Biology:Aminodeoxychorismate lyase
From HandWiki
| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 4-aminobenzoate + 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
- "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. 1990. doi:10.1073/pnas.87.23.9391. PMID 2251281.
- "Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme". J. Bacteriol. 174 (16): 5317–23. 1992. doi:10.1128/jb.174.16.5317-5323.1992. PMID 1644759.
- "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli". J. Biochem. 128 (1): 29–38. 2000. doi:10.1093/oxfordjournals.jbchem.a022727. PMID 10876155. Link to article.
- "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. 2011. doi:10.1371/journal.pone.0024158. PMID 21935381.
- "A chemogenomic screening of sulfanilamide-hypersensitive Saccharomyces cerevisiae mutants uncovers ABZ2, the gene encoding a fungal aminodeoxychorismate lyase". Eukaryot. Cell 6 (11): 2102–11. 2007. doi:10.1128/EC.00266-07. PMID 17873082. PMC 2168415. https://digital.csic.es/bitstream/10261/65650/1/accesoRestringido.pdf.
- "Structure and catalytic mechanism of yeast 4-amino-4-deoxychorismate lyase". J. Biol. Chem. 288 (32): 22985–92. 2013. doi:10.1074/jbc.M113.480335. PMID 23818518.
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