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

BRENDA support

3.1.13.1: exoribonuclease II

This is an abbreviated version!
For detailed information about exoribonuclease II, go to the full flat file.

Word Map on EC 3.1.13.1

Reaction

Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =

Synonyms

3'-5'exoribonuclease, 3’-5’exoribonuclease, 5'->3' exoribonuclease 2, AB205_0003320, Dis, Dis3, EC 3.1.4.20, exonuclease ISG20, More, PfRNase II, RC-RNase 2, ribonuclease 2, ribonuclease II, ribonuclease Q, Ribonuclease R, RNase, RNase 2, RNase A, RNase II, RNase R, RNase-2, RNaseR, Rnb, RNR, RNR1, Rrp44, XRN2

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.13 Exoribonucleases producing 5′-phosphomonoesters
                3.1.13.1 exoribonuclease II

Posttranslational Modification

Posttranslational Modification on EC 3.1.13.1 - exoribonuclease II

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
residue Lys501 is acetylated in RNase II. This modification, reversibly controlled by the acetyltransferase Pka and the deacetylase CobB, a SIRT family deacetylase, affects binding of the substrate and thus decreases the catalytic activity of RNase II. Acetylation can regulate the activity of a bacterial ribonuclease. Lys501 is the major site of acetylation in this enzyme, but some other lysine residues in RNase II are also susceptible to acetylation. After enzyme inhibitor nicotinamide treatment, the acetylation level of RNase II increases 2-3fold in both wild-type and mutant strains. Inactivation of CobB increased the acetylation of wild-type RNase II