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Literature summary for 1.1.1.39 extracted from

  • Sato, I.; Yoshikawa, J.; Furusawa, A.; Chiku, K.; Amachi, S.; Fujii, T.
    Isolation and properties of malic enzyme and its gene in Rhodopseudomonas palustris No. 7 (2010), Biosci. Biotechnol. Biochem., 74, 75-81.
    View publication on PubMed
Search for more literature for 1.1.1.39

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109 Rhodopseudomonas palustris

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA enzyme activity is allosterically regulated by acetyl-CoA, almost complete inhibition at 0.05 mM Rhodopseudomonas palustris
Ca2+ inhibits 30% at 1 mM and 60% at 10 mM Rhodopseudomonas palustris
EDTA complete inhibition at 0.1 mM Rhodopseudomonas palustris
fructose 6-phosphate competitive versus (S)-malate, 70% inhibition at 2.5 mM Rhodopseudomonas palustris
Li+ slight inhibition Rhodopseudomonas palustris
Na+ complete inhibition at 10 mM, no effect by Na+ at 1 mM Rhodopseudomonas palustris
oxaloacetate competitive versus (S)-malate, 20% inhibition at 2.5 mM Rhodopseudomonas palustris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics, overview Rhodopseudomonas palustris
0.11
-
 NAD+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris
1.7
-
 (S)-malate pH 7.2, 30°C, with NAD+ Rhodopseudomonas palustris
1.8
-
 NADP+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris
15
-
 (S)-malate pH 7.2, 30°C, with NADP+ Rhodopseudomonas palustris

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates 7fold at 1-10 mM Rhodopseudomonas palustris
Mg2+ activates 12fold at 1 mM and 15fold at 10 mM Rhodopseudomonas palustris
Mn2+ activates 13fold at 1 mM and 15fold at 10 mM Rhodopseudomonas palustris
additional information malic enzyme activity is markedly enhanced by mono- and divalent cations Rhodopseudomonas palustris
NH4+ activates 12fold at 1 mM and 20fold at 10 mM Rhodopseudomonas palustris
Zn2+ 5fold activation at 5 mM, only slight activation at 10 mM Rhodopseudomonas palustris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
86000
-
 x * 86000 Rhodopseudomonas palustris
650000
-
-
 Rhodopseudomonas palustris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Rhodopseudomonas palustris
-
 pyruvate + NADH + H+ + CO2
-
 ?
(S)-malate + NAD+ Rhodopseudomonas palustris No. 7
-
 pyruvate + NADH + H+ + CO2
-
 ?
(S)-malate + NADP+ Rhodopseudomonas palustris NADP+ shows 22% of the activity with NAD+ pyruvate + NADPH + H+ + CO2
-
 ?
(S)-malate + NADP+ Rhodopseudomonas palustris No. 7 NADP+ shows 22% of the activity with NAD+ pyruvate + NADPH + H+ + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodopseudomonas palustris A4F2S6
-
-
Rhodopseudomonas palustris No. 7 A4F2S6
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 1500fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, adsorption chromatography, ultrafiltration, and gel filtration Rhodopseudomonas palustris

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
64
-
 purified enzyme, pH 7.2, 30°C Rhodopseudomonas palustris

Storage Stability

Storage Stability Organism
-80°C, purified native enzyme, 8 months, completely stable Rhodopseudomonas palustris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Rhodopseudomonas palustris pyruvate + NADH + H+ + CO2
-
 ?
(S)-malate + NAD+
-
 Rhodopseudomonas palustris No. 7 pyruvate + NADH + H+ + CO2
-
 ?
(S)-malate + NADP+ NADP+ shows 22% of the activity with NAD+ Rhodopseudomonas palustris pyruvate + NADPH + H+ + CO2
-
 ?
(S)-malate + NADP+ NADP+ shows 22% of the activity with NAD+ Rhodopseudomonas palustris No. 7 pyruvate + NADPH + H+ + CO2
-
 ?
additional information the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate Rhodopseudomonas palustris ?
-
 ?
additional information the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate Rhodopseudomonas palustris No. 7 ?
-
 ?

Subunits

Subunits Comment Organism
oligomer x * 86000 Rhodopseudomonas palustris

Synonyms

Synonyms Comment Organism
malic enzyme
-
 Rhodopseudomonas palustris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Rhodopseudomonas palustris

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 purified enzyme, stable up to, loss of activity above Rhodopseudomonas palustris
70
-
 purified enzyme, almost complete inactivation Rhodopseudomonas palustris

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
480
-
 (S)-malate pH 7.2, 30°C, with NADP+ Rhodopseudomonas palustris
520
-
 NADP+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris
720
-
 NAD+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris
770
-
 (S)-malate pH 7.2, 30°C, with NAD+ Rhodopseudomonas palustris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Rhodopseudomonas palustris

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
 purified enzyme, most stable at Rhodopseudomonas palustris

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme uses both NAD+ and NADP+ Rhodopseudomonas palustris
NAD+ preferred cofactor Rhodopseudomonas palustris
NADP+
-
 Rhodopseudomonas palustris

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.36
-
 oxaloacetate pH 7.2, 30°C, versus (S)-malate Rhodopseudomonas palustris
7.4
-
 fructose 6-phosphate pH 7.2, 30°C, versus (S)-malate Rhodopseudomonas palustris

pI Value

Organism Comment pI Value Maximum pI Value
Rhodopseudomonas palustris sequence calculation
-
 6.3

General Information

General Information Comment Organism
additional information enzyme activity is allosterically regulated by acetyl-CoA Rhodopseudomonas palustris
physiological function malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview Rhodopseudomonas palustris

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2900
-
 NADP+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris
3100
-
 (S)-malate pH 7.2, 30°C, with NAD+ Rhodopseudomonas palustris
3300
-
 (S)-malate pH 7.2, 30°C, with NADP+ Rhodopseudomonas palustris
6900
-
 NAD+ pH 7.2, 30°C, with (S)-malate Rhodopseudomonas palustris