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Literature summary for 4.1.1.49 extracted from

  • Perez, E.; Cardemil, E.
    Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: the relevance of Glu299 and Leu460 for nucleotide binding (2010), Protein J., 29, 299-305.
    View publication on PubMed
Search for more literature for 4.1.1.49

Cloned(Commentary)

Cloned (Comment) Organism
expressed in the PEP carboxykinase-deficient Saccharomyces cerevisiae strain PUK-3B Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
E299A the mutation has no effect on catalytic efficiency Saccharomyces cerevisiae
L460A the mutation decreases the catalytic efficiency to about 14% of the wild type value as a consequence of the 7fold increase in the Km (ATP-Mn2-). The mutation decreases the catalytic efficiency to about 7% of the wild type value as a consequence of the 3fold increase in Km (ADP-Mn-) and the reduction in kcat Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 ADP mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.026
-
 ATP mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.03
-
 ATP wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.034
-
 ADP wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.051
-
 oxaloacetate mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.066
-
 oxaloacetate wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.099
-
 ADP mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.104
-
 phosphoenolpyruvate mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.108
-
 phosphoenolpyruvate mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.13
-
 oxaloacetate mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.204
-
 ATP mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
0.307
-
 phosphoenolpyruvate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
14
-
 CO2 mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
18
-
 CO2 wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
47
-
 CO2 mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required for activity Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61000
-
 4 * 61000, calculated from amino acid sequence Saccharomyces cerevisiae
284000
-
 gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate + CO2
-
 Saccharomyces cerevisiae ATP + oxaloacetate
-
 r
ATP + oxaloacetate
-
 Saccharomyces cerevisiae ADP + phosphoenolpyruvate + CO2
-
 ?
additional information PEP carboxykinase utilizes 2'-dADP and 2'-dATP as substrates with kinetic and equilibrium dissociation constants very similar to those of ADP and ATP, respectively Saccharomyces cerevisiae ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 61000, calculated from amino acid sequence Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
ATP, oxaloacetate carboxy-lyase (transphosphorylating)
-
 Saccharomyces cerevisiae
PEP carboxykinase
-
 Saccharomyces cerevisiae
PEPCK
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 ATP mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
13
-
 ADP mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
18
-
 ADP mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
32
-
 ATP mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
38
-
 ATP wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
62
-
 ADP wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
130
-
 ADP mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
180
-
 ATP mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
1200
-
 ATP mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
1300
-
 ATP wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C Saccharomyces cerevisiae
1800
-
 ADP mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
1800
-
 ADP wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae