Dihydroneopterin aldolase
| dihydroneopterin aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
![]() oktamer | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.2.25 | ||||||||
| CAS no. | 37290-59-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Dihydroneopterin aldolase | |||||||
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![]() crystal structure of 7,8-dihydroneopterin aldolase in complex with guanine | |||||||
| Identifiers | |||||||
| Symbol | FolB | ||||||
| Pfam | PF02152 | ||||||
| Pfam clan | CL0334 | ||||||
| InterPro | IPR006157 | ||||||
| SCOP2 | 1b9l / SCOPe / SUPFAM | ||||||
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[1] The enzyme dihydroneopterin aldolase (EC 4.1.2.25) catalyzes the chemical reaction
- 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde
This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropt eridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming). Other names in common use include 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-, and dihydropteridine glycolaldehyde-lyase. This enzyme participates in folate biosynthesis.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1NBU, PDB: 1RRI, PDB: 1RRW, PDB: 1RRY, PDB: 1RS2, PDB: 1RS4, PDB: 1RSD, PDB: 1RSI, PDB: 1U68, PDB: 1Z9W, PDB: 2CG8, PDB: 2NM2, and PDB: 2NM3.
References
- ↑ Wang, Yi; Li, Yue; Wu, Yan; Yan, Honggao (2007). "Mechanism of dihydroneopterin aldolase". The FEBS Journal. 274 (9): 2240–2252. doi:10.1111/j.1742-4658.2007.05761.x. ISSN 1742-4658. PMID 17388809.
Further reading
- Hennig, Michael; D′Arcy, Allan; Hampele, Isabella C.; Page, Malcolm G. P.; Oefner, Christian; Dale, Glenn E. (May 1998). "Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus". Nature Structural Biology. 5 (5): 357–362. doi:10.1038/nsb0598-357. ISSN 1545-9985. PMID 9586996.
- Sanders, William J.; Nienaber, Vicki L.; Lerner, Claude G.; McCall, J. Owen; Merrick, Sean M.; Swanson, Susan J.; Harlan, John E.; Stoll, Vincent S.; Stamper, Geoffrey F.; Betz, Stephen F.; Condroski, Kevin R.; Meadows, Robert P.; Severin, Jean M.; Walter, Karl A.; Magdalinos, Peter (2004-03-01). "Discovery of Potent Inhibitors of Dihydroneopterin Aldolase Using CrystaLEAD High-Throughput X-ray Crystallographic Screening and Structure-Directed Lead Optimization". Journal of Medicinal Chemistry. 47 (7): 1709–1718. doi:10.1021/jm030497y. ISSN 0022-2623. PMID 15027862.
- Wang, Yi; Li, Yue; Yan, Honggao (2006-12-01). "Mechanism of Dihydroneopterin Aldolase: Functional Roles of the Conserved Active Site Glutamate and Lysine Residues". Biochemistry. 45 (51): 15232–15239. doi:10.1021/bi060949j. ISSN 0006-2960. PMC 3018710. PMID 17176045.
- Czeczot, Alexia de Matos; Muniz, Mauro Neves; Perelló, Marcia Alberton; Silva, Éverton Edésio Dinis; Timmers, Luís Fernando Saraiva Macedo; Berger, Andresa; Gonzalez, Laura Calle; Arraché Gonçalves, Guilherme; Moura, Sidnei; Machado, Pablo; Bizarro, Cristiano Valim; Basso, Luiz Augusto (2024-12-31). "Crystal structure of dihydroneopterin aldolase from Mycobacterium tuberculosis associated with 8-mercaptoguanine, and development of novel S8-functionalized analogues as inhibitors: Synthesis, enzyme inhibition, in vitro toxicity and antitubercular activity". Journal of Enzyme Inhibition and Medicinal Chemistry. 39 (1). doi:10.1080/14756366.2024.2388207. ISSN 1475-6366. PMC 11328599. PMID 39140692.
- Garçon, Arnaud; Levy, Colin; Derrick, Jeremy P. (July 2006). "Crystal Structure of the Bifunctional Dihydroneopterin Aldolase/6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Streptococcus pneumoniae". Journal of Molecular Biology. 360 (3): 644–653. doi:10.1016/j.jmb.2006.05.038. PMID 16781731.
- Hitchings, George H.; Burchall, James J. (January 1965), "Inhibition of Folate Biosynthesis and Function as a Basis for Chemotherapy", in Nord, F. F. (ed.), Advances in Enzymology and Related Areas of Molecular Biology, Advances in Enzymology - and Related Areas of Molecular Biology, vol. 27 (1 ed.), Wiley, pp. 417–468, doi:10.1002/9780470122723.ch9, ISBN 978-0-470-12498-7, PMID 4387360, retrieved 2024-12-09
- Bermingham, Alun; Derrick, Jeremy P. (July 2002). "The folic acid biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery". BioEssays. 24 (7): 637–648. doi:10.1002/bies.10114. ISSN 0265-9247. PMID 12111724.
- Mathis JB, Brown GM (1970). "The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase". J. Biol. Chem. 245 (11): 3015–25. doi:10.1016/S0021-9258(18)63090-X. PMID 4912541.
External links
Media related to Dihydroneopterin aldolase at Wikimedia Commons

