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Literature summary for 3.1.1.96 extracted from

  • Lim, K.; Tempczyk, A.; Bonander, N.; Toedt, J.; Howard, A.; Eisenstein, E.; Herzberg, O.
    A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal structure of Hemophilus influenzae HI0670 (2003), J. Biol. Chem., 278, 13496-13502.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.96

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure is determined at a 1.64 A resolution. Comparison of the structures of the Escherichioa coli enzyme and the enzyme from Haemophilus influenzae together with modeling of the enzyme/D-Tyr-tRNA complex provides the structural basis for a proposed catalytic mechanism and explains the enzyme specificity data Haemophilus influenzae

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae P44814
-
-
Haemophilus influenzae DSM 11121 P44814
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haemophilus influenzae

Subunits

Subunits Comment Organism
dimer
-
 Haemophilus influenzae

Synonyms

Synonyms Comment Organism
D-Tyr-tRNATyr deacylase
-
 Haemophilus influenzae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
64
-
 Tm-value Haemophilus influenzae

General Information

General Information Comment Organism
physiological function the enzyme helps maintain the fidelity of protein synthesis Haemophilus influenzae