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Literature summary for 2.6.1.42 extracted from

  • Korpela, T.K.; Saarinen, R.
    Affinity chromatography of B6-vitamin-dependent enzymes: purification of pig-heart branched-chain amino acid transaminase (1985), J. Chromatogr., 318, 333-341.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol
-
Sus scrofa

General Stability

General Stability Organism
caproate protects the enzyme Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
pig, hog
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
specific activity 4660 units, 1 unit is defined as the change of absorbance units at 348 nm and 37° within 30 min Sus scrofa

Storage Stability

Storage Stability Organism
2°C, preparation concentrated by ultracentrifugation, enzyme retains 75% of its activity for 4 months Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information B6-vitamin-dependent enzyme Sus scrofa ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Sus scrofa