EC Number   |
General Information |
Reference |
|---|
   3.1.1.29 | evolution |
Ankzf1 is Saccharomyces cerevisiae Vms1 homologue |
751694 |
| 3.1.1.29 | evolution |
performing the essential function of recycling peptidyl-tRNAs, peptidyl-tRNA hydrolases are ubiquitous in all domains of life. The multicomponent eukaryotic Pth system differs greatly from the bacterial system composed predominantly of a single Pth1 enzyme |
752098 |
| 3.1.1.29 | evolution |
Vms1 is a member of a clade of eRF1 homologues that is designated the Vms1-like RF1 clade (VLRF1) |
-, 751694 |
| 3.1.1.29 | malfunction |
backbone dynamics of VcPth and its mutants, NMR and molecular dynamics simulation, overview |
752162 |
| 3.1.1.29 | malfunction |
since build-up of peptidyl-tRNAs is toxic, defects in enzyme function result in cell death |
730449 |
| 3.1.1.29 | metabolism |
enzyme Vms1, which contains a Cdc48-binding VIM motif, is implicated in the ribosome quality control (RQC) pathway. The 60S subunits retain the peptidyl-tRNA nascent chains, which recruit the RQC complex comprised of Rqc1-Rqc2-Ltn1-Cdc48-Ufd1-Npl4. Nascent chains ubiquitylated by the E3/ubiquitin ligase Ltn1 are extracted from the 60S by the ATPase Cdc48-Ufd1-Npl4 and presented to the 26S proteasome for degradation. The Vms1-dependent reaction does not display strong dependence on substrate ubiquitylation |
-, 751694 |
| 3.1.1.29 | more |
enzyme structure analysis, overview |
-, 749860 |
| 3.1.1.29 | more |
enzyme structure and dynamics by NMR spectroscopy and molecular dynamics simulations. Of the substrate binding segments, the gate loop is rigid, the base loop displays slow motions, while the lid loop displays fast timescale motions. The NMR structure of Mycobacterium smegmatis MsPth shares the canonical Pth fold with theNMR structure of Mycobacterium tuberculosis MtPth |
-, 749971 |
| 3.1.1.29 | more |
enzyme Vms1 activity is dependent on a conserved catalytic glutamine. The putative catalytic region of Vms1 and other VLRF1 proteins is flanked by additional N- and C-terminal domains. The N-terminal C2H2-zinc finger of Vms1 is specifically related to those of Rei1 and certain SBDS paralogues, which function at late steps in 60S subunit maturation |
-, 751694 |
| 3.1.1.29 | more |
PTRHD1 lacks the conserved, catalytically essential His20 |
752098 |
