EC Number   |
General Information |
Reference |
|---|
    3.2.2.1 | malfunction |
changes in the levels of purine, pyrimidine, and cytokinin metabolites in knockout mutants, phenotypes, overview |
-, 732656 |
| 3.2.2.1 | more |
active site structure, homology modelling, overview |
731139 |
| 3.2.2.1 | more |
all plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base |
732656 |
| 3.2.2.1 | more |
molecular mechanism underlying the conformational change necessary for enzymatic catalysis, overview |
-, 731054 |
| 3.2.2.1 | more |
regulation mechanisms of key residues and loops 1 and 2 for the base release, molecular dynamics simulations, overview. The base release process is not the rate-limiting step in the entire hydrolysis process, and the very low barrier of about 5.6 kcal/mol can bewashed out easily by the notable exothermicity fromthe substrate hydrolysis step. Glu82/Trp83 in loop 1 and His247/Arg252 in loop 2 are important to modulate the base release. Partial helix-to-coil change of loop 2 occurs along with the base release process |
731341 |
| 3.2.2.1 | more |
the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides. All plant nucleoside N-ribohydrolases exhibit a conserved sequence motif, DTDPGIDD, at the N-terminus, and the second Asp of the DTDPGIDD conserved motif functions as the active site base |
-, 732656 |
| 3.2.2.1 | physiological function |
both isoforms URH1 and URH2 are unimportant for seedling establishment and plant growth, both isoform URH1 and URH2 are required for efficient inosine and xanthosine hydrolytic activity |
716358 |
| 3.2.2.1 | physiological function |
isoform NSH3 functions as an extracellular, purine-specific hydrolase that is involved in degradation of extracellular nucleosides and participates in wound and pathogen responses |
716542 |
