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Literature summary for 4.3.1.1 extracted from

  • La, I.J.; Kim, J.; Kim, J.R.; Kim, K.T.; Kim, J.S.; Yoon, M.Y.
    Activation changes of Hafnia alvei aspartase by acetic anhydride (2002), Bull. Korean Chem. Soc., 23, 1057-1061.
No PubMed abstract available
Search for more literature for 4.3.1.1

Activating Compound

Activating Compound Comment Organism Structure
Acetic anhydride activation up to 7.5fold, allosteric Hafnia alvei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.97
-
 aspartate 40°C, pH 7.85, acetylated enzyme Hafnia alvei
2.5
-
 aspartate 40°C, pH 7.85, native enzyme Hafnia alvei

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Km-value for acetylated enzyme: 2.1 mM, for native enzyme: 1.05 mM Hafnia alvei

Organism

Organism UniProt Comment Textmining
Hafnia alvei
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Hafnia alvei fumarate + NH3
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 acetylated enzyme Hafnia alvei
45
-
 native enzyme Hafnia alvei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
 acetylated enzyme Hafnia alvei
8.5
-
 native enzyme Hafnia alvei