EC Number   |
General Information |
Reference |
|---|
    3.2.2.5 | evolution |
the enzyme is evolving and has diverged into NAD+ glycohydrolase-inactive variants that correlate with tissue tropism. Of a total 454 amino acids, the activity-deficient variants differ at only nine highly conserved positions |
-, 732106 |
| 3.2.2.5 | evolution |
the enzyme shows significant structural and functional analogy to the members of the CD38/ADP-ribosyl cyclase family but a lack of ADP-ribosyl cyclase activity that might be ascribed to subtle changes in its active site. In sharp contrast with mammalian CD38, the signature Glu124 is as critical as Glu202 for catalysis by the parasite enzyme. Sequence comparisons |
731344 |
| 3.2.2.5 | malfunction |
shRNA-mediated knockdown of the NADase in bone marrow cells results in a reduction of erythroid colony formation and an increase in NAD level, and treatment of the bone marrow cells with NAD, nicotinamide, or nicotinamide riboside, which induce an increase in NAD content, results in a significant decrease in erythroid progenitors |
-, 732135 |
| 3.2.2.5 | malfunction |
the enzyme represents one major virulent exoprotein in the streptococcal toxic shock syndrome, overview |
707174 |
| 3.2.2.5 | more |
models of molecular evolution shows that SPN is evolving under positive selection and diverging into NAD+ glycohydrolase-active and -inactive subtypes |
708939 |
| 3.2.2.5 | more |
no one single residue can account for the inability of the deficient variants to cleave the glycosidic bond of beta-NAD+ into nicotinamide and ADP-ribose. Reciprocal changes at 3 specific residues are required to both abolish activity of the proficient version and restore full activity to the deficient variant |
-, 732106 |
| 3.2.2.5 | more |
structural determinants for the functional evolution from a cyclase to a hydrolase, overview |
709059 |
| 3.2.2.5 | more |
the catalytic glutamine 218 of NADase is a crucial residue for NADase activity |
-, 732135 |
| 3.2.2.5 | more |
the Gram-positive pathogen Streptococcus pyogenes injects a beta-NAD+-glycohydrolase into the cytosol of an infected host cell using the cytolysin-mediated translocation pathway, where SPN accelerates the death of the host cell |
709150 |
| 3.2.2.5 | more |
three dimensional homology modeling of the enzyme, very important role of Glu202 and of the hydrophobic domains overwhelmingly in the efficiency of the nicotinamide-ribosyl bond cleavage step. The nicotinamide-ribosyl bond is cleaved upon the first step of catalysis and is surrounded by three hydrophobic side chains Leu123, Tyr172 and Phe102 |
731344 |
