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Literature summary extracted from

  • McLoughlin, D.J.; MacQuarrie, R.
    Purification and properties of the major isozymic form of cytoplasmic glycerol-3-phosphate dehydrogenase from rabbit liver (1978), Biochim. Biophys. Acta, 527, 204-211.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.8 0.022
-
NADH
-
Oryctolagus cuniculus
1.1.1.8 0.075
-
dihydroxyacetone phosphate
-
Oryctolagus cuniculus
1.1.1.8 0.083
-
NAD+
-
Oryctolagus cuniculus
1.1.1.8 0.909
-
glycerol 3-phosphate
-
Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.8 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.8 sequential affinity chromatography Oryctolagus cuniculus
1.1.1.8 several isozymes, distinct in isoelectric points Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.8 liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.8 295
-
-
Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
1.1.1.8 4°C, stable Oryctolagus cuniculus

Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.8 NAD+
-
Oryctolagus cuniculus
1.1.1.8 NADH
-
Oryctolagus cuniculus