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Literature summary for 1.2.7.1 extracted from

  • Takenaka, M.; Yoon, K.S.; Matsumoto, T.; Ogo, S.
    Acetyl-CoA production by encapsulated pyruvate ferredoxin oxidoreductase in alginate hydrogels (2017), Biores. Technol., 227, 279-285.
    View publication on PubMed

General Stability

General Stability Organism
the operational stability of the enzyme in alginate hydrogels retains over 68% initial activity after 10 repeated cycles Citrobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
CoA free enzyme, at pH 7.0 and 30°C Citrobacter sp.
0.12
-
pyruvate free enzyme, at pH 7.0 and 30°C Citrobacter sp.
0.37
-
pyruvate enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.
0.54
-
CoA enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 2 mM used in assay conditions Citrobacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
2 * 120000, SDS-PAGE Citrobacter sp.
240000
-
gel filtration Citrobacter sp.

Organism

Organism UniProt Comment Textmining
Citrobacter sp.
-
-
-

Oxidation Stability

Oxidation Stability Organism
the enzyme shows high O2-sensitivity Citrobacter sp.

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration Citrobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is incapable of using NAD+ and NADP+ as electron acceptors Citrobacter sp. ?
-
?
pyruvate + CoA + oxidized methyl viologen
-
Citrobacter sp. acetyl-CoA + CO2 + reduced methyl viologen + H+
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 120000, SDS-PAGE Citrobacter sp.

Synonyms

Synonyms Comment Organism
PFOR
-
Citrobacter sp.
pyruvate ferredoxin oxidoreductase
-
Citrobacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Citrobacter sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50 the enzyme retains more than 60% of the initial activity 30-50°C, even after 30 min incubation Citrobacter sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
35
-
pyruvate enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.
39
-
CoA enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.
94
-
pyruvate free enzyme, at pH 7.0 and 30°C Citrobacter sp.
109
-
CoA free enzyme, at pH 7.0 and 30°C Citrobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Citrobacter sp.

pH Range

pH Minimum pH Maximum Comment Organism
6 8 the enzyme retains more than 70% of the initial activity at pH 6.0-8.0, even after 30 min incubation Citrobacter sp.

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Citrobacter sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
72
-
CoA enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.
95
-
pyruvate enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C Citrobacter sp.
780
-
pyruvate free enzyme, at pH 7.0 and 30°C Citrobacter sp.
3900
-
CoA free enzyme, at pH 7.0 and 30°C Citrobacter sp.