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

BRENDA support

Literature summary for 1.2.1.10 extracted from

  • Lei, Y.; Pawelek, P.D.; Powlowski, J.
    A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds (2008), Biochemistry, 47, 6870-6882.
    View publication on PubMed
Search for more literature for 1.2.1.10

Cloned(Commentary)

Cloned (Comment) Organism
pT7.5-dmpFG plasmid expressed in Escherichia coli C41(DE3) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli XL2-Blue
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on DEAE and NAD+-linked affinity columns, combined with an ammonium sulfate fractionation step Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + CoA + NAD+ + H+
-
 Escherichia coli acetyl-CoA + NADH
-
 ?
acetaldehyde + CoA + NAD+ + H+
-
 Escherichia coli XL2-Blue acetyl-CoA + NADH
-
 ?

Synonyms

Synonyms Comment Organism
DmpF
-
 Escherichia coli
NAD+/CoA-dependent aldehyde dehydrogenase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
CoA shares a binding site with NAD+. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis Escherichia coli
NAD+ shares a binding site with CoA. Rossmann fold can alternately bind CoA or NAD+ cofactors required for enzymatic catalysis Escherichia coli