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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.26.12 - ribonuclease E and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97YC2

for references in articles please use BRENDA:EC3.1.26.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.26 Endoribonucleases producing 5'-phosphomonoesters
                3.1.26.12 ribonuclease E
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q97YC2 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
Synonyms
rnase e, endoribonuclease rnase e, ribonuclease e, rnasee, rnase es, endoribonuclease e, rne protein, rnase ev, ncgl2281, sso1404, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
76106-82-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
single-stranded RNA + H2O
?
show the reaction diagram
preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11936
2 * 11936, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 11936, calculated from sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. The crystal structure of SSO1404 is solved at 1.6 A resolution revealing the first ribonuclease with a ferredoxin-like fold
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D10A
inactive mutant enzyme
D13A
mutant enzyme shows wild-type level activity
D14A
mutant enzyme shows wild-type level activity
D65A
2fold drop in activity compared to wild-type
F37A
inactive mutant enzyme
N18A
mutant enzyme shows wild-type level activity
Q33A
slightly reduced activity
R17A
very low activity
R19A
very low activity
R31A
inactive mutant enzyme
R67A
mutant enzyme shows wild-type level activity
S35A
slightly reduced activity
T12A
2fold drop in activity compared to wild-type
Y34A
slightly reduced activity
Y9A
very low activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion with an N-terminal His6 tag in Escherichia coli strain BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beloglazova, N.; Brown, G.; Zimmerman, M.D.; Proudfoot, M.; Makarova, K.S.; Kudritska, M.; Kochinyan, S.; Wang, S.; Chruszcz, M.; Minor, W.; Koonin, E.V.; Edwards, A.M.; Savchenko, A.; Yakunin, A.F.
A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats
J. Biol. Chem.
283
20361-20371
2008
Saccharolobus solfataricus (Q97YC2), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97YC2)
Manually annotated by BRENDA team