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Literature summary for 2.3.1.1 extracted from

  • Shi, D.; Sagar, V.; Jin, Z.; Yu, X.; Caldovic, L.; Morizono, H.; Allewell, N.M.; Tuchman, M.
    The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation (2008), J. Biol. Chem., 283, 7176-7184.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 Neisseria gonorrhoeae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop method Neisseria gonorrhoeae

Protein Variants

Protein Variants Comment Organism
D336N point mutation Neisseria gonorrhoeae
P427S point mutation Neisseria gonorrhoeae
V312I point mutation Neisseria gonorrhoeae

Organism

Organism UniProt Comment Textmining
Neisseria gonorrhoeae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel affinity and DEAE columns Neisseria gonorrhoeae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
29.1
-
-
 Neisseria gonorrhoeae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-glutamate assay at pH 8.5, 30°C, 5 min Neisseria gonorrhoeae N-acetyl-L-glutamate + CoA
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Neisseria gonorrhoeae

Synonyms

Synonyms Comment Organism
N-acetyl-L-glutamate synthase
-
 Neisseria gonorrhoeae
NAGS
-
 Neisseria gonorrhoeae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Neisseria gonorrhoeae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Neisseria gonorrhoeae