Literature summary for 2.3.1.1 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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

Crystallization (Comment)

Organism

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

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

Inhibitors

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

Organism

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

Subunits

Subunits	Comment	Organism
tetramer	crystallization data	Homo sapiens
tetramer	crystallization data	Maricaulis maris

Synonyms

Synonyms	Comment	Organism
NAGS/K	-	Homo sapiens
NAGS/K	-	Maricaulis maris

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Release 2023.1 (January 2023)