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Literature summary extracted from

  • Cea, G.; Wilson, L.; Bolivar, J.; Markovits, A.; Illanes, A.
    Effect of chain length on the activity of free and immobilized alcohol dehydrogenase towards aliphatic alcohols (2009), Enzyme Microb. Technol., 44, 135-138.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 additional information Equus caballus activity is severely reduced towards aliphatic alcohols of more than 8 carbon atoms for the free enzyme, but not so with immobilized HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols higher than 50% of the highest value, obtained with C8 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Equus caballus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.1 liver
-
 Equus caballus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 butanol + NAD+ immobilized HLAD shows about 95% reaction rate and free HLAD shows about 90% reaction rate with butanol compared to ethanol at pH 8.8 and 30°C Equus caballus butyraldehyde + NADH + H+
-
 ?
1.1.1.1 docosanol + NAD+ immobilized HLAD shows about 60% reaction rate and free HLAD shows about 20% reaction rate with docosanol compared to ethanol at pH 8.8 and 30°C Equus caballus ? + NADH + H+
-
 ?
1.1.1.1 dodecanol + NAD+ immobilized HLAD shows about 60% reaction rate and free HLAD shows about 35% reaction rate with dodecanol compared to ethanol at pH 8.8 and 30°C Equus caballus dodecanal + NADH + H+
-
 ?
1.1.1.1 ethanol + NAD+ immobilized HLAD shows 100% reaction rate and free HLAD shows about 55% reaction rate with ethanol at pH 8.8 and 30°C Equus caballus aldehyde + NADH + H+
-
 ?
1.1.1.1 hexadecanol + NAD+ immobilized HLAD shows about 60% reaction rate and free HLAD shows about 15% reaction rate with hexadecanol compared to ethanol at pH 8.8 and 30°C Equus caballus hexadecanal + NADH + H+
-
 ?
1.1.1.1 additional information activity is severely reduced towards aliphatic alcohols of more than 8 carbon atoms for the free enzyme, but not so with immobilized HLAD, exhibiting an activity towards C22 and C24 aliphatic alcohols higher than 50% of the highest value, obtained with C8 Equus caballus ?
-
 ?
1.1.1.1 octanol + NAD+ immobilized and free HLAD show 100% reaction rate with octanol compared to ethanol at pH 8.8 and 30°C Equus caballus octanal + NADH + H+
-
 ?
1.1.1.1 tetracosanol + NAD+ immobilized HLAD shows about 55% reaction rate and free HLAD shows about 15% reaction rate with tetracosanol compared to ethanol at pH 8.8 and 30°C Equus caballus ? + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 HLAD
-
 Equus caballus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.1 35
-
 HLAD is a mesophilic enzyme whose activity and stability are significantly impaired at temperatures over 35°C Equus caballus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 8.8
-
 activity for both free and immobilized HLAD increases with pH up to 8.8 Equus caballus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
 Equus caballus