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

\rightleftharpoons

4-aminobenzoate + pyruvate

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. (Tokyo) 128. (1): 29–38. 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". 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.

Carbon-carbon lyases (EC 4.1)

4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase

4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase

4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase

4.1.99: Other	Tryptophanase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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