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Literature summary for 2.7.2.3 extracted from

  • Bojanovski, M.; Kulbe, K.D.; Lamprecht, W.
    Liver 3-phosphoglycerate kinase. Purification and some molecular properties of the bovine-liver enzyme (1974), Eur. J. Biochem., 45, 321-331.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization from ammonium sulfate precipitation Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
250fold from liver, to homogeneity Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
143
-
purified enzyme Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 3-phospho-D-glycerate
-
Bos taurus ADP + 1,3-diphosphoglycerate
-
r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Bos taurus

pH Stability

pH Stability pH Stability Maximum Comment Organism
6
-
unstable below Bos taurus

Cofactor

Cofactor Comment Organism Structure
ADP
-
Bos taurus
ATP required as phosphate donor Bos taurus

pI Value

Organism Comment pI Value Maximum pI Value
Bos taurus 3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
-
3.8
Bos taurus 3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
-
5.75
Bos taurus 3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
-
7.45