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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.1.21 - aspartate dehydrogenase

for references in articles please use BRENDA:EC1.4.1.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme is strictly specific for L-aspartate as substrate. It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyses spontaneously to form oxaloacetate. The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC 2.5.1.72, quinolinate synthase, preventing its hydrolysis and enabling the de novo biosynthesis of NAD+.
Specify your search results
Select one or more organisms in this record: ?
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
aspartate dehydrogenase, l-aspdh, aspdh, l-aspartate dehydrogenase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-iminosuccinate + H2O = oxaloacetate + NH3
show the reaction diagram
(1b), spontaneous
-
-
-
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
show the reaction diagram
overall reaction
-
-
-
L-aspartate + NAD(P)+ = 2-iminosuccinate + NAD(P)H + H+
show the reaction diagram
(1a)
-
-
-
PATHWAY SOURCE
PATHWAYS
Select items on the left to see more content.