Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.1.49 extracted from

  • Sepulveda, C.; Poch, A.; Espinoza, R.; Cardemil, E.
    Electrostatic interactions play a significant role in the affinity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase for Mn2+ (2010), Biochimie, 92, 814-819.
    View publication on PubMed
Search for more literature for 4.1.1.49

Protein Variants

Protein Variants Comment Organism
E272Q the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 11fold Saccharomyces cerevisiae
E284Q the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 69fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity Saccharomyces cerevisiae
K212M the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 17fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity Saccharomyces cerevisiae
K212R the mutation does not affect the Mn2+ affinity of the enzyme Saccharomyces cerevisiae
K213Q the mutation increases the activation constant for Mn2+ in the main reaction of the enzyme 107fold, the mutation changes the nucleotide-independent oxalacetate decarboxylase activity of PEP carboxykinase into an ADP-requiring activity Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
 oxaloacetate mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.068
-
 oxaloacetate mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.13
-
 oxaloacetate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.17
-
 phosphoenolpyruvate mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.185
-
 phosphoenolpyruvate mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.2
-
 oxaloacetate mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.216
-
 phosphoenolpyruvate mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.238
-
 oxaloacetate mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.307
-
 phosphoenolpyruvate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.32
-
 phosphoenolpyruvate mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.651
-
 phosphoenolpyruvate mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
2
-
 oxaloacetate Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
2 3 CO2 mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
9
-
 CO2 mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
11
-
 CO2 mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
14
-
 CO2 mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
17
-
 CO2 wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activated by Mn2+ Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + oxaloacetate
-
 Saccharomyces cerevisiae ADP + phosphoenolpyruvate + CO2
-
 r

Synonyms

Synonyms Comment Organism
PEP carboxykinase
-
 Saccharomyces cerevisiae
PEPCK
-
 Saccharomyces cerevisiae
phosphoenolpyruvate carboxykinase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.014
-
 phosphoenolpyruvate mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.07
-
 phosphoenolpyruvate mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.08
-
 oxaloacetate Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.08
-
 oxaloacetate mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.11
-
 oxaloacetate mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.13
-
 phosphoenolpyruvate mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.28
-
 oxaloacetate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.58
-
 oxaloacetate mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.85
-
 oxaloacetate mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
5.1
-
 phosphoenolpyruvate mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
19
-
 phosphoenolpyruvate mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
63
-
 phosphoenolpyruvate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae