Literature summary for 3.1.13.B1 extracted from

Clouet-d'Orval, B.; Rinaldi, D.; Quentin, Y.; Carpousis, A.J.
Euryarchaeal beta-CASP proteins with homology to bacterial RNase J Have 5'- to 3'-exoribonuclease activity (2010), J. Biol. Chem., 285, 17574-17583.

Search for more literature for 3.1.13.B1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyrococcus abyssi
expression in Escherichia coli	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	Organism
E209A	significantly reduced activity compared with the wild type protein	Pyrococcus abyssi
H388A	significantly reduced activity compared with the wild type protein	Pyrococcus abyssi
H410A	mutant enzyme has full activity	Pyrococcus abyssi
H410V	significant loss of activity	Thermococcus kodakarensis
H86A	significantly reduced activity compared with the wild type protein	Pyrococcus abyssi

Inhibitors

Inhibitors	Comment	Organism	Structure
1,10-phenanthroline	20 mM, strong inhibition	Pyrococcus abyssi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	the addition of divalent ions to the reaction buffer does not stimulate the reaction	Pyrococcus abyssi

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus abyssi	Q9V076	-	-
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543	Q9V076	-	-
Thermococcus kodakarensis	Q5JH57	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus abyssi
-	Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5'-pC-sR47 + H2O	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	Pyrococcus abyssi	5'-phosphomononucleotides	-	?
5'-pC-sR47 + H2O	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	Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543	5'-phosphomononucleotides	-	?
additional information	pre-tRNA(Trp) is a poor substrate	Pyrococcus abyssi	?	-	?
additional information	pre-tRNA(Trp) is a poor substrate	Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543	?	-	?
RNA + H2O	highly processive 5'-to-3'-exoribonuclease	Thermococcus kodakarensis	3'-phosphomononucleotides	-	?

Synonyms

Synonyms	Comment	Organism
Pab-RNase J	-	Pyrococcus abyssi
PAB1751	-	Pyrococcus abyssi
Tk-RNase J	-	Thermococcus kodakarensis
Tk1469	-	Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
65	-	assay at	Pyrococcus abyssi
65	-	assay at	Thermococcus kodakarensis
95	-	activity increases with temperature up to 95°C, the maximum temperature tested	Pyrococcus abyssi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	8	-	Pyrococcus abyssi
7.5	-	assay at	Thermococcus kodakarensis

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Release 2023.1 (January 2023)