Phosphoribosylanthranilate isomerase

From Wikipedia, the free encyclopedia

In enzymology, a phosphoribosylanthranilate isomerase (EC 5.3.1.24) is an enzyme that catalyzes the chemical reaction

N-(5-phospho-beta-D-ribosyl)anthranilate $\rightleftharpoons$ 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate

Hence, this enzyme has one substrate, N-(5-phospho-beta-D-ribosyl)anthranilate, and one product, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.

This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. 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. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.

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 1DL3, 1LBM, 1NSJ, 1V5X, and 1VZW.

[edit] References

IUBMB entry for 5.3.1.24
BRENDA references for 5.3.1.24 (Recommended.)
PubMed references for 5.3.1.24
PubMed Central references for 5.3.1.24
Google Scholar references for 5.3.1.24
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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. PMID 16526091.