Dihydroneopterin aldolase
| dihydroneopterin aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 oktamer | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.2.25 | ||||||||
| CAS no. | 37290-59-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Dihydroneopterin aldolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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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In enzymology, a dihydroneopterin aldolase (EC 4.1.2.25) is an enzyme that 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
Thus, the substrate (biochemistry) of this enzyme is , whereas its two products are and 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 1NBU, 1RRI, 1RRW, 1RRY, 1RS2, 1RS4, 1RSD, 1RSI, 1U68, 1Z9W, 2CG8, 2NM2, and 2NM3.
References[]
- Mathis JB, Brown GM (1970). "The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase". J. Biol. Chem. 245 (11): 3015–25. PMID 4912541.
External links[]
Media related to Dihydroneopterin aldolase at Wikimedia Commons
- EC 4.1.2
- Enzymes of known structure
- EC 4.1 stubs