Cloned (Comment) | Organism |
---|---|
gene adhE, sequence comparisons | Citrobacter sp. S-77 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Citrobacter sp. S-77 | |
0.013 | - |
acetyl-CoA | pH 7.0, 30°C | Citrobacter sp. S-77 | |
10.5 | - |
acetaldehyde | pH 7.0, 30°C | Citrobacter sp. S-77 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
plasma membrane | - |
Citrobacter sp. S-77 | 5886 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
400000 | - |
gel filtration | Citrobacter sp. S-77 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetaldehyde + CoA + NAD+ | Citrobacter sp. S-77 | - |
acetyl-CoA + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Citrobacter sp. S-77 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from plasma membrane by ultracentrifugation, hydroxyapatite and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration. The enzyme cannot be solubilized from membrane with detergents, either 1% Triton X-100 or 1% sulfobetaine 3-12 | Citrobacter sp. S-77 |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
7.36 | - |
purified native enzyme, acetaldehyde oxidation with NAD+, pH 7.0, 30°C | Citrobacter sp. S-77 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetaldehyde + CoA + NAD+ | - |
Citrobacter sp. S-77 | acetyl-CoA + NADH + H+ | - |
? | |
acetaldehyde + CoA + NAD+ | best substrates | Citrobacter sp. S-77 | acetyl-CoA + NADH + H+ | - |
r | |
acetaldehyde + CoA + NADP+ | low activity with NADP+ compared to NAD+ | Citrobacter sp. S-77 | acetyl-CoA + NADPH + H+ | - |
r | |
butyraldehyde + CoA + NAD+ | 21.0% activity compared to acetaldehyde | Citrobacter sp. S-77 | butyryl-CoA + NADH + H+ | - |
r | |
additional information | the enzyme has the ability to oxidize straight-chain aldehydes. The ADHES77 shows relatively high specific activity for acetaldehyde, as compared to activities for propionaldehyde, butyraldehyde, and valeraldehyde. The ADHES77 can use various types of aldehydes as substrates, in which the ADHES77 has a preference for C2 acetaldehyde when compared to C3-C5 aldehydes. No activity with formaldehyde and benzaldehyde as substrates | Citrobacter sp. S-77 | ? | - |
? | |
propionaldehyde + CoA + NAD+ | 51.8% activity compared to acetaldehyde | Citrobacter sp. S-77 | propionyl-CoA + NADH + H+ | - |
r | |
valerylaldehyde + CoA + NAD+ | 5.6% activity compared to acetaldehyde | Citrobacter sp. S-77 | valeryl-CoA + NADH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 96300, SDS-PAGE | Citrobacter sp. S-77 |
Synonyms | Comment | Organism |
---|---|---|
acetaldehyde-alcohol dehydrogenase | - |
Citrobacter sp. S-77 |
AdhE | - |
Citrobacter sp. S-77 |
ADHES77 | - |
Citrobacter sp. S-77 |
bifunctional acetaldehyde-alcohol dehydrogenase | - |
Citrobacter sp. S-77 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | - |
- |
Citrobacter sp. S-77 |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 60 | activity range, profile overview | Citrobacter sp. S-77 |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 35 | purified native enzyme, 30 min, completely stable | Citrobacter sp. S-77 |
40 | - |
purified native enzyme, 30 min, loss of 20% activity | Citrobacter sp. S-77 |
45 | - |
purified native enzyme, 30 min, loss of 60% activity and partial thermal degradation | Citrobacter sp. S-77 |
50 | - |
purified native enzyme, 30 min, complete inactivation and thermal degradation | Citrobacter sp. S-77 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.013 | - |
acetyl-CoA | pH 7.0, 30°C | Citrobacter sp. S-77 | |
13 | - |
acetaldehyde | pH 7.0, 30°C | Citrobacter sp. S-77 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Citrobacter sp. S-77 |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8 | narrow activity range, inactivation at pH 5.5, profile overview | Citrobacter sp. S-77 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the purified ADHES77 preferred to use NAD+ as an electron acceptor as compared to NADP+. In the specific activities of acetaldehyde dehydrogenase, the catalytic efficiencies for NAD+ i about 15.7 greater than for NADP+. Similarly, in the catalytic reductions of acetyl-CoA, the ADHES77 preferentially utilizes NADH as an electron donor, exhibiting approximately 5.6fold higher activity than for NADPH. The results suggest that the ADHES77 prefers to use NAD(H) as redox partners as compared to NADP(H) | Citrobacter sp. S-77 | |
NAD+ | preferred cofactor | Citrobacter sp. S-77 | |
NADH | preferred cofactor | Citrobacter sp. S-77 | |
NADP+ | - |
Citrobacter sp. S-77 | |
NADPH | - |
Citrobacter sp. S-77 |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region | Citrobacter sp. S-77 |
physiological function | acetaldehyde-alcohol dehydrogenase (ADHE) is a bifunctional enzyme consisting of two domains of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase (ADH). The N-terminal domain is responsible for the conversion of acetyl-CoA to acetaldehyde and the C-terminal domain is subsequently responsible for the conversion of acetaldehyde to ethanol. The enzyme is important in the cellular alcohol metabolism. The coenzyme A-acylating ADHE from Citrobacter sp. S-77 may play a pivotal role in modulating intracellular acetaldehyde concentration | Citrobacter sp. S-77 |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.808 | - |
acetaldehyde | pH 7.0, 30°C | Citrobacter sp. S-77 | |
192.31 | - |
acetyl-CoA | pH 7.0, 30°C | Citrobacter sp. S-77 |