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Literature summary for 2.7.2.4 extracted from

  • Paulus, H.; Gray, E.
    Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies (1967), J. Biol. Chem., 242, 4980-4986.
    View publication on PubMed
Search for more literature for 2.7.2.4

Inhibitors

Inhibitors Comment Organism Structure
ADP competitive inhibition Paenibacillus polymyxa
L-lysine
-
 Paenibacillus polymyxa
L-threonine
-
 Paenibacillus polymyxa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information at 37°C, but not at 25°C, the apparent Km for L-aspartate is highly dependent on enzyme concentration, increasing from 0.4 mM to about 50 mM. As the enzyme concentration decreases from 13.4 to 0.17 units per ml, the presence of dioxane increases apparent Km for L-aspartate Paenibacillus polymyxa
1
-
 ATP pH 8.0, 37°C Paenibacillus polymyxa
1.5
-
 L-aspartate pH 8.0, 25°C Paenibacillus polymyxa

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Paenibacillus polymyxa
Mg2+
-
 Paenibacillus polymyxa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate Paenibacillus polymyxa
-
 ADP + 4-phospho-L-aspartate
-
 r

Organism

Organism UniProt Comment Textmining
Paenibacillus polymyxa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partially Paenibacillus polymyxa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
22.2
-
-
 Paenibacillus polymyxa

Storage Stability

Storage Stability Organism
-15°C, diluted with glycerol to a final concentration of 40%, no loss of enzyme activity observed over a period of more than 1 year Paenibacillus polymyxa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Paenibacillus polymyxa ADP + 4-phospho-L-aspartate
-
 r
additional information aspartate analogues succinate, maleate, L-glutamate and DL-2-amino-3-phosphonopropionate have no influence on the reaction Paenibacillus polymyxa ?
-
 ?

Subunits

Subunits Comment Organism
More at 37°C, but not at 25°C, the active form of aspartokinase dissociates into lower molecular weight units which have markedly lower affinity for L-aspartate than the native enzyme Paenibacillus polymyxa