Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.6.1.19 extracted from

  • Kriz, M.; Snasel, J.; Kopecky, V.; Pav, O.; Rosenberg, I.; Stepanek, J.
    Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy (2012), Biochim. Biophys. Acta, 1824, 1039-1044.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2'-5'-linked oligoadenylates natural 2'-5'-linked tetraadenylates and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogues of AMP are enzyme activators with equal potency. The enzyme is activated by the binding of 2'-5'-linked oligoadenylates to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography and dialysis Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
leukemia cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information assay substrate is 32P-labeled synthetic substrate r(C11U2C7) Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer active enzyme form Homo sapiens
More the estimated secondary structural composition of inactive monomeric RNase L is 44% alpha-helix, 28% beta-sheet, 17% beta-turns and 11% of unordered structures, whereas dimerization causes a slight decrease in alpha-helix and increase in beta-sheet (ca. 2%) content. Enzyme dimerization affects at least three Tyr, five Phe and two Trp residues. The alpha-beta structural switch may fix domain positions in the hinge region (residues ca. 336-363) during homodimer formation, Raman spectroscopy, overview Homo sapiens

Synonyms

Synonyms Comment Organism
RNase L
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

General Information

General Information Comment Organism
physiological function key enzyme in the defense system Homo sapiens