CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.1130.10
Functional Family 7,8-dihydroneopterin aldolase

Enzyme Information

4.1.2.25
Dihydroneopterin aldolase.
based on mapping to UniProt P56740
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
-!- The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. -!- The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8). -!- The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81. -!- The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
5.1.99.8
7,8-dihydroneopterin epimerase.
based on mapping to UniProt P56740
7,8-dihydroneopterin = 7,8-dihydromonapterin.
-!- The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25. -!- The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81).

UniProtKB Entries (1)

P56740
FOLB_STAAU
Staphylococcus aureus
Dihydroneopterin aldolase

PDB Structure

PDB 1RRI
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Discovery of Potent Inhibitors of Dihydroneopterin Aldolase Using CrystaLEAD High-Throughput X-ray Crystallographic Screening and Structure-Directed Lead Optimization.
Sanders, W.J., Nienaber, V.L., Lerner, C.G., McCall, J.O., Merrick, S.M., Swanson, S.J., Harlan, J.E., Stoll, V.S., Stamper, G.F., Betz, S.F., Condroski, K.R., Meadows, R.P., Severin, J.M., Walter, K.A., Magdalinos, P., Jakob, C.G., Wagner, R., Beutel, B.A.
J.Med.Chem.