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Literature summary for 1.2.1.12 extracted from

  • Brownlee, A.G.; Phillips, D.R.; Polya, G.M.
    Purification and characterization of two high-affinity (adenosine 3,5-monophosphate)-binding proteins from yeast. Identification as multiple forms of glyceraldehyde-3-phosphate dehydrogenase (1980), Eur. J. Biochem., 109, 39-49.
    View publication on PubMed
Search for more literature for 1.2.1.12

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
 4 * 37000, SDS-PAGE Saccharomyces cerevisiae
180000
-
 gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 high-affnity cAMP-binding protein I and II
-

Purification (Commentary)

Purification (Comment) Organism
high-affinity cAMP-binding protein I and II Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Saccharomyces cerevisiae 3-phospho-D-glyceroyl phosphate + NADH
-
 ?
additional information high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 37000, SDS-PAGE Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Saccharomyces cerevisiae