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.
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| 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).
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UniProtKB Entries (1)
| P56740 |
FOLB_STAAU
Staphylococcus aureus
Dihydroneopterin aldolase
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PDB Structure
| PDB | 1RRY |
| 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.
J.Med.Chem.
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