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ENZYME

ENZYME entry: EC 3.1.26.12

PURL: https://purl.expasy.org/enzyme/EC/3.1.26.12
Accepted Name
ribonuclease E
Alternative Name(s)
endoribonuclease E
RNase E
Reaction catalysed
Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
Comment(s)
  • RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication.
  • The enzyme binds to monophosphorylated 5' ends of substrates but exhibits sequential cleavages in the 3' to 5' direction.
  • 2'-O-methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5' to that locus.
  • In Escherichia coli, the enzyme is found in the RNA degradosome.
  • The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, EC 4.1.1.11 and EC 2.7.7.8.
  • Formerly EC 3.1.26.n1.
Cross-references
BRENDA3.1.26.12
EC2PDB3.1.26.12
ExplorEnz3.1.26.12
KEGG Ligand Database for Enzyme Nomenclature3.1.26.12
IUBMB Enzyme Nomenclature3.1.26.12
MEDLINEFind literature relating to 3.1.26.12
MetaCyc3.1.26.12
Rhea expert-curated reactions3.1.26.12
UniProtKB/Swiss-Prot
P57429, RNE_BUCAIQ8K9J9, RNE_BUCAPQ89AH3, RNE_BUCBP
P21513, RNE_ECOLIP44443, RNE_HAEINA0R152, RNE_MYCS2
P71905, RNE_MYCTUQ8YP69, RNE_NOSS1P72656, RNE_SYNY3

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.26.-
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