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Literature summary for 4.1.1.49 extracted from

  • Andrade, C.; Sepulveda, C.; Cardemil, E.; Jabalquinto, A.M.
    The role of tyrosine 207 in the reaction catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase (2010), Biol. Res., 43, 191-195.
    View publication on PubMed
Search for more literature for 4.1.1.49

Cloned(Commentary)

Cloned (Comment) Organism
mutant enzyme Y207L is expressed in the PEP carboxykinase-deficient Saccharomyces cerevisiae strain PUK-3B Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 ADP mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.016
-
 ADP wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
0.5
-
 phosphoenolpyruvate mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
2
-
 CO2 wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
3
-
 phosphoenolpyruvate wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae
29
-
 CO2 mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity Saccharomyces cerevisiae
Mn2+ the enzyme possesses one binding site for Mn2+ per enzyme monomer Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
251000
-
 Superose-12 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
-
 r

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Saccharomyces cerevisiae