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Literature summary for 5.4.2.4 extracted from

  • Rose, Z.B.; Dube, S.
    The purification and kinetic properties of bisphosphoglycerate synthase from horse red blood cells (1976), Arch. Biochem. Biophys., 177, 284-292.
    View publication on PubMed
Search for more literature for 5.4.2.4

Activating Compound

Activating Compound Comment Organism Structure
2-phosphoglycerate required, can be substituted by 3-phosphoglycerate Equus caballus
3-phosphoglycerate required, can be substituted by 2-phosphoglycerate Equus caballus

Inhibitors

Inhibitors Comment Organism Structure
2,3-diphosphoglycerate product inhibition Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
copurification of EC 5.4.2.1 (phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase), three activities in one enzyme protein Equus caballus

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Equus caballus
-

Storage Stability

Storage Stability Organism
-80°C, precipitated with ammonium sulfate, 3 months stable Equus caballus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,3-Diphosphoglycerate
-
 Equus caballus 2,3-Diphosphoglycerate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6
-
 1,3-diphosphoglycerate 4°C Equus caballus
12.5
-
 1,3-diphosphoglycerate 25°C Equus caballus
23.4
-
 1,3-diphosphoglycerate 37°C Equus caballus