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BRENDA support

Literature summary for 5.4.2.4 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Homo sapiens P07738
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

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