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Literature summary extracted from

  • Levinger, L.; Hopkinson, A.; Desetty, R.; Wilson, C.
    Effect of changes in the flexible arm on tRNase Z processing kinetics (2009), J. Biol. Chem., 284, 15685-15691.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.11 tRNase Z cDNA baculovirus-expressed from methionine 24 in insect Sf-9 cells Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.11 DELTAFA deletion of the flexible arm (FA) hand close to its boundaries with the stalk does not interfere with stability and expression of tRNase ZL. DELTAFA hand variant has a Km ca. 100times higher and a kcat ca. 2times lower than wild-type tRNase Z Drosophila melanogaster
3.1.26.11 G196A/Pro201A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 G200A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 G209A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 I212A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 K207A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 K207A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 K214A/Lys218A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 L187A substitution of alanine causes Km to increase almost as much as deletion of the entire flexible arm hand, with barely any decrease in kcat. A higher concentration of L187A enzyme than that of wild-type tRNase Z has to be used to accommodate the lower catalytic efficiency of the variant Drosophila melanogaster
3.1.26.11 L206A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
3.1.26.11 additional information a conserved leucine at the ascending stalk/hand boundary causes practically the same increase in Km as the hand deletion, thus nearly eliminating its ability to bind substrate. Km also increases with substitutions in theGP(alpha4-alpha5) loop and at other conserved residues in the flexible arm hand predicted to contact substrate. Substitutions that reduce kcat are clustered in the beta10-beta11 loop Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.11 Drosophila melanogaster Q8MKW7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.26.11 nickel chelate affinity purification of soluble tRNase Z Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
3.1.26.11 tRNase Z
-
Drosophila melanogaster

General Information

EC Number General Information Comment Organism
3.1.26.11 physiological function flexible arm of tRNase Z consists of 35–40 residues in a globular, compact alphaalphabetabetaeta structure (the hand) extruded from the body of the enzyme and held apart from it by an extended two-stranded polypeptide stalk Drosophila melanogaster