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Literature summary for 3.2.2.1 extracted from

  • Chen, N.; Zhao, Y.; Lu, J.; Wu, R.; Cao, Z.
    Mechanistic insights into the rate-limiting step in purine-specific nucleoside hydrolase (2015), J. Chem. Theory Comput., 11, 3180-3188 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular mechanics and dynamics simulations. The ribose release process can be divided into ribose dissociation and ribose release steps The ribose dissociation includes cleavage and exchange stages, in which a metastable 6fold intermediate will recover to an 8fold coordination shell of Ca2+ . The estimated barrier for the rate-determining step of the entire reaction is 13.0 kcal/mol, which is comparable to the experimental value of 16.7 kcal/mol. The gating mechanism arising from loop1 and loop2, as well as key residues around the active pocket, plays an important role in manipulating the ribose release Trypanosoma vivax

Organism

Organism UniProt Comment Textmining
Trypanosoma vivax Q9GPQ4
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Synonyms

Synonyms Comment Organism
IAG-nucleoside hydrolase
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Trypanosoma vivax