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Literature summary for 5.4.2.4 extracted from

  • Chu, W.T.; Zheng, Q.C.; Zhang, H.X.
    Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation (2014), Phys. Chem. Chem. Phys., 16, 3946-3954.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-phospho-D-glyceroyl phosphate Homo sapiens
-
2,3-bisphospho-D-glycerate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-
placenta
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glyceroyl phosphate
-
Homo sapiens 2,3-bisphospho-D-glycerate
-
?

Synonyms

Synonyms Comment Organism
BPGM
-
Homo sapiens

General Information

General Information Comment Organism
metabolism the main activity of the enzyme is synthase (EC 5.4.2.4), converting 1,3-bisphosphoglycerate to 2,3-bisphosphoglycerate. The second activity is mutase (phosphoglycerate mutase, EC 5.4.2.1), catalyzing the interconversion between 2-phosphoglycerate and 3-phosphoglycerate. The third activity is phosphatase (S-succinylglutathione hydrolase, EC 3.1.3.13), hydrolyzing 2,3-bisphosphoglycerate to 3-phosphoglycerate or 2-phosphoglycerate and phosphate Homo sapiens
additional information proposed mechanisms for the phosphatase and the synthase reactions involving residues His11 and Glu89 Homo sapiens
physiological function bisphosphoglycerate mutase is a multi-activity enzyme. Its main function is to synthesize the 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin, the enzyme regulates 2,3-bisphosphoglycerate levels, quantum mechanics/molecular mechanics simulations based on the metadynamics and umbrella sampling simulations, detailed overview Homo sapiens