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
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3.1.26.12
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degradosome
-
polynucleotide
-
phosphorylase
-
pnpase
-
srnas
-
endonuclease
-
hfq
-
helicase
-
endonucleolytic
-
exoribonuclease
-
single-stranded
-
enolase
-
stem-loops
-
polya
-
rna-binding
-
polycistronic
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ribonucleolytic
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e-dependent
-
base-pairing
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dead-box
-
autoregulation
-
e-mediated
-
e-like
-
ompa
-
endoribonucleolytic
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5'-terminal
-
intercistronic
-
cole1-type
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monophosphorylated
-
5'-monophosphorylated
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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
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Reaction
Reaction on EC 3.1.26.12 - ribonuclease E
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endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
catalytic mechanism, the 10-mer and 13-mer RNAs are bound entirely by one tetramer, while the 15-mer RNA is long enough for it to be shared between two different tetramers in the crystal lattice, and this RNA extends from the 5' sensing pocket of one tetramer into the binding channel and catalytic site of a symmetry-related tetramer. Two molecules of 15-mer RNA pass each other in antiparallel orientations and form a highly distorted duplex, Asp 303 and Asp 346 might act as general bases to activate the attacking water
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
molecular mechanism, residues A326 and L385 are involved in substrate binding