Anthranilate synthase

From Wikipedia, the free encyclopedia

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

chorismate + L-glutamine anthranilate + pyruvate + L-glutamate

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

This enzyme belongs to the family of lyases, specifically 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.

Contents 1 Structural studies 2 References 3 External links 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

• IUBMB entry for 4.1.3.27
• BRENDA references for 4.1.3.27 (Recommended.)
• PubMed references for 4.1.3.27
• PubMed Central references for 4.1.3.27
• Google Scholar references for 4.1.3.27
• Baker TI, Crawford IP (1966). "Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli". J. Biol. Chem. 241: 5577–84. PMID 5333199. 
• Creighton TE and Yanofsky C (1970). "Chorismate to tryptophan (Escherichia coli) - Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase". Methods Enzymol. 17A: 365–380. 
• Kung CC, Huang WN, Huang YC, Yeh KC (2006). "Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry". Proteomics. 6: 2746–58. doi:10.1002/pmic.200500108. PMID 16526091. 
• Ito J, Yanofsky C (1969). "Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits". J. Bacteriol. 97: 734–42. PMID 4886290. 
• Zalkin H, Kling D (1968). "Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium". Biochemistry. 7: 3566–73. doi:10.1021/bi00850a034. PMID 4878701. 

[edit] External links

The CAS registry number for this enzyme class is 9031-59-8.

• IUBMB entry for 4.1.3.27

• KEGG entry for 4.1.3.27

• BRENDA entry for 4.1.3.27

• NiceZyme view of 4.1.3.27

• EC2PDB: PDB structures for 4.1.3.27

• PRIAM entry for 4.1.3.27

• PUMA2 entry for 4.1.3.27

• IntEnz: Integrated Enzyme entry for 4.1.3.27

• MetaCyc entry for 4.1.3.27

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0004049: anthranilate synthase

• AMIGO entry for GO code 0004049: anthranilate synthase