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Literature summary extracted from

  • Mercaldi, G.F.; Pereira, H.M; Cordeiro, A.T.; Michels, P.A.M.; Thiemann, O.H.
    Structural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutase (2012), FEBS J., 279, 2012-2021.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.2.12 additional information independent on 2,3-bisphosphoglycerate Trypanosoma brucei

Application

EC Number Application Comment Organism
5.4.2.12 drug development TbiPGAM is an attractive molecular target for drug development, the apoenzyme conformation described here provides opportunities for its use in structure-based drug design approaches Trypanosoma brucei

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.2.12 recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) Trypanosoma brucei

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.2.12 purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.003 ml of 8 mg/ml protein solution containing 20 mM Tris-acetate-EDTA, pH 7.4, 50 mM NaCl, 001 mM CoCl2, with 0.003 ml of reservoir solution containing 0.05 M ammonium sulfate, 0.1 M Bis-Tris, pH 6.1, and 25% w/v PEG 3350, 18°C, X-ray diffraction structure determination and analysis at 2.3 A resolution Trypanosoma brucei

Protein Variants

EC Number Protein Variants Comment Organism
5.4.2.12 D319A site-directed mutagenesis, substitution of the metal-binding residue Asp319 by Ala results in complete loss of independent PGAM activity Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.4.2.12 0.148
-
 3-phospho-D-glycerate recombinant enzyme, pH 7.4, 37°C Trypanosoma brucei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.2.12 Co2+ two metal sites (M1 and M2) containing cobalt ions are present in the phosphatase domain of the enzyme structure, interaction between Asp319 and the metal bound to the active site, contribution to the domain movement Trypanosoma brucei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.2.12 56000
-
 recombinant enzyme, gel filtration Trypanosoma brucei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.2.12 2-phospho-D-glycerate Trypanosoma brucei
-
 3-phospho-D-glycerate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.4.2.12 Trypanosoma brucei Q9NG18
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.2.12 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography and gel filtration Trypanosoma brucei

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
5.4.2.12 monomer 1 * 56000, SDS-PAGE, recombinant enzyme Trypanosoma brucei
5.4.2.12 More ligand-induced conformational changes, overview Trypanosoma brucei

Synonyms

EC Number Synonyms Comment Organism
5.4.2.12 independent PGAM
-
 Trypanosoma brucei
5.4.2.12 iPGAM
-
 Trypanosoma brucei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.2.12 37
-
 assay at Trypanosoma brucei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.4.2.12 3226
-
 3-phospho-D-glycerate recombinant enzyme, pH 7.4, 37°C Trypanosoma brucei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.2.12 7.4
-
 assay at Trypanosoma brucei

General Information

EC Number General Information Comment Organism
5.4.2.12 evolution PGAMs that are dependent on (EC 5.4.2.11) or independent of the 2,3-bisphosphoglycerate cofactor are members of two distinct protein families Trypanosoma brucei
5.4.2.12 additional information ligand-induced conformational changes, overview Trypanosoma brucei

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.4.2.12 3226
-
 3-phospho-D-glycerate recombinant enzyme, pH 7.4, 37°C Trypanosoma brucei