Biology:Dihydroneopterin aldolase
| dihydroneopterin aldolase | |||||||||
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 oktamer | |||||||||
| Identifiers | |||||||||
| EC number | 4.1.2.25 | ||||||||
| CAS number | 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 | |||||||||
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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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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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 1NBU, 1RRI, 1RRW, 1RRY, 1RS2, 1RS4, 1RSD, 1RSI, 1U68, 1Z9W, 2CG8, 2NM2, and 2NM3.
References
- "The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase". J. Biol. Chem. 245 (11): 3015–25. 1970. PMID 4912541.
External links
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