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Prokaryotic acetaldehyde dehydrogenase, dimerisation
Members of this family are found in prokaryotic acetaldehyde dehydrogenase (acylating), and adopt a structure consisting of an alpha-beta-alpha-beta(3) core. They mediate dimerisation of the protein [1]. [1]. 12764229. Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. Manjasetty BA, Powlowski J, Vrielink A;. Proc Natl Acad Sci U S A 2003;100:6992-6997. (from Pfam)
Semialdehyde dehydrogenase, NAD binding domain
This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase [1]. 10369777. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R;. J Mol Biol 1999;289:991-1002. (from Pfam)
acetaldehyde dehydrogenase
acetylating acetaldehyde dehydrogenase
acetylating acetaldehyde dehydrogenase catalyzes the formation of acetyl-CoA from acetalaldehyde
acetaldehyde dehydrogenase (acetylating)
Members of this protein family are acetaldehyde dehydrogenase (acetylating), EC 1.2.1.10. This enzyme oxidizes acetaldehyde, using NAD(+), and attaches coenzyme A (CoA), yielding acetyl-CoA. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate, etc.
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