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Literature summary for 1.1.1.1 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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
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?

Organism

Organism UniProt Comment Textmining
Equus caballus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
liver
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Equus caballus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
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?
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+
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?
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+
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?
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+
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?
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+
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?
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 ?
-
?
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+
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?
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+
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?

Synonyms

Synonyms Comment Organism
HLAD
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Equus caballus

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
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Equus caballus