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Literature summary for 4.1.1.12 extracted from

  • Wilson, E.M.; Kornberg, H.L.
    Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp. (1963), Biochem. J., 88, 578-587.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
2-oxoglutarate activates Achromobacter sp.
acetaldehyde activates Achromobacter sp.
Glyoxal activates Achromobacter sp.
glyoxylate activates Achromobacter sp.
oxalacetate activates Achromobacter sp.
pyruvate activates Achromobacter sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Achromobacter sp.

General Stability

General Stability Organism
rapid loss of activity in dilute solution Achromobacter sp.

Inhibitors

Inhibitors Comment Organism Structure
beta-Ala weak Achromobacter sp.
DL-beta-Methylaspartate
-
Achromobacter sp.
DL-erythro-beta-hydroxyaspartate
-
Achromobacter sp.
DL-threo-beta-hydroxyaspartate
-
Achromobacter sp.
L-Ala
-
Achromobacter sp.
Maleate
-
Achromobacter sp.
phosphate strong inhibition by phosphate buffers above pH 5.0 Achromobacter sp.
succinate
-
Achromobacter sp.
Tartrate weak Achromobacter sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
L-Asp
-
Achromobacter sp.

Organism

Organism UniProt Comment Textmining
Achromobacter sp.
-
-
-

Storage Stability

Storage Stability Organism
4°C, pH 7, stable in concentrated solution Achromobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Asp
-
Achromobacter sp. L-Ala + CO2
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5 6
-
Achromobacter sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
5
-
rapid loss of activity Achromobacter sp.
7
-
4°C, stable in concentrated solution Achromobacter sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate bound to the enzyme probably in a reduced form Achromobacter sp.