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Literature summary extracted from

  • Maheswaran, M.; Urbanke, C.; Forchhammer, K.
    Complex formation and catalytic activation by the PII signaling protein of N-acetyl-L-glutamate kinase from Synechococcus elongatus strain PCC 7942 (2004), J. Biol. Chem., 279, 55202-55210.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.2.8 ATP maximum activity at 10 mM Synechococcus elongatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.8 ADP inhibitor of complex formation with PII protein Synechococcus elongatus
2.7.2.8 arginine feedback inhibition Synechococcus elongatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.8 additional information
-
 additional information formation of complex between enzyme and signal transduction protein PII decreases Km-value by a factor of 10 and increases Vmax 4fold Synechococcus elongatus
2.7.2.8 2.7
-
 N-acetyl-L-glutamate pH 7.5, complex of enzyme and PII protein Synechococcus elongatus
2.7.2.8 27.4
-
 N-acetyl-L-glutamate pH 7.5, free enzyme Synechococcus elongatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.8 Mg2+ required, maximum activity above 20 mM Synechococcus elongatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.2.8 32000
-
 6 * 32000, calculated Synechococcus elongatus
2.7.2.8 180000
-
 sedimentation anaylsis Synechococcus elongatus

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.8 Synechococcus elongatus
-
 strain PCC 7942, recombinant protein with His6-tag
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.2.8 3.3
-
 pH 7.5, free enzyme Synechococcus elongatus
2.7.2.8 13.3
-
 pH 7.5, complex of enzyme and PII protein Synechococcus elongatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.8 ATP + N-acetyl-L-glutamate
-
 Synechococcus elongatus ADP + N-acetyl-L-glutamate 5-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.2.8 hexamer 6 * 32000, calculated Synechococcus elongatus
2.7.2.8 More enzyme hexamer forms a complex with PII signaling protein trimer Synechococcus elongatus
2.7.2.8 More in vivo complex of enzyme with signal transduction protein PII Synechococcus elongatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.8 7.5
-
 both free enzyme and complex with protein PII Synechococcus elongatus