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. Author manuscript; available in PMC: 2019 Jul 9.
Published in final edited form as: Chem Rev. 2018 Oct 18;118(22):11194–11258. doi: 10.1021/acs.chemrev.8b00369

Table 1.

Chemical Test of Leaving Group Activation for N-Ribosyltransferases*

Enzyme [kcat p-NO2-φ-riboside]/[kcat substrate]
CfNH (IU-nucleoside hydrolase)a 8.5 graphic file with name nihms-1034037-t0089.jpg
LmNH (IU-nucleoside hydrolase)b 1.8
IAG-nucleoside hydrolasec 0.024
GI-nucleoside hydrolased 0.0003
Purine nucleoside phosphorylasee 0.000017
AMP nucleosidasef 0.000015
Reactions compared p-nitrophenyl β-D-riboside as substrate to a,b,cinosine, dguanosine, and einosine. fp-Nitrophenyl β-D-riboside 5′-phosphate and AMP were compared as substrates for AMP nucleosidase. bLmNH is the enzyme from Leishmania major. Results from reference 89, 90.
*

Reactions compared p-nitrophenyl β-D-riboside as substrate to a,b,cinosine, dguanosine, and einosine. fp-Nitrophenyl β-D-riboside 5′-phosphate and AMP were compared as substrates for AMP nucleosidase. bLmNH is the enzyme from Leishmania major. Results from refs 89 and 90.