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Literature summary for 1.2.1.12 extracted from

  • Arutyunova, E.I.; Danshina, P.V.; Domnina, L.V.; Pleten, A.P.; Muronetz, V.I.
    Oxidation of glyceraldehyde-3-phosphate dehydrogenase enhances its binding to nucleic acids (2003), Biochem. Biophys. Res. Commun., 307, 547-552.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress ?
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress Oryctolagus cuniculus ?
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 ?
additional information oxidation of SH-groups of the active site of GAPDH enhances its binding with total transfer RNA or with total DNA. Both NAD+ and NADH inhibit GAPDH-RNA or GAPDH-DNA interaction Oryctolagus cuniculus ?
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 ?

Synonyms

Synonyms Comment Organism
GAPDH
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 Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Oryctolagus cuniculus
NADH
-
 Oryctolagus cuniculus