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1.2.1.10: acetaldehyde dehydrogenase (acetylating)

This is an abbreviated version!
For detailed information about acetaldehyde dehydrogenase (acetylating), go to the full flat file.

Word Map on EC 1.2.1.10

Reaction

acetaldehyde
+
CoA
+
NAD+
=
acetyl-CoA
+
NADH
+
H+

Synonyms

4-hydroxy-2-ketovalerate aldolase/acylating acetaldehyde dehydrogenase, ACDH, acetaldehyde dehydrogenase, Acetaldehyde dehydrogenase [acetylating], acetaldehyde-alcohol dehydrogenase, acetyl-CoA reductase, acylating acetaldehyde dehydrogenase, AdhE, ADHES77, aldehyde dehydrogenase, aldehyde dehydrogenase (acylating), aldehyde/alcohol dehydrogenase, ALDH, BAD, bi-functional alcohol/aldehyde dehydrogenase, bifunctional acetaldehyde-alcohol dehydrogenase, BphJ, CoA-acylating aldehyde dehydrogenase, CoA-dependent aldehyde dehydrogenase, coenzyme A linked aldehyde dehydrogenase, coenzyme A-acylating aldehyde dehydrogenase, DmpF, DmpFG, MhpF, More, NAD+/CoA-dependent aldehyde dehydrogenase, nonphosphorylating acylating aldehyde dehydrogenase, PduP, Teth514_0627, Teth514_1942, Tsac_0416, TTHB247

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.10 acetaldehyde dehydrogenase (acetylating)

Subunits

Subunits on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
hexamer
6 * 97700, calculated, 6 * 94900, SDS-PAGE
homodimer
2 * 80000, SDS-PAGE
homotetramer
monomer
-
1 * 33344, electrospray ionization mass spectrometry
oligomer
the enzyme occurs in an oligomeric form called spirosomes. Incubation with NAD+ and Fe2+ is sufficient to extend the filaments. The addition of coenzyme A does not impair the conformational change triggered by NAD+ and Fe2+. In the same conditions, NADH and Fe2+ are not able to trigger a conformational change from the compact to the extended form. CryoEM analysis of the AdhE spirosomes in their compact and extended forms, enzyme filaments and quarternary structure analysis, overview
pentamer
5 * 51700, calculated, 5 * 52400, SDS-PAGE
polymer
-
ca. 40 * 96000, pyruvate-formate-lyase-deactivase with alcohol and aldehyde dehydrogenase activity, nucleotide sequence
tetramer
additional information