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Literature summary for 1.1.1.8 extracted from

  • Brosemer, R.W.; Kuhn, R.W.
    Comparative structural properties of honeybee and rabbit alpha-glycerophosphate dehydrogenases (1969), Biochemistry, 8, 2095-2105.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
adenosine diphosphate ribose 0.094 mM slightly inhibits NADH binding by honeybee GPDH, but not by rabbit GPDH Apis mellifera
adenosine diphosphate ribose
-
Oryctolagus cuniculus
L-glycerol 3-phosphate inhibits dihydroxyacetone phosphate reduction Apis mellifera
L-glycerol 3-phosphate inhibits dihydroxyacetone phosphate reduction Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid analysis Oryctolagus cuniculus
additional information
-
amino acid analysis Apis mellifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sn-glycerol 3-phosphate + NAD+ Oryctolagus cuniculus
-
dihydroxyacetone phosphate + NADH + H+
-
r
sn-glycerol 3-phosphate + NAD+ Apis mellifera
-
dihydroxyacetone phosphate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Apis mellifera
-
honey bee
-
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle thoracic flight muscle Apis mellifera
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sn-glycerol 3-phosphate + NAD+
-
Oryctolagus cuniculus dihydroxyacetone phosphate + NADH + H+
-
r
sn-glycerol 3-phosphate + NAD+
-
Apis mellifera dihydroxyacetone phosphate + NADH + H+
-
r

Subunits

Subunits Comment Organism
dimer
-
Apis mellifera
dimer determined after carboxypeptidase A digestion Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
NADH 2 mol per mol enzyme Oryctolagus cuniculus
NADH 2 mol per mol enzyme Apis mellifera