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

BRENDA support

Literature summary extracted from

  • Tsuji, K.; Yoon, K.S.; Ogo, S.
    Biochemical characterization of a bifunctional acetaldehyde-alcohol dehydrogenase purified from a facultative anaerobic bacterium Citrobacter sp. S-77 (2016), J. Biosci. Bioeng., 121, 253-258 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.1 gene adhE, sequence comparisons Citrobacter sp. S-77
1.2.1.10 gene adhE, sequence comparisons Citrobacter sp. S-77

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 additional information
-
additional information Michaelis-Menten kinetics Citrobacter sp. S-77
1.1.1.1 7.43
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77
1.1.1.1 460
-
ethanol pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 additional information
-
additional information Michaelis-Menten kinetics Citrobacter sp. S-77
1.2.1.10 0.013
-
acetyl-CoA pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 10.5
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.1 plasma membrane
-
Citrobacter sp. S-77 5886
-
1.2.1.10 plasma membrane
-
Citrobacter sp. S-77 5886
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.10 400000
-
gel filtration Citrobacter sp. S-77

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 ethanol + NAD+ Citrobacter sp. S-77
-
acetaldehyde + NADH + H+
-
r
1.2.1.10 acetaldehyde + CoA + NAD+ Citrobacter sp. S-77
-
acetyl-CoA + NADH + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Citrobacter sp. S-77
-
-
-
1.2.1.10 Citrobacter sp. S-77
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.1 native enzyme from plasma membrane by ultracentrifugation, hydroxyapatite and hydrophobic interaction chromatography, followed by ultrafiltration and gel filtration Citrobacter sp. S-77
1.2.1.10 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 [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.1 1.7
-
purified native enzyme, pH 7.0, 30°C, ethanol oxidation with NAD+ Citrobacter sp. S-77
1.2.1.10 7.36
-
purified native enzyme, acetaldehyde oxidation with NAD+, pH 7.0, 30°C Citrobacter sp. S-77

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 ethanol + NAD+
-
Citrobacter sp. S-77 acetaldehyde + NADH + H+
-
r
1.2.1.10 acetaldehyde + CoA + NAD+
-
Citrobacter sp. S-77 acetyl-CoA + NADH + H+
-
?
1.2.1.10 acetaldehyde + CoA + NAD+ best substrates Citrobacter sp. S-77 acetyl-CoA + NADH + H+
-
r
1.2.1.10 acetaldehyde + CoA + NADP+ low activity with NADP+ compared to NAD+ Citrobacter sp. S-77 acetyl-CoA + NADPH + H+
-
r
1.2.1.10 butyraldehyde + CoA + NAD+ 21.0% activity compared to acetaldehyde Citrobacter sp. S-77 butyryl-CoA + NADH + H+
-
r
1.2.1.10 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 ?
-
?
1.2.1.10 propionaldehyde + CoA + NAD+ 51.8% activity compared to acetaldehyde Citrobacter sp. S-77 propionyl-CoA + NADH + H+
-
r
1.2.1.10 valerylaldehyde + CoA + NAD+ 5.6% activity compared to acetaldehyde Citrobacter sp. S-77 valeryl-CoA + NADH + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.2.1.10 homotetramer 4 * 96300, SDS-PAGE Citrobacter sp. S-77

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 acetaldehyde-alcohol dehydrogenase
-
Citrobacter sp. S-77
1.1.1.1 AdhE
-
Citrobacter sp. S-77
1.1.1.1 ADHES77
-
Citrobacter sp. S-77
1.1.1.1 bifunctional acetaldehyde-alcohol dehydrogenase
-
Citrobacter sp. S-77
1.2.1.10 acetaldehyde-alcohol dehydrogenase
-
Citrobacter sp. S-77
1.2.1.10 AdhE
-
Citrobacter sp. S-77
1.2.1.10 ADHES77
-
Citrobacter sp. S-77
1.2.1.10 bifunctional acetaldehyde-alcohol dehydrogenase
-
Citrobacter sp. S-77

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.1 30
-
assay at Citrobacter sp. S-77
1.2.1.10 40
-
-
Citrobacter sp. S-77

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.1.10 20 60 activity range, profile overview Citrobacter sp. S-77

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.10 30 35 purified native enzyme, 30 min, completely stable Citrobacter sp. S-77
1.2.1.10 40
-
purified native enzyme, 30 min, loss of 20% activity Citrobacter sp. S-77
1.2.1.10 45
-
purified native enzyme, 30 min, loss of 60% activity and partial thermal degradation Citrobacter sp. S-77
1.2.1.10 50
-
purified native enzyme, 30 min, complete inactivation and thermal degradation Citrobacter sp. S-77

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.1 2.5
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77
1.1.1.1 3.2
-
ethanol pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 0.013
-
acetyl-CoA pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 13
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 7
-
assay at Citrobacter sp. S-77
1.2.1.10 6.5
-
-
Citrobacter sp. S-77

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.10 5.5 8 narrow activity range, inactivation at pH 5.5, profile overview Citrobacter sp. S-77

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 additional information the purified ADHES77 prefers to use NAD+ as an electron acceptor as compared to NADP+. In the specific activity of ethanol dehydrogenase, the catalytic efficiency for NAD+ is about 56.7fold greater than for NADP+. Similarly, in the catalytic reduction of acetaldehyde, the ADHES77 preferentially utilizes NADH as an electron donor, exhibiting approximately 12.5fold 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
1.1.1.1 NAD+ preferred cofactor Citrobacter sp. S-77
1.1.1.1 NADH preferred cofactor Citrobacter sp. S-77
1.1.1.1 NADP+
-
Citrobacter sp. S-77
1.1.1.1 NADPH
-
Citrobacter sp. S-77
1.2.1.10 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
1.2.1.10 NAD+ preferred cofactor Citrobacter sp. S-77
1.2.1.10 NADH preferred cofactor Citrobacter sp. S-77
1.2.1.10 NADP+
-
Citrobacter sp. S-77
1.2.1.10 NADPH
-
Citrobacter sp. S-77

General Information

EC Number General Information Comment Organism
1.1.1.1 additional information the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region Citrobacter sp. S-77
1.1.1.1 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
1.2.1.10 additional information the enzyme's two functional domains are fused into a single polypeptide by a linker amino acid region Citrobacter sp. S-77
1.2.1.10 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.1 0.007
-
ethanol pH 7.0, 30°C Citrobacter sp. S-77
1.1.1.1 0.336
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 0.808
-
acetaldehyde pH 7.0, 30°C Citrobacter sp. S-77
1.2.1.10 192.31
-
acetyl-CoA pH 7.0, 30°C Citrobacter sp. S-77