Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.2.1 extracted from

  • Luo, M.; Li, L.; Schramm, V.L.
    Remote mutations alter transition-state structure of human purine nucleoside phosphorylase (2008), Biochemistry, 47, 2565-2576.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K22E/H104R the transition state of the mutant is fully dissociative, N7-protonated hypoxanthine with C1'-N9 distance above 3.0 A, with partial participation of phosphate, C1-Ophosphate distance is 2.26 A, 2'-C-exo-ribosyl ring pucker and the O5'-C5'-C4'-O4' dihedral angle near 60°. The transition state of the mutant is altered from the fully dissociative DN*AN character for the human wild-type purine nucleoside phosphorylase to a late phosphate-associative character Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-