|
type |
Journal Article |
authors |
Magnani G, Lomazzi M, Peracchi A. |
title |
Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase. |
journal |
Biochem J. |
Activity |
4.1.3.38 |
Family |
4.1.3.38.b |
sel |
selected |
ui |
23957380 |
year |
(2013) |
volume |
455 |
number |
2 |
pages |
149-55 |
| |
abstract |
Enzymes that produce or recycle folates are the targets of widely used antimalarial drugs. Despite the interest in the folate metabolism of Plasmodium falciparum, the molecular identification of ADCL (aminodeoxychorismate lyase), which synthesizes the p-aminobenzoate moiety of folate, remained unresolved. In the present study, we demonstrate that the plasmodial gene PF14_0557 encodes a functional ADCL and report a characterization of the recombinant enzyme. |
last changed |
2014/02/25 11:04 |
|