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Literature summary extracted from

  • Nowicki, M.W.; Kuaprasert, B.; McNae, I.W.; Morgan, H.P.; Harding, M.M.; Michels, P.A.; Fothergill-Gilmore, L.A.; Walkinshaw, M.D.
    Crystal structures of Leishmania mexicana phosphoglycerate mutase suggest a one-metal mechanism and a new enzyme subclass (2009), J. Mol. Biol., 394, 535-543.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.2.12 His-tagged enzyme is expressed in Escherichia coli BL21 cells Leishmania mexicana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.2.12 iPGAM crystallized with 3-phosphoglycerate or 2-phosphoglycerate at high and low cobalt concentrations (4 mM and 0.01 mM), hanging drop vapor diffusion method, using 0.08 M ammonium acetate, 0.04 M trisodium citrate dihydrate pH 6.0, and 24% (w/v) PEG 4000 Leishmania mexicana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.2.12 Co2+ two Co2+ are coordinated within the active site Leishmania mexicana

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.12 Leishmania mexicana Q86N96
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.2.12 metal affinity Talon column chromatography Leishmania mexicana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.2.12 2-phospho-D-glycerate
-
 Leishmania mexicana 3-phospho-D-glycerate
-
 r

Synonyms

EC Number Synonyms Comment Organism
5.4.2.12 cofactor-independent phosphoglycerate mutase 1
-
 Leishmania mexicana
5.4.2.12 iPGAM
-
 Leishmania mexicana

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.2.12 additional information phosphoglycerate mutase is cofactor-independent Leishmania mexicana