Dihydroneopterin aldolase

dihydroneopterin aldolase
oktamer
Identifiers
EC no.4.1.2.25
CAS no.37290-59-8
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Dihydroneopterin aldolase
crystal structure of 7,8-dihydroneopterin aldolase in complex with guanine
Identifiers
SymbolFolB
PfamPF02152
Pfam clanCL0334
InterProIPR006157
SCOP21b9l / SCOPe / SUPFAM
Available protein structures:
PDB  IPR006157 PF02152 (ECOD; PDBsum)  
AlphaFold

[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

  1. ↑ 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

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