3.1.26.12: ribonuclease E
This is an abbreviated version!
For detailed information about ribonuclease E, go to the full flat file.
Word Map on EC 3.1.26.12
-
3.1.26.12
-
degradosome
-
polynucleotide
-
phosphorylase
-
pnpase
-
srnas
-
endonuclease
-
hfq
-
helicase
-
endonucleolytic
-
exoribonuclease
-
single-stranded
-
enolase
-
stem-loops
-
polya
-
rna-binding
-
polycistronic
-
ribonucleolytic
-
e-dependent
-
base-pairing
-
dead-box
-
autoregulation
-
e-mediated
-
e-like
-
ompa
-
endoribonucleolytic
-
5'-terminal
-
intercistronic
-
cole1-type
-
monophosphorylated
-
5'-monophosphorylated
-
shine-dalgarno
-
rho-independent
-
hfq-dependent
-
glucosamine-6-phosphate
-
riboswitches
-
au-rich
-
glm
-
rna-processing
-
crescentus
-
analysis
-
medicine
- 3.1.26.12
-
degradosome
- polynucleotide
- phosphorylase
- pnpase
- srnas
- endonuclease
- hfq
- helicase
-
endonucleolytic
- exoribonuclease
-
single-stranded
- enolase
-
stem-loops
- polya
-
rna-binding
-
polycistronic
-
ribonucleolytic
-
e-dependent
-
base-pairing
-
dead-box
-
autoregulation
-
e-mediated
-
e-like
- ompa
-
endoribonucleolytic
-
5'-terminal
-
intercistronic
-
cole1-type
-
monophosphorylated
-
5'-monophosphorylated
-
shine-dalgarno
-
rho-independent
-
hfq-dependent
- glucosamine-6-phosphate
- riboswitches
-
au-rich
- glm
-
rna-processing
- crescentus
- analysis
- medicine
Reaction
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions =
Synonyms
Ams/Rne/Hmp1 polypeptide, AqaRng, endoribonuclease E, endoribonuclease RNase E, More, NCgl2281, ribonuclease E, RNase E, RNase E/G, RNase E/G-type endoribonuclease, RNase ES, RNase EV, RNaseE, Rne, Rne protein, RneC, Rng, SSO1404, SynRne
ECTree
Advanced search results
Application
Application on EC 3.1.26.12 - ribonuclease E
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
analysis
-
the enzyme can be a model for investigation of the action of site specific nucleases
medicine
-
extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
medicine
-
extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
-