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Literature summary extracted from

  • Patterson, A.; Price, N.C.; Nairn, J.
    Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding (2010), Acta Crystallogr. Sect. F, 66, 1415-1420.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.2.4 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.2.4 hanging drop vapor diffusion method, using 18-22% (w/v) PEG 6K, 100 mM HEPES pH 6.8-7.2, at 17°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.4 Homo sapiens P07738
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.2.4 Ni-Speharose column chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.4.2.4 erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.4 1,3-Diphosphoglycerate
-
Homo sapiens 2,3-Diphosphoglycerate
-
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Synonyms

EC Number Synonyms Comment Organism
5.4.2.4 bisphosphoglycerate mutase
-
Homo sapiens
5.4.2.4 BPGAM a trifunctional enzyme that possesses mutase, synthase and phosphatase activities Homo sapiens