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Literature summary for 2.7.2.4 extracted from

  • Biswas, C.; Paulus, H.
    Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. IV. Arrangement and function of the subunits (1973), J. Biol. Chem., 248, 2894-2900.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-lysine
-
Paenibacillus polymyxa
L-threonine
-
Paenibacillus polymyxa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE Paenibacillus polymyxa
43000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE 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
ATP + L-aspartate Paenibacillus polymyxa 63 / ATCC 25901
-
ADP + 4-phospho-L-aspartate
-
r

Organic Solvent Stability

Organic Solvent Comment Organism
urea enzyme is completely inactivated by 4 M Paenibacillus polymyxa

Organism

Organism UniProt Comment Textmining
Paenibacillus polymyxa
-
i.e. Paenibacillus polymyxa
-
Paenibacillus polymyxa 63 / ATCC 25901
-
i.e. Paenibacillus polymyxa
-

Purification (Commentary)

Purification (Comment) Organism
-
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
ATP + L-aspartate
-
Paenibacillus polymyxa 63 / ATCC 25901 ADP + 4-phospho-L-aspartate
-
r

Subunits

Subunits Comment Organism
tetramer 2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE Paenibacillus polymyxa