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Literature summary extracted from

  • McHarg, J.; Kelly, S.M.; Price, N.C.; Cooper, A.; Littlechild, J.A.
    Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase (1999), Eur. J. Biochem., 259, 939-945.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.3 overexpression in Saccharomyces cerevisiae Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.3 P204F site-directed mutagenesis, mutation in the hinge region of the enzyme, which plays a role in protein folding during catalysis, less well folded with considerable loss of secondary and tertiary structure, no activity Saccharomyces cerevisiae
2.7.2.3 P204H site-directed mutagenesis, mutation in the hinge region of the enzyme, which plays a role in protein folding during catalysis, secondary and tertiary structure is similar to the wild-type, but the mutant is less stable to heat and guanidinium chloride denaturation, 3-4fold increase of Km for 3-phospho-D-glycerate and ATP Saccharomyces cerevisiae

General Stability

EC Number General Stability Organism
2.7.2.3 Pro204 is important for stability and catalytic mechanism of the enzyme Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.3 Guanidinium chloride 0.5 M, 30% loss of activity for the mutant P204H, 5% loss of activity for the wild-type, both are unfolded at 1 M Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.3 additional information
-
 additional information kinetics Saccharomyces cerevisiae
2.7.2.3 0.33
-
 ATP wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 0.77
-
 3-phospho-D-glycerate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 1.25
-
 ATP mutant P204H, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 2.5
-
 3-phospho-D-glycerate mutant P204H, pH 7.5, 25°C Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate Saccharomyces cerevisiae
-
 ATP + 3-phospho-D-glycerate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.3 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate Pro204 is important for stability and catalytic mechanism of the enzyme Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.2.3 1.4
-
 purified mutant P204F Saccharomyces cerevisiae
2.7.2.3 4.5
-
 purified mutant P204H Saccharomyces cerevisiae
2.7.2.3 468
-
 purified wild-type enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.3 ADP + 3-phospho-D-glyceroyl phosphate
-
 Saccharomyces cerevisiae ATP + 3-phospho-D-glycerate
-
 r
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Saccharomyces cerevisiae ADP + 1,3-diphosphoglycerate
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.3 25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.3 3.4
-
 ATP mutant P204H, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 3.4
-
 3-phospho-D-glycerate mutant P204H, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 354
-
 ATP wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae
2.7.2.3 354
-
 3-phospho-D-glycerate wild-type enzyme, pH 7.5, 25°C Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.3 7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.3 ADP
-
 Saccharomyces cerevisiae
2.7.2.3 ATP required as phosphate donor Saccharomyces cerevisiae