Title : Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis.

Pub. Date : 2001 Jan 30

PMID : 11170405






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Contacts between PNP and catalytic site ligands are shorter in the transition state analogue complex of PNP.ImmH.PO(4) than in the Michaelis complexes of PNP.inosine.SO(4) or PNP.hypoxanthine.ribose 1-PO(4). Inosine purine nucleoside phosphorylase Bos taurus
2 Contacts between PNP and catalytic site ligands are shorter in the transition state analogue complex of PNP.ImmH.PO(4) than in the Michaelis complexes of PNP.inosine.SO(4) or PNP.hypoxanthine.ribose 1-PO(4). Inosine purine nucleoside phosphorylase Bos taurus
3 Contacts between PNP and catalytic site ligands are shorter in the transition state analogue complex of PNP.ImmH.PO(4) than in the Michaelis complexes of PNP.inosine.SO(4) or PNP.hypoxanthine.ribose 1-PO(4). Inosine purine nucleoside phosphorylase Bos taurus
4 Contacts between PNP and catalytic site ligands are shorter in the transition state analogue complex of PNP.ImmH.PO(4) than in the Michaelis complexes of PNP.inosine.SO(4) or PNP.hypoxanthine.ribose 1-PO(4). Inosine purine nucleoside phosphorylase Bos taurus