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Literature summary for 1.1.1.284 extracted from

  • Sanghani, P.C.; Bosron, W.F.; Hurley, T.D.
    Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation (2002), Biochemistry, 41, 15189-15194.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion at 4°C. A 15-20 mg/ml enzyme solution equilibrated with a mother liquor containing 0.1 M phosphate buffer, pH 7.1, 10 mM ZnSO4, 1 mM DTT, and 12-16% PEG 8000. Ternary complex with S-(hydroxymethyl)glutathione and the reduced coenzyme to 2.6 A resolution Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc in the ternary complex with S-(hydroxymethyl)glutathione and the reduced coenzyme the active site zinc has a tetrahedral coordination environment with Cys44, His66 and Cys173 as the protein ligands in addition to S-(hydroxymethy)glutathione Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the enzyme plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Glutathione-dependent formaldehyde dehydrogenase
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Homo sapiens