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Literature summary extracted from

  • Harmon, F.R.; Goss, N.H.; Wood, H.G.
    Stabilization of the quaternary structure of transcarboxylase by cobalt (II) ions (1982), Biochemistry, 21, 2847-2852.
    View publication on PubMed

General Stability

EC Number General Stability Organism
2.1.3.1 Co2+ protects Propionibacterium freudenreichii subsp. shermanii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.3.1 Guanidinium chloride Co2+ protects Propionibacterium freudenreichii subsp. shermanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.3.1 Co2+ requirement Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 Co2+ 3 types of Co2+: tightly i.e. catalytic, not so tightly, and weakly bound, above 2 mM, stabilizes quarternary structure, no exchange between catalytic and stabilizing Co2+ Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 Co2+ no formation of Co-thiol bonds Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 Zn2+ slightly stabilizing Propionibacterium freudenreichii subsp. shermanii

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.1 Propionibacterium freudenreichii subsp. shermanii
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.1.3.1 oxygen prevents reassembly of dissociated subunits Propionibacterium freudenreichii subsp. shermanii

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.3.1 (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate mechanism Propionibacterium freudenreichii subsp. shermanii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.3.1 33.6
-
-
 Propionibacterium freudenreichii subsp. shermanii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.3.1 25
-
 assay at Propionibacterium freudenreichii subsp. shermanii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.3.1 25
-
 dissociation and rapid loss of activity in dilute solution in alkaline 50 mM buffer (t1/2: 12 min), Co2+ protects, Zn2+ protects slightly (t1/2: 22 min) Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 50
-
 denaturation within 1 min, Co2+ protects, Zn2+ protects slightly Propionibacterium freudenreichii subsp. shermanii

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.1.3.1 5.5
-
 26S-form stable Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 8
-
 dilute solution, 50 mM buffer, 25°C: enzyme dissociates into subunits and rapidly loses activity, Co2+ protects, Zn2+ protects slightly Propionibacterium freudenreichii subsp. shermanii
2.1.3.1 9
-
 enzyme dissociates into 12SH, 5SE, 6SE and 6SH subunits, in the presence of Co2+: the 6SE subunits binds to 12SH subunit Propionibacterium freudenreichii subsp. shermanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.3.1 biotin requirement Propionibacterium freudenreichii subsp. shermanii