EC Number   |
General Information |
Reference |
|---|
   3.2.2.3 | malfunction |
a knockout mutant for isoform NSH1 shows symptoms of accelerated senescence, accompanied by marked accumulation of uridine and xanthosine under conditions of prolonged darkness |
716542 |
| 3.2.2.3 | malfunction |
changes in the levels of purine, pyrimidine, and cytokinin metabolites in knockout mutants, phenotypes, overview |
732656 |
| 3.2.2.3 | more |
the presence of a tyrosine at position 249 (PpNRH1 numbering) confers high hydrolase activity for purine ribosides |
732656 |
| 3.2.2.3 | physiological function |
isoform NSH1 represents the leading activity in purine and pyrimidine breakdown in a cell |
716542 |
| 3.2.2.3 | physiological function |
nucleoside hydrolase NSH1 activates NSH2 in vitro and in vivo, forming a complex with almost two orders of magnitude higher catalytic efficiency for xanthosine hydrolysis than observed for NSH1 alone. An inactive NSH1 point mutant can activate NSH2 in vivo, fully preventing purine nucleoside accumulation in Nsh1 mutant background |
751844 |
| 3.2.2.3 | physiological function |
uridine-ribohydrolase is a key regulator in the uridine degradation pathway of Arabidopsis thaliana, with a pivotal function of URH1 as regulative in pyrimidine degradation. The enzyme activity must be well balanced in the early phase of plant development |
700741 |
