Literature summary for 5.4.2.12 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.

Search for more literature for 5.4.2.12

Activating Compound

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

Application

Application	Comment	Organism
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)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants	Comment	Organism
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]

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei	Q9NG18	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
independent PGAM	-	Trypanosoma brucei
iPGAM	-	Trypanosoma brucei

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

General Information

General Information	Comment	Organism
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
additional information	ligand-induced conformational changes, overview	Trypanosoma brucei

kcat/KM [mM/s]

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

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Release 2023.1 (January 2023)