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Literature summary for 1.1.1.284 extracted from

  • Estonius, M.; Hoeoeg, J.O.; Danielsson, O.; Joernvall, H.
    Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme (1994), Biochemistry, 33, 15080-15085.
    View publication on PubMed
Search for more literature for 1.1.1.284

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
D57L considerable loss of formaldehyde dehydrogenase activity Homo sapiens
D57L/Y93F fall in ratio kcat/Km for hydroxymethylglutathione by a factor of 1250, alcohol dehydrogenase activity of the mutant has gained a characteristic class I property, complete inhibition by 4-methylpyrazole at concentrations only partially reducing the activity of the wild-type class III enzyme Homo sapiens
T48A enzyme has essentially no alcohol dehydrogenase activity but has some glutathione-dependent formaldehyde dehydrogenase activity Homo sapiens
Y93F decreased turnover number for substrates in general, inhibition of alcohol dehydrogenase activity by 4-methylpyrazole, which is not found in the wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 class II alcohol dehydrogenase
-

Purification (Commentary)

Purification (Comment) Organism
wild-type recombinant enzyme Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formaldehyde + glutathione + NAD+
-
 Homo sapiens S-formylglutathione + NADH + H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Homo sapiens