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Literature summary for 6.3.4.9 extracted from

  • Shenoy, B.C.; Wood, H.G.
    Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii (1988), FASEB J., 2, 2396-2401.
    View publication on PubMed

General Stability

General Stability Organism
divalent metal is required for storage stability, Mg2+, Mn2+, Co2+, Zn2+, or Ni2+ Propionibacterium freudenreichii subsp. shermanii
loses activity by repeated freezing and thawing Propionibacterium freudenreichii subsp. shermanii

Inhibitors

Inhibitors Comment Organism Structure
Co2+ activates, inhibition at high concentrations Propionibacterium freudenreichii subsp. shermanii
Cu2+
-
Propionibacterium freudenreichii subsp. shermanii
EDTA
-
Propionibacterium freudenreichii subsp. shermanii
Hg2+
-
Propionibacterium freudenreichii subsp. shermanii
Zn2+ activates, inhibition at high concentrations Propionibacterium freudenreichii subsp. shermanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0009
-
1.3 S subunit of apotranscarboxylase
-
Propionibacterium freudenreichii subsp. shermanii
0.038
-
ATP
-
Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0017 mM Propionibacterium freudenreichii subsp. shermanii
Mg2+ divalent metal ion required Propionibacterium freudenreichii subsp. shermanii
Mg2+ affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+ Propionibacterium freudenreichii subsp. shermanii
Mg2+ Km: 0.0019 mM Propionibacterium freudenreichii subsp. shermanii
Mn2+ affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+ Propionibacterium freudenreichii subsp. shermanii
Mn2+ Km: 0.0015 mM Propionibacterium freudenreichii subsp. shermanii
Ni2+ affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0013 mM Propionibacterium freudenreichii subsp. shermanii
Zn2+ affinity of the enzyme towards metal in decreasing order: Zn2+, Ni2+, Mn2+, Co2+, Mg2+, Km: 0.0003 mM Propionibacterium freudenreichii subsp. shermanii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
gel filtration Propionibacterium freudenreichii subsp. shermanii

Organism

Organism UniProt Comment Textmining
Propionibacterium freudenreichii subsp. shermanii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Propionibacterium freudenreichii subsp. shermanii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0124
-
-
Propionibacterium freudenreichii subsp. shermanii

Storage Stability

Storage Stability Organism
-20°C, stable for 6 months Propionibacterium freudenreichii subsp. shermanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + 1.3 S subunit of apotranscarboxylase
-
Propionibacterium freudenreichii subsp. shermanii ?
-
?
ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxyltransferase]
-
Propionibacterium freudenreichii subsp. shermanii AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxyltransferase]
-
?

Subunits

Subunits Comment Organism
monomer 1 * 30000, SDS-PAGE Propionibacterium freudenreichii subsp. shermanii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Propionibacterium freudenreichii subsp. shermanii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60 about 30% of maximal activity at 20°C and 60°C Propionibacterium freudenreichii subsp. shermanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Propionibacterium freudenreichii subsp. shermanii