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Literature summary for 4.1.1.112 extracted from

  • Sender, P.D.; Martin, M.G.; Peiru, S.; Magni, C.
    Characterization of an oxaloacetate decarboxylase that belongs to the malic enzyme family (2004), FEBS Lett., 570, 217-222.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli M15 Lactococcus lactis

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate 2 mM inhibitor in presence of 10 mM Mn2+, 11% inhibition Lactococcus lactis
Ca2+ 2 mM inhibitor in presence of 1 mM Mn2+, 30% inhibition Lactococcus lactis
citrate 0.5 mM inhibitor or 2 mM inhibitor in presence of 10 mM Mn2+, 24% inhibition Lactococcus lactis
Cu2+ 0.5 mM inhibitor in presence of 1 mM Mn2+, complete inhibition Lactococcus lactis
EDTA 10 mM, complete inhibition Lactococcus lactis
fumarate 2 mM inhibitor in presence of 10 mM Mn2+, 21% inhibition Lactococcus lactis
malate 2 mM inhibitor in presence of 10 mM Mn2+, 54% inhibition Lactococcus lactis
malonate 0.5 mM inhibitor in presence of 10 mM Mn2+, 84% inhibition Lactococcus lactis
NAD+ 2 mM inhibitor in presence of 10 mM Mn2+, complete inhibition Lactococcus lactis
NADH 2 mM inhibitor in presence of 10 mM Mn2+, complete inhibition Lactococcus lactis
Ni2+ 2 mM inhibitor in presence of 1 mM Mn2+, 40% inhibition Lactococcus lactis
oxalate 0.5 mM inhibitor in presence of 10 mM Mn2+, 80% inhibition Lactococcus lactis
pyruvate 2 mM inhibitor in presence of 10 mM Mn2+, 8% inhibition Lactococcus lactis
succinate 2 mM inhibitor in presence of 10 mM Mn2+, 23% inhibition Lactococcus lactis
Zn2+ 0.5 mM inhibitor in presence of 1 mM Mn2+, complete inhibition Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.52
-
oxaloacetate
-
Lactococcus lactis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Lactococcus lactis
Mn2+ dependent on, maximal activity in presence of 10 mM Mn2+ Lactococcus lactis
Ni2+ activates Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
CRL264
-
Lactococcus lactis CRL264
-
CRL264
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Lactococcus lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Oxaloacetate
-
Lactococcus lactis Pyruvate + CO2
-
ir
Oxaloacetate
-
Lactococcus lactis CRL264 Pyruvate + CO2
-
ir

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Lactococcus lactis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
58
-
no activity above Lactococcus lactis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5
-
oxaloacetate
-
Lactococcus lactis
20.26
-
oxaloacetate
-
Lactococcus lactis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.4
-
-
Lactococcus lactis

pH Range

pH Minimum pH Maximum Comment Organism
3.5 5.5 pH 3.5: about 55% of maximal activity, pH 5.5: about 40% of maximal activity Lactococcus lactis