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

BRENDA support

Literature summary for 1.5.1.6 extracted from

  • Tsybovsky, Y.; Malakhau, Y.; Strickland, K.C.; Krupenko, S.A.
    The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1 (2013), Chem. Biol. Interact., 202, 62-69 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.6

Protein Variants

Protein Variants Comment Organism
C707A site-directed mutagenesis of the C-terminal residue, replacement of Cys707 with an alanine results in the enzyme lacking the ability to differentiate between the oxidized and reduced coenzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the C-terminal domain (Ct-FDH) of the enzyme is a structural and functional homologue of aldehyde dehydrogenases (ALDHs, EC 1.2.1.4). This domain is capable of catalyzing the NADP+-dependent oxidation of short chain aldehydes to their corresponding acids, and similar to most ALDHs it has two conserved catalytic residues, Cys707 and Glu673. These residues define the conformation of the bound coenzyme and the affinity of its interaction with the protein, proposed mechanism by which Cys707 helps to differentiate between the oxidized and reduced coenzyme during ALDH catalysis, overview Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
10-formyltetrahydrofolate dehydrogenase
-
 Rattus norvegicus
ALDH1L1
-
 Rattus norvegicus
FDH
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Rattus norvegicus