Literature summary for 3.1.26.5 extracted from

Gao, X.; Oshima, K.; Ueda, T.; Nakashima, T.; Kimura, M.
A three-dimensional model of RNase P in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 (2017), Biochem. Biophys. Res. Commun., 493, 1063-1068 .

Search for more literature for 3.1.26.5

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pre-tRNA + H2O	Pyrococcus horikoshii	the enzyme is involved in maturation of the 5'-end of tRNA	tRNA + 5'-oligoribonucleotide	-	?
pre-tRNA + H2O	Pyrococcus horikoshii	the enzyme is involved in maturation of the 5'-end of tRNA	mature tRNA + 5'-terminal oligonucleotide	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O59150 AND O59248 AND O59425 AND O59543 AND P62009	the enzyme consists of a catalytic RNase P RNA and five protein cofactors designated PhoPop5 (O59150), PhoRpp21 (O59248), PhoRpp29 (O59425), PhoRpp30 (O59543), and PhoRpp38 (P62009)	-
Pyrococcus horikoshii	O59425 and O59150 and O59543 and O59248 and P62009	O59425: ribonuclease P protein component 1 (PhoRpp29), O59150: ribonuclease P protein component 2 (PhoPop5), O59543: ribonuclease P protein component 3 (PhoRpp30), O59248: ribonuclease P protein component 4 (RPP21), 50S ribosomal protein L7Ae (PhoRpp38). RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pre-tRNA + H2O	the enzyme is involved in maturation of the 5'-end of tRNA	Pyrococcus horikoshii	tRNA + 5'-oligoribonucleotide	-	?
pre-tRNA + H2O	the enzyme is involved in maturation of the 5'-end of tRNA	Pyrococcus horikoshii	mature tRNA + 5'-terminal oligonucleotide	-	?
pre-tRNA(Tyr) + H2O	-	Pyrococcus horikoshii	mature tRNA(Tyr) + 5'-terminal oligonucleotide	-	?
pre-tRNA-Tyr + H2O	-	Pyrococcus horikoshii	tRNA-Tyr + 5'-oligoribonucleotide	-	?

Subunits

Subunits	Comment	Organism
More	RNase P consists of a catalytic RNase P RNA (PhopRNA) and five protein cofactors designated PhoPop5, PhoRpp21, PhoRpp29, PhoRpp30, and PhoRpp38. A heterotetramer composed of PhoPop5 and PhoRpp30 bridges helices P3 and P16 in the PhopRNA C-domain, thereby probably stabilizing a double-stranded RNA structure (helix P4) containing catalytic Mg2+ ions, while a heterodimer of PhoRpp21 and PhoRpp29 locates on a single-stranded loop connecting helices P11 and P12 in the specificity domain (S-domain) in PhopRNA, probably forming an appropriate conformation of the precursor tRNA (pre-tRNA) binding site. The fifth protein PhoRpp38 binds each kink-turn motif in helices P12.1, P12.2, and P16 in PhopRNA	Pyrococcus horikoshii
More	construction of a 3-D model of Pyrococcus horikoshii RNase P on the basis of crystallographic data. In the resulting 3-D structure, interactions of alpha-helices in proteins with double-stranded RNA structures appear to play an important role in stabilization of an appropriate PhopRNA conformation. Comparison of the resulting 3-D model with the crystal structure of the bacterial RNase P suggests that RNA-RNA interactions in bacterial RNase P are replaced by protein-RNA interactions in archaeal RNase P	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
RNase P	-	Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.6	-	assay at	Pyrococcus horikoshii

General Information

General Information	Comment	Organism
metabolism	the enzyme is involved in maturation of the 5'-end of tRNA	Pyrococcus horikoshii
physiological function	the enzyme is involved in maturation of the 5'-end of tRNA	Pyrococcus horikoshii

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)