyde forming), LKR/SDH, lysine-ketoglutarate reductase/saccharopine dehydrogenase, nSpe-Sdh, saccharopine dehydrogenase, saccharopine dehydrogenase (L-glutamate forming), saccharopine reductase, SDH, spermidine synthase-saccharopine dehydrogenase, SR1

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.10 saccharopine dehydrogenase (NADP+, L-glutamate-forming)

Crystallization

Crystallization on EC 1.5.1.10 - saccharopine dehydrogenase (NADP+, L-glutamate-forming)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
with hanging-drop vapour-diffusion technique
-
analysis of the apoenzyme crystal structure determined at 1.7 A resolution
apo form of enzyme. Protein consists of domain I, a variant of the Rossman fold and binding to NADPH, domain II with an alpha/beta structure and binding saccharopine, and domain III with all-helical fold involved in closing the active site of the enzyme once substrates are bound
-