Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Robin, A.Y.; Cobessi, D.; Curien, G.; Robert-Genthon, M.; Ferrer, J.L.; Dumas, R.
    A new mode of dimerization of allosteric enzymes with ACT domains revealed by the crystal structure of the aspartate kinase from Cyanobacteria (2010), J. Mol. Biol., 399, 283-293.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 expressed in Escherichia coli Synechocystis sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.2.4 refined at 2.55 A resolution in complex with L-lysine and L-threonine Synechocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-lysine enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-lysine, the enzyme displays partial inhibition by L-threonine (50% residual activity at saturation with L-threonine) with a K0.5 value of 0.7 mM Synechocystis sp.
2.7.2.4 L-threonine enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-threonine, the enzyme is inhibited by Lys in a cooperative manner, but the inhibition requires very high concentrations of L-lysine Synechocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.4 140000
-
gel filtration, homodimer Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Synechocystis sp. P74569
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
Synechocystis sp. ADP + 4-phospho-L-aspartate
-
?

Subunits

EC Number Subunits Comment Organism
2.7.2.4 homodimer crystal structure, dimerization involves only the catalytic domain Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 AKbeta
-
Synechocystis sp.
2.7.2.4 AKsyn
-
Synechocystis sp.
2.7.2.4 aspartate kinase beta
-
Synechocystis sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 30
-
assay at Synechocystis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 8
-
assay at Synechocystis sp.