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
isoform NSH3 functions as an extracellular, purine-specific hydrolase that is involved in degradation of extracellular nucleosides and participates in wound and pathogen responses
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
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
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
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
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
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