Aminodeoxychorismate lyase

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In enzymology, an aminodeoxychorismate lyase (EC 4.1.3.38) is an enzyme that catalyzes the chemical reaction

4-amino-4-deoxychorismate $\rightleftharpoons$ 4-aminobenzoate + pyruvate

Hence, this enzyme has one substrate, 4-amino-4-deoxychorismate, and two products, 4-aminobenzoate and pyruvate.

This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 4-amino-4-deoxychorismate pyruvate-lyase (4-aminobenzoate-forming). Other names in common use include enzyme X, 4-amino-4-deoxychorismate lyase, and 4-amino-4-deoxychorismate pyruvate-lyase. This enzyme participates in folate biosynthesis.

[edit] References

IUBMB entry for 4.1.3.38
BRENDA references for 4.1.3.38 (Recommended.)
PubMed references for 4.1.3.38
PubMed Central references for 4.1.3.38
Google Scholar references for 4.1.3.38
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: 9391–5. doi:10.1073/pnas.87.23.9391. 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: 5317–23. PMID 1644759.
Yoshimura T, Esaki N (Tokyo). "Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli". J. Biochem.: 29–38. PMID 10876155.