Aminodeoxychorismate lyase
4-amino-4-deoxychorismate lyase (EC 4.1.3.38) is an enzyme that participates in folate biosynthesis by catalyzing the production of PABA by the following reaction
- 4-amino-4-deoxychorismate 4-aminobenzoate + pyruvate
| 4-amino-4-deoxychorismate lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.1.3.38 | ||||||||
| 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 | ||||||||
| |||||||||
This enzyme has one substrate, 4-amino-4-deoxychorismate, and two products, 4-aminobenzoate (PABA) and pyruvate.
This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. This enzyme, encoded by the pabC gene in bacteria and plants, is also known as PabC or ADC lyase. The fungal enzyme has been designated ABZ2.
All known examples of 4-amino-4-deoxychorismate lyase bind PLP (pyridoxal-5'-phosphate), a cofactor employed during catalysis.
References
- Ye QZ, Liu J, Walsh CT (1990). "p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase". Proc. Natl. Acad. Sci. U.S.A. 87 (23): 9391–5. doi:10.1073/pnas.87.23.9391. PMC 55171. PMID 2251281.
- Green JM, Merkel WK, Nichols BP (1992). "Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme". J. Bacteriol. 174 (16): 5317–23. PMC 206368. PMID 1644759.
- Nakai T, Mizutani H, Miyahara I, Hirotsu K, Takeda S, Jhee KH, Yoshimura T, Esaki N (2000). "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli". J. Biochem. 128 (1): 29–38. doi:10.1093/oxfordjournals.jbchem.a022727. PMID 10876155. Link to article.
- O'Rourke PEF, Eadsforth TC, Fyfe PK, Shepherd SM, Hunter WN (2011). "Pseudomonas aeruginosa 4-amino-4-deoxychorismate lyase: spatial conservation of an active site tyrosine and classification of two types of enzyme". PLOS ONE. 6 (9): e24158. doi:10.1371/journal.pone.0024158. PMC 3174152. PMID 21935381.
- Botet J, Mateos L, Revuelta JL, Santos MA (2007). "A chemogenomic screening of sulfanilamide-hypersensitive Saccharomyces cerevisiae mutants uncovers ABZ2, the gene encoding a fungal aminodeoxychorismate lyase" (PDF). Eukaryot. Cell. 6 (11): 2102–11. doi:10.1128/EC.00266-07. PMC 2168415. PMID 17873082.
- Dai YN, Chi CB, Zhou K, Cheng W, Jiang YL, Ren YM, Ruan K, Chen Y, Zhou CZ (2013). "Structure and catalytic mechanism of yeast 4-amino-4-deoxychorismate lyase". J. Biol. Chem. 288 (32): 22985–92. doi:10.1074/jbc.M113.480335. PMC 3743474. PMID 23818518.
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