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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.284
-
 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.284 D57L considerable loss of formaldehyde dehydrogenase activity Homo sapiens
1.1.1.284 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
1.1.1.284 T48A enzyme has essentially no alcohol dehydrogenase activity but has some glutathione-dependent formaldehyde dehydrogenase activity Homo sapiens
1.1.1.284 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

EC Number Organism UniProt Comment Textmining
1.1.1.284 Homo sapiens
-
 class II alcohol dehydrogenase
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.284 NAD+
-
 Homo sapiens