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Literature summary for 5.3.2.2 extracted from

  • Annett, R.G.; Kosicki, G.W.
    Oxalacetate keto-enol tautomerase. Purification and characterization (1969), J. Biol. Chem., 244, 2059-2067.
    View publication on PubMed
Search for more literature for 5.3.2.2

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate
-
 Sus scrofa
acetoacetate
-
 Sus scrofa
citrate
-
 Sus scrofa
CuCl2
-
 Sus scrofa
Diethyloxaloacetate
-
 Sus scrofa
DL-malic acid
-
 Sus scrofa
HgCl2
-
 Sus scrofa
KCl
-
 Sus scrofa
Lactate
-
 Sus scrofa
LiCl
-
 Sus scrofa
malonate
-
 Sus scrofa
MgCl2
-
 Sus scrofa
NaCl
-
 Sus scrofa
PCMB
-
 Sus scrofa
pyruvate
-
 Sus scrofa
Urea
-
 Sus scrofa
ZnCl2
-
 Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.06
-
-
 Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
keto-Oxaloacetate
-
 Sus scrofa Enol-oxaloacetate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
 40% loss of activity after 10 min Sus scrofa

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5
-
 quick denaturation below Sus scrofa
4
-
 at pH 8 or pH 4 more stable than at values in between Sus scrofa
8
-
 at pH 8 or pH 4 more stable than at values in between Sus scrofa
8.5
-
 quick denaturation above Sus scrofa