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Literature summary for 2.3.1.101 extracted from

  • Shima, S.; Thauer, R.K.; Ermler, U.
    Hyperthermophilic and salt-dependent formyltransferase from Methanopyrus kandleri (2004), Biochem. Soc. Trans., 32, 269-272.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
potassium cyclic 2,3-diphosphoglycerate required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations Methanopyrus kandleri

General Stability

General Stability Organism
potassium cyclic 2,3-diphosphoglycerate and potassium phosphate stabilize the enzyme Methanopyrus kandleri

Metals/Ions

Metals/Ions Comment Organism Structure
K+ potassium cyclic 2,3-diphosphoglycerate required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations Methanopyrus kandleri
potassium phosphate required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by potassium cyclic 2,3-diphosphoglycerate, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations Methanopyrus kandleri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M Methanopyrus kandleri
32000
-
4 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.5 M Methanopyrus kandleri

Organism

Organism UniProt Comment Textmining
Methanopyrus kandleri
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information the hyperthermophilic methanogenic archaeon grows on H2 and CO2 as sole energy source best at 98°C Methanopyrus kandleri
-

Subunits

Subunits Comment Organism
dimer 2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M Methanopyrus kandleri
More structure analysis, at low salt conditions the enzyme is in an equilibrium of dimer, trimer and tetramer, the latter being the active and most thermostable enzyme form, the dimer is also active, but the monomer is inactive Methanopyrus kandleri
tetramer 4 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.5 M Methanopyrus kandleri

Synonyms

Synonyms Comment Organism
formyltransferase
-
Methanopyrus kandleri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the enzyme is thermostable Methanopyrus kandleri
90
-
30 min, wild-type enzyme, loss of 70% activity at 0.8-1.0 M potassium phosphate Methanopyrus kandleri