View source for 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase

{{enzyme
| Name = Anthranilate Synthase 1i1q
[[File:Anthranilate Synthase 1i1q.png|thumb|right|One of many anthranilate synthase structures.]]
| EC_number = 4.1.3.27
| CAS_number = 9031-59-8
| IUBMB_EC_number = 4/1/3/27
| GO_code = 0004049
| image = 
| width = 
| caption = 
}}
In [[enzymology]], an '''anthranilate synthase''' ({{EC number|4.1.3.27}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:chorismate + L-glutamine <math>\rightleftharpoons</math> anthranilate + pyruvate + L-glutamate 2

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[chorismate]] and [[L-glutamine]], whereas its 3 [[product (chemistry)|products]] are [[anthranilate]], [[pyruvate]], and [[L-glutamate]].

==Function==

{{Empty section|date=November 2013}}

==Reaction==
In [[enzymology]], an '''anthranilate synthase''' ({{EC number|4.1.3.27}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
: chorismate + L-glutamine <math>\rightleftharpoons</math> anthranilate + pyruvate + L-glutamate
[[File:Reaction Paint.png|thumb|right|Chemical equation of reaction occurring in anthranilate synthase]]
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[chorismate]] and [[L-glutamine]], whereas its 3 [[product (chemistry)|products]] are [[anthranilate]], [[pyruvate]], and [[L-glutamate]].

==Homologs==

{{Empty section|date=November 2013}}

==Paralogs==

{{Empty section|date=November 2013}}

==Nomenclature==
This enzyme belongs to the family of [[lyase]]s, 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 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1I1Q}}, {{PDB link|1I7Q}}, {{PDB link|1I7S}}, {{PDB link|1QDL}}, and {{PDB link|2I6Y}}.

==Application==

{{Empty section|date=November 2013}}

==References==
{{reflist|1}}
* {{cite journal | author = Baker TI, Crawford IP | year = 1966 | title = Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli | journal = J. Biol. Chem.  | volume = 241 | pages = 5577&ndash;84  | pmid = 5333199 | issue = 23 }}
* {{cite journal | author = Creighton TE and Yanofsky C | year = 1970 | title = Chorismate to tryptophan (Escherichia coli) - Anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase | journal = Methods Enzymol.  | volume = 17A | pages = 365&ndash;380 }}
* {{cite journal | author = Kung CC, Huang WN, Huang YC, Yeh KC | year = 2006 | title = Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry | journal = Proteomics.  | volume = 6 | pages = 2746&ndash;58  | pmid = 16526091 | doi = 10.1002/pmic.200500108 | issue = 9 }}
* {{cite journal | author = Ito J, Yanofsky C | year = 1969 | title = Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits | journal = J. Bacteriol.  | volume = 97 | pages = 734&ndash;42  | pmid = 4886290 | issue = 2 | pmc = 249753 }}
* {{cite journal | author = Zalkin H, Kling D | year = 1968 | title = Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium | journal = Biochemistry.  | volume = 7 | pages = 3566&ndash;73  | pmid = 4878701 | doi = 10.1021/bi00850a034 | issue = 10 }}

[[Category:EC 4.1.3]]
[[Category:Enzymes of known structure]]
[[Category:Anthranilates]]


{{4.1-enzyme-stub}}