Information on EC 3.1.13.B1 - 5'-3' exoribonuclease

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.13.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
5'-3' exoribonuclease
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(A)40 + H2O
adenosine + 39 AMP
show the reaction diagram
5'-pA(A)39 + H2O
40 AMP
show the reaction diagram
5'-pC-sR47 + H2O
5'-phosphomononucleotides
show the reaction diagram
sR47 RNA labeled either at its 5' end as a 5'-[32P]monophosphate. The enzyme is a highly processive 5'-to-3'-exoribonuclease.The principal product of the 5' end-labeled RNA is [32P]GMP as guanosine is the 5'-nucleotide of sR47. Single-stranded DNA is degraded by the enzyme, suggesting that the it does not discriminate between ribose and 2'-deoxyribose nucleosides. Double-stranded DNA is resistant to degradation. The enzyme requires a free 5' end to initiate degradation
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?
5'-pppA(A)39 + H2O
ATP + 39 AMP
show the reaction diagram
5'-pppA(A)41 + H2O
ATP + 41 AMP
show the reaction diagram
RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
RNA + H2O
5'-phosphomononucleotides
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
20 mM, strong inhibition
initiation factor a/eIF2(gamma)
binding of translation initiation factor a/eIF2(gamma) to the 5'-end of mRNA counteracts the 5'-to-3' exoribonucleolytic activity in vitro. The factor binds by virtue of the gamma-subunit to the 5'-end of tri-phosphorylated mRNAs and thereby increases the stability of the 5'-part of mRNAs
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
activity increases with temperature up to 95°C, the maximum temperature tested
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia col
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E209A
significantly reduced activity compared with the wild type protein
H388A
significantly reduced activity compared with the wild type protein
H410A
mutant enzyme has full activity
H86A
significantly reduced activity compared with the wild type protein
H410V
significant loss of activity
additional information