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), ALDH, BAD, 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, 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)

Engineering

Engineering on EC 1.2.1.10 - acetaldehyde dehydrogenase (acetylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
I171A
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I171F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
I195A
the variant has a 20fold higher catalytic efficiency for butyraldehyde and pentaldehyde compared to the catalytic efficiency of the wild type toward its natural substrate acetaldehyde. The mutation results in a 35% reduction in acetaldehyde channeling efficiency
I195F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
I195W
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
N170A
the mutation does not substantially alter aldehyde channeling efficiencies. The level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
N170D
level of activation of BphI by the mutant enzyme are reduced by more than 3fold in the presence of NADH and more than 4.5fold when the enzyme is undergoing turnover
I159A
additional information