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Literature summary for 1.2.1.10 extracted from

  • Smith, L.T.; Kaplan, N.O.
    Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri (1980), Arch. Biochem. Biophys., 203, 663-675.
    View publication on PubMed
Search for more literature for 1.2.1.10

General Stability

General Stability Organism
dithioerythritol stabilizes Clostridium kluyveri
no stabilization by detergents, acetone, ethanol, NAD+, glycerol, CoA, anaerobic conditions Clostridium kluyveri

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA competitive inhibitor with respect to NAD+; competitive to NAD+ Clostridium kluyveri
NADH competitive inhibitor with respect to CoA; competitive to CoA Clostridium kluyveri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
 CoA
-
 Clostridium kluyveri
0.3
-
 NAD+
-
 Clostridium kluyveri
0.39
-
 acetaldehyde
-
 Clostridium kluyveri
11
-
 pantetheine
-
 Clostridium kluyveri
22
-
 2-mercaptoethanol
-
 Clostridium kluyveri

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol soluble fraction Clostridium kluyveri 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
290000
-
 gel filtration and sedimentation coefficient Clostridium kluyveri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetaldehyde + CoA + NAD+ Clostridium kluyveri during ethanol fermentation acetyl-CoA + NADH
-
 r

Organism

Organism UniProt Comment Textmining
Clostridium kluyveri
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Clostridium kluyveri

Reaction

Reaction Comment Organism Reaction ID
acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH + H+ bi-uni-uni-uni-ping-pong mechanism Clostridium kluyveri
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
48.6
-
-
 Clostridium kluyveri

Storage Stability

Storage Stability Organism
-70°C, 10 mM Tris-HCl buffer, pH 8, 3 mM dithioerythritol, 2 weeks, 15% loss of activity Clostridium kluyveri
-70°C, 3 mM dithioerythritol, 85% of enzymatic activity remains after 2 weeks Clostridium kluyveri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + 2-mercaptoethanol + NAD+ 14% activity compared to CoA Clostridium kluyveri S-acetyl-2-mercaptoethanol + NADH + H+
-
 r
acetaldehyde + CoA + NAD+ 0.1 mM CoA can be replaced by 25 mM pantetheine, 46% of CoA activity, 25 mM 2-mercaptoethanol, 14% of CoA activity, 25 mM dithioerythritol, 10% of CoA activity, 25 mM glutathione, 8.6% of CoA activity, 25 mM cysteamine, 4.6% of CoA activity Clostridium kluyveri acetyl-CoA + NADH
-
 r
acetaldehyde + CoA + NAD+ during ethanol fermentation Clostridium kluyveri acetyl-CoA + NADH
-
 r
acetaldehyde + pantetheine + NAD+ 46% activity compared to CoA Clostridium kluyveri S-acetyl-pantetheine + NADH + H+
-
 r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
 NADH oxidation Clostridium kluyveri
6.8
-
 NADH oxidation, with potassium phosphate buffer Clostridium kluyveri
9.1
-
 NAD+ reduction Clostridium kluyveri

pH Range

pH Minimum pH Maximum Comment Organism
5 8 less than 50% of maximal activity above and below Clostridium kluyveri

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 8 enzyme activity falls to 50% at pH 5 and pH 8 Clostridium kluyveri

Cofactor

Cofactor Comment Organism Structure
CoA
-
 Clostridium kluyveri
additional information enzyme is able to acetylate other thiols than CoA, e.g. pantetheine, 2-mercaptoethanol, dithioerythritol, glutathione, cysteamine Clostridium kluyveri
NAD+
-
 Clostridium kluyveri