Oxaloacetate tautomerase: Difference between revisions

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{{enzyme
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| Name = phosphoribosylanthranilate isomerase
| EC_number = 5.3.1.24
| CAS_number = 37259-82-8
| IUBMB_EC_number = 5/3/1/24
| GO_code = 0004640
| image = Phosphoribosylanthranilate isomerase Structure.png
| width =
| caption = 3D rendering of Phosophoribosylanthranilate Isomerase
}}
{{Infobox protein family
| Symbol = PRAI
| Name = PRAI
| image = PDB 1dl3 EBI.jpg
| width =
| caption = crystal structure of mutually generated monomers of dimeric phosphoribosylantranilate isomerase from ''[[Thermotoga maritima]]''
| Pfam = PF00697
| Pfam_clan = CL0036
| InterPro = IPR001240
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1pii
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
 
In [[enzymology]], a '''phosphoribosylanthranilate isomerase''' ({{EC number|5.3.1.24}}) is an [[enzyme]] that [[catalysis|catalyzes]] the third step of the [[Tryptophan biosynthesis|synthesis of the amino acid tryptophan.]]<ref>{{cite journal | author = Creighton TE, Yanofsky C | date = 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 }}</ref>
 
This enzyme participates in the [[phenylalanine]], [[tyrosine]] and [[tryptophan]] [[biosynthesis]] pathway, also known as the [[Aromatic amino-acid|aromatic amino acid]] biosynthesis pathway 
 
In yeast it is encoded by the ''TRP1'' gene.<ref>{{cite web |url=http://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002414 |title=TRP1/YDR007W Summary |work= Saccharomyces genome database |publisher=Stanford University }}</ref>
 
==Reaction==
 
:N-(5-phospho-beta-D-ribosyl)anthranilate <math>\rightleftharpoons</math> 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
[[File:Phosphoribosylanthranilate isomerase.jpg|thumbnail|center|Phosphoribosylanthranilate isomerase Reaction]]
 
In other words, this enzyme has one [[substrate (biochemistry)|substrate]], N-(5-phospho-beta-D-ribosyl)anthranilate, and one [[product (chemistry)|product]], 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. As the name phosphoribosylanthranilate '''isomerase''' suggests, it functions as an [[isomerase]], rearranging the parts of the molecule without adding or removing molecules or atoms
 
== [[Nomenclature]] ==
 
This enzyme belongs to the family of [[isomerase]]s, specifically those intramolecular [[oxidoreductase]]s interconverting [[aldose]]s and [[ketose]]s.  The systematic name of this enzyme class is N-(5-phospho-beta-D-ribosyl)anthranilate aldose-ketose-isomerase. Other names in common use include:
* PRA isomerase,
* PRAI,
* IGPS:PRAI (indole-3-glycerol-phosphate,
* synthetase/N-5'-phosphoribosylanthranilate isomerase complex), and
* N-(5-phospho-beta-D-ribosyl)anthranilate ketol-isomerase.  
 
== Structure ==
 
Phosphoribosylanthranilate isomerase (PRAI) is [[monomeric]] and [[labile]] in most [[mesophilic]] microorganisms, but [[protein dimer|dimeric]] and stable in the [[hyperthermophile]] ''[[Thermotoga maritima]]'' (tPRAI).<ref name="pmid10745009">{{cite journal | author = Thoma R, Hennig M, Sterner R, Kirschner K | title = Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima | journal = Structure | volume = 8 | issue = 3 | pages = 265–76 |date=March 2000 | pmid = 10745009 | doi = | url = }}</ref> The comparison to the known 2.0 A [[secondary structure|structure]] of PRAI from ''Escherichia coli'' (ePRAI) shows that tPRAI has a [[TIM barrel|TIM-barrel]] fold, whereas helix alpha5 in ePRAI is replaced by a [[turn (biochemistry)|loop]]. The [[protein subunit|subunits]] of tPRAI associate via the N-terminal faces of their central [[beta-barrel]]s. Two long, symmetry-related [[loop (biochemistry)|loops]] that protrude reciprocally into cavities of the other subunit provide for multiple [[hydrophobic]] interactions. Moreover, the [[side chains]] of the N-terminal [[methionine]]s and the C-terminal [[leucines]] of both [[Protein subunit|subunits]] are immobilized in a [[Hydrophobe|hydrophobic]] cluster, and the number of [[salt]] bridges is increased in tPRAI. These features appear to be mainly responsible for the high [[thermostability]] of tPRAI.<ref name="pmid9166771">{{cite journal | author = Hennig M, Sterner R, Kirschner K, Jansonius JN | title = Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability | journal = Biochemistry | volume = 36 | issue = 20 | pages = 6009–16 |date=May 1997 | pmid = 9166771 | doi = 10.1021/bi962718q | url = }}</ref>
 
==[[Homologous]] Genes==
This enzyme is found in plant species such as [[Arabidopsis thaliana|''Arabidopsis thaliana'']] and [[Oryza sativa|''Oryza sativa'']] (Asian Rice). One form of bacterium it is found in [[Thermotoga maritima]].
 
Phosphoribosylanthranilate isomerase is also found in various forms of fungi such as [[Kluyveromyces lactis|''Kluyveromyces lactis'']]'' ''(yeast), [[Saccharomyces cerevisiae|''Saccharomyces cerevisiae'']] (yeast), and [[Ashbya gossypii|''Ashbya gossypii'']]. <ref>HomoloGene Database. National Center for Biotechnology Information. Blast search for phosphoribosylanthranilate isomerase. http://www.ncbi.nlm.nih.gov/homologene/?term=phosphoribosylanthranilate%20isomerase</ref>
 
==References==
{{reflist}}
 
== Further reading ==
{{refbegin}}
* {{cite journal | author = Braus GH, Luger K, Paravicini G, Schmidheini T, Kirschner K, Hütter R | title = The role of the TRP1 gene in yeast tryptophan biosynthesis | journal = J. Biol. Chem. | volume = 263 | issue = 16 | pages = 7868–75 |date=June 1988 | pmid = 3286643 | doi = }}
{{refend}}
 
{{InterPro content|IPR001240}}[[Category:EC 5.3.1]]
[[Category:Enzymes of known structure]]
[[Category:Protein domains]]

Latest revision as of 20:44, 19 December 2014

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