Indole-3-glycerol-phosphate synthase

From Wikipedia, the free encyclopedia

In enzymology, an indole-3-glycerol-phosphate synthase (EC 4.1.1.48) is an enzyme that catalyzes the chemical reaction

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate $\rightleftharpoons$ 1-C-(indol-3-yl)-glycerol 3-phosphate + CO₂ + H₂O

Hence, this enzyme has one substrate, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate, but 3 products: 1-C-(indol-3-yl)-glycerol 3-phosphate, CO₂, and H₂O.

This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing 1-C-(indol-3-yl)glycerol-3-phosphate-forming]. Other names in common use include indoleglycerol phosphate synthetase, indoleglycerol phosphate synthase, indole-3-glycerophosphate synthase, 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, and carboxy-lyase (cyclizing). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and two-component system - general. It employs one cofactor, pyruvate.

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

[edit] Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1A53, 1I4N, 1J5T, 1JCM, 1JUK, 1JUL, 1LBF, 1LBL, 1PII, 1VC4, and 2C3Z.

[edit] References

IUBMB entry for 4.1.1.48
BRENDA references for 4.1.1.48 (Recommended.)
PubMed references for 4.1.1.48
PubMed Central references for 4.1.1.48
Google Scholar references for 4.1.1.48
Creighton TE, Yanofsky C (1966). "Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon". J. Biol. Chem. 241: 4616–24. PMID 5332729.
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.