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Literature summary for 1.2.1.12 extracted from

  • Chernorizov, K.A.; Elkina, J.L.; Semenyuk, P.I.; Svedas, V.K.; Muronetz, V.I.
    Novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase: covalent modification of NAD-binding site by aromatic thiols (2010), Biochemistry (Moscow), 75, 1444-1449.
    View publication on PubMed
Search for more literature for 1.2.1.12

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: N-((R)-mandelyl)-(S)-cysteine Oryctolagus cuniculus
N-(phenoxyacetyl)-L-cysteine inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site Oryctolagus cuniculus
N-(phenylacetyl)-glutathione inhibits by forming disulfide bonds with the Cys149 residue in the enzyme active site Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
101
-
 pH 8.9, 22°C Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Oryctolagus cuniculus 3-phospho-D-glyceroyl phosphate + NADH
-
 ?