Enzyme

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     5. Isomerases
        5.1 Racemases and epimerases
            5.1.99 Acting on other compounds
ID:5.1.99.7
Description:Dihydroneopterin triphosphate 2'-epimerase.
Alternative Name: D-erythro-7,8-dihydroneopterin triphosphate epimerase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.1.99.7
BRENDA Enzyme Link: BRENDA 5.1.99.7
KEGG Enzyme Link: KEGG5.1.99.7
BioCyc Enzyme Link: BioCyc 5.1.99.7
ExPASy Enzyme Link: ExPASy5.1.99.7
EC2PDB Enzyme Link: EC2PDB 5.1.99.7
ExplorEnz Enzyme Link: ExplorEnz 5.1.99.7
PRIAM enzyme-specific profiles Link: PRIAM 5.1.99.7
IntEnz Enzyme Link: IntEnz 5.1.99.7
MEDLINE Enzyme Link: MEDLINE 5.1.99.7
MSA:

5.1.99.7;

Phylogenetic Tree:

5.1.99.7;

Uniprot:
M-CSA:
RHEA:28346 7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate
RULE(radius=1)
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase.Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G1998 Jul 109651328
Purification, cloning, and functional expression of dihydroneopterin triphosphate 2'-epimerase from Escherichia coli.Ahn C, Byun J, Yim J1997 Jun 139182560
FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa.Pribat A, Blaby IK, Lara-Núñez A, Gregory JF 3rd, de Crécy-Lagard V, Hanson AD2010 Jan19897652