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Literature summary for 3.1.26.11 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
Search for more literature for 3.1.26.11

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
G196A/Pro201A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
G200A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
G209A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
I212A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
K207A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
K207A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
K214A/Lys218A significant reductions in kcat as compared to wild-type tRNase Z Drosophila melanogaster
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
L206A increases in Km as compared to wild-type tRNase Z Drosophila melanogaster
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

Organism UniProt Comment Textmining
Drosophila melanogaster Q8MKW7
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-

Purification (Commentary)

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

Synonyms

Synonyms Comment Organism
tRNase Z
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 Drosophila melanogaster

General Information

General Information Comment Organism
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