B6db activities : 4_1_3

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	4.1.3.38
Description	4-amino-4-deoxychorismate lyase
Alternative names	Aminodeoxychorismate lyase. ADC lyase. 4-amino-4-deoxychorismate pyruvate-lyase.
Catalyzed reaction	4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
Cofactor	Pyridoxal-phosphate.
Comments	Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 6.3.5.8, aminodeoxychorismate synthase, to form p-aminobenzoate.
	At least three different subgroups of enzymes with this activity appear to exist. These enzymes all belong to the fold-type IV group, but show very limited sequence similarity to each other.
PDB	1ET0;
Organisms	-Bacteria -Plants -Fungi
Family	4.1.3.38_a (13) 4.1.3.38_b (5) 4.1.3.38_c (5)

Links	Enzyme (activities) 4.1.3.38 BRENDA (activities) 4.1.3.38 KEGG (pathways) 4.1.3.38 PLPMDB (PLP mutants) 4.1.3.38

References	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 2102-11. Basset, G.J.; Ravanel, S.; Quinlivan, E.P.; White, R.; Giovannoni, J.J.; Rebeille, F.; Nichols, B.P.; Shinozaki, K.; Seki, M.; Gregory, J.F. 3rd.; Hanson, A.D. (2004) Folate synthesis in plants: the last step of the p-aminobenzoate branch is catalyzed by a plastidial aminodeoxychorismate lyase Plant J 40 453-61.. Nakai, T.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Takeda, S.; Jhee, K. H.; Yoshimura, T.; Esaki, N. (2000) Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli J Biochem (Tokyo) 128 29-38.. Green, J. M.; Nichols, B. P. (1991) p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC J Biol Chem 266 12971-5.. Articles on 4.1.3.38

last changed	2008/02/27 13:02

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