Literature summary for 3.1.26.5 extracted from

Kakuta, Y.; Ishimatsu, I.; Numata, T.; Kimura, K.; Yao, M.; Tanaka, I.; Kimura, M.
Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21 (2005), Biochemistry, 44, 12086-12093.

Search for more literature for 3.1.26.5

Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion against 0.2 M triammonium citrate, pH 7.0, 20% v/v polyethylene glycol 3350, 10 mM ZnCl2 and 10% v/v ethanol. Stucture of a ribonuclease P protein Ph1601p determined at 1.6 A resolution with the aid of anomalous signals from selenomethionines and zinc ion	Pyrococcus horikoshii

Protein Variants

Protein Variants	Comment	Organism
C68S/C71S	mutant enzyme exhibits little enzymatic activity, mutation in ribonuclease P protein Ph1601p	Pyrococcus horikoshii
C97S/C100S	mutant enzyme exhibits little enzymatic activity, mutation in ribonuclease P protein Ph1601p	Pyrococcus horikoshii
R105A	mutation in ribonuclease P protein Ph1601p, mutation causes a significant reduction of the reconstituted RNase P activity as compared with that reconstituted by wild-type Ph1601p	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	-	strain OT3	-
Pyrococcus horikoshii OT-3	-	strain OT3	-

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)