Anthranilate synthase

In enzymology, an anthranilate synthase (EC 4.1.3.27) is an enzyme that catalyzes the chemical reaction In enzymology, an anthranilate synthase (EC 4.1.3.27) is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate. In enzymology, an anthranilate synthase (EC 4.1.3.27) is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate. The complex is made up of α and β subunits. Gel filtration experiments reveal that the complex occurs as an α2β2 tetramer under native conditions, and as an αβ dimer under high salt concentrations. The αβ dimers interact through the α subunits to form the complex. This enzyme belongs to the family of lyases, to be specific the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is chorismate pyruvate-lyase (amino-accepting; anthranilate-forming). Other names in common use include anthranilate synthetase, chorismate lyase, and chorismate pyruvate-lyase (amino-accepting). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system - general. As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1I1Q, 1I7Q, 1I7S, 1QDL, and 2I6Y.