Anthranilate synthase

Anthranilate Synthase 1i1q
One of many anthranilate synthase structures.
Identifiers
EC number 4.1.3.27
CAS number 9031-59-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, an anthranilate synthase (EC 4.1.3.27) is an enzyme that catalyzes the chemical reaction

chorismate + L-glutamine \rightleftharpoons anthranilate + pyruvate + L-glutamate 2

Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate.

Reaction

In enzymology, an anthranilate synthase (EC 4.1.3.27) is an enzyme that catalyzes the chemical reaction

chorismate + L-glutamine \rightleftharpoons anthranilate + pyruvate + L-glutamate
Chemical equation of reaction occurring in anthranilate synthase

Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate.

Structure and assembly

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.[1] The αβ dimers interact through the α subunits to form the complex.

Nomenclature

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.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1I1Q, 1I7Q, 1I7S, 1QDL, and 2I6Y.

References

  1. Poulsen, C; Bongaerts, RJ; Verpoorte, R (March 1993). "urification and characterization of anthranilate synthase from Catharanthus roseus". European journal of biochemistry 212 (2): 431–40. doi:10.1111/j.1432-1033.1993.tb17679.x. PMID 8444181.
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