Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.60
Description:Dihydroneopterin triphosphate aldolase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.60
BRENDA Enzyme Link: BRENDA 4.1.2.60
KEGG Enzyme Link: KEGG4.1.2.60
BioCyc Enzyme Link: BioCyc 4.1.2.60
ExPASy Enzyme Link: ExPASy4.1.2.60
EC2PDB Enzyme Link: EC2PDB 4.1.2.60
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.60
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.60
IntEnz Enzyme Link: IntEnz 4.1.2.60
MEDLINE Enzyme Link: MEDLINE 4.1.2.60
MSA:

4.1.2.60;

Phylogenetic Tree:

4.1.2.60;

Uniprot:
M-CSA:
RHEA:52772 7,8-dihydroneopterin 3'-triphosphate = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde triphosphate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
6-pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria.Pribat A, Jeanguenin L, Lara-Núñez A, Ziemak MJ, Hyde JE, de Crécy-Lagard V, Hanson AD2009 Jul19395485
Plasmodium falciparum: a paradigm for alternative folate biosynthesis in diverse microorganisms?Hyde JE, Dittrich S, Wang P, Sims PF, de Crécy-Lagard V, Hanson AD2008 Nov18805734
An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites.Dittrich S, Mitchell SL, Blagborough AM, Wang Q, Wang P, Sims PF, Hyde JE2008 Feb18093090