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Literature summary extracted from

  • Mayans, O.; Ivens, A.; Nissen, L.J.; Kirschner, K.; Wilmanns, M.
    Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry (2002), EMBO J., 21, 3245-3254.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.18 the crystal structure of the dimeric class III phosphoribosyltransferase. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is coordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families Saccharolobus solfataricus

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.18 Saccharolobus solfataricus P50384
-
-
2.4.2.18 Saccharolobus solfataricus P2 P50384
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-

Subunits

EC Number Subunits Comment Organism
2.4.2.18 dimer
-
 Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
2.4.2.18 AnPRT
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 Saccharolobus solfataricus
2.4.2.18 anthranilate phosphoribosyltransferase
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 Saccharolobus solfataricus