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

BRENDA support

Literature summary extracted from

  • Shi, D.; Li, Y.; Cabrera-Luque, J.; Jin, Z.; Yu, X.; Zhao, G.; Haskins, N.; Allewell, N.M.; Tuchman, M.
    A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris (2011), PLoS ONE, 6, e28825.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.2.8 L-arginine slight activation is observed at 1 mM L-arginine Maricaulis maris

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.8 expressed in Escherichia coli as a His-tagged fusion protein Maricaulis maris

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.1 development of a structural model of human enzyme that is fully consistent with the functional effects of the 14 missense mutations that have been identified in N-acetylglutamate synthase-deficient patients Homo sapiens
2.3.1.1 to 2.7 A resolution. Enzyme is a tetramer. Each subunit has an amino acid kinase domain, which is likely responsible for N-acetylglutamate kinase activity and has a putative arginine binding site, and an N-acetyltransferase domain that contains the putative N-acetylglutamate synthase active site. The angle of rotation between amino acid kinase and N-acetyltransferase domains varies among crystal forms and subunits within the tetramer. A rotation of 26° is sufficient to close the predicted AcCoA binding site, thus reducing enzymatic activity Maricaulis maris
2.7.2.8 crystal structure of Maricaulis maris NAGS/K (mmNAGS/K) at 2.7 A resolution shows that it is a tetramer Maricaulis maris

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.8 I106M to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A Maricaulis maris
2.7.2.8 I294M to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A Maricaulis maris
2.7.2.8 L367M to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A Maricaulis maris

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.1 L-arginine allosteric inhibition Homo sapiens
2.3.1.1 L-arginine allosteric inhibition Maricaulis maris

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.1 Homo sapiens
-
 bifunctional N-acetylglutamate synthase/kinase
-
2.3.1.1 Maricaulis maris Q0ASS9 bifunctional N-acetylglutamate synthase/kinase
-
2.7.2.8 Maricaulis maris
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.8 using Ni-NTA chromatography Maricaulis maris

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 20.1
-
 pH 7.4, 37°C Maricaulis maris

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.3.1.1 tetramer crystallization data Homo sapiens
2.3.1.1 tetramer crystallization data Maricaulis maris
2.7.2.8 tetramer crystal structure Maricaulis maris

Synonyms

EC Number Synonyms Comment Organism
2.3.1.1 NAGS/K
-
 Homo sapiens
2.3.1.1 NAGS/K
-
 Maricaulis maris
2.7.2.8 NAGS-K enzyme has both N-acetylglutamate synthase and kinases activity Maricaulis maris