show all | hide all No of entries

Information on EC 1.4.99.6 - D-arginine dehydrogenase

for references in articles please use BRENDA:EC1.4.99.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25, L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.
Specify your search results
Select one or more organisms in this record: ?
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
D-alanine dehydrogenase, D-amino acid dehydrogenase, D-amino acid dehydrogenase DadA, DAADH, DAD, DadA, DADH, DauA, NADP+-dependent D-amino acid dehydrogenase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor
show the reaction diagram
D-arginine + acceptor = iminoarginine + reduced acceptor
show the reaction diagram
(1a)
-
-
0
iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3
show the reaction diagram
(1b), spontaneous
-
-
0
PATHWAY SOURCE
PATHWAYS
Select items on the left to see more content.