Anthranilate Synthase 1i1q
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| Identifiers | |||||||||
| EC no. | 4.1.3.27 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
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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 2
Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its 3 products are anthranilate, pyruvate, and L-glutamate.
Function
edit![[icon]](/wiki/File:Wiki_letter_w_cropped.svg){kind=small} | This section is empty. You can help by adding to it. (November 2013) |
Reaction
editIn 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.
Homologs
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Paralogs
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Nomenclature
editThis 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
editAs of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1I1Q, 1I7Q, 1I7S, 1QDL, and 2I6Y.
Application
edit| | This section is empty. You can help by adding to it. (November 2013) |
References
edit- Baker TI, Crawford IP (1966). "Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli". J. Biol. Chem. 241 (23): 5577–84. doi:10.1016/S0021-9258(18)96383-0. 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. Vol. 17A. pp. 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 (9): 2746–58. doi:10.1002/pmic.200500108. PMID 16526091.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - 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 (2): 734–42. doi:10.1128/jb.97.2.734-742.1969. PMC 249753. PMID 4886290.
- Zalkin H, Kling D (1968). "Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium". Biochemistry. 7 (10): 3566–73. doi:10.1021/bi00850a034. PMID 4878701.
Category:EC 4.1.3 Category:Enzymes of known structure Category:Anthranilates
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