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Literature summary for 1.1.1.284 extracted from

  • Sanghani, P.C.; Robinson, H.; Bosron, W.F.; Hurley, T.D.
    Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes (2002), Biochemistry, 41, 10778-10786.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method at 4°C from a 15-20 mg/ml enzyme solution equilibrated with 0.1 M potassium phosphate buffer pH 6.9-7.1, 0.1 mM ZnSO4, 1 mM dithiothreitol, 12-15% PEG8000. Binary complex with substrate 12-hydroxydodecanoic acid and a ternary complex with NAD+ and the inhibitor dodecanoic acid are determined at 2.0 and 2.3 A resolution by X-ray crystallography using the anomalous diffraction signal of zinc Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
dodecanoic acid
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc mettaloenzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
12-hydroxydodecanoic acid + glutathione + NAD+
-
Homo sapiens S-(11-carboxy)undecanyl-glutathione + NADH + H+
-
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Synonyms

Synonyms Comment Organism
ADH3
-
Homo sapiens
c-ADH
-
Homo sapiens
class III alcohol dehydrogenase
-
Homo sapiens
EC 1.2.1.1 formerly, part transferred Homo sapiens
FDH incorrect Homo sapiens
formaldehyde dehydrogenase incorrect Homo sapiens
formaldehyde dehydrogenase (glutathione) incorrect Homo sapiens
formic dehydrogenase incorrect Homo sapiens
GD-FAlDH
-
Homo sapiens
Glutathione-dependent formaldehyde dehydrogenase incorrect Homo sapiens
GS-FDH incorrect Homo sapiens
NAD- and glutathione-dependent formaldehyde dehydrogenase
-
Homo sapiens
NAD-dependent formaldehyde dehydrogenase
-
Homo sapiens
NAD-linked formaldehyde dehydrogenase incorrect Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens