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

BRENDA support

Literature summary for 3.1.26.5 extracted from

  • Walker, S.C.; Engelke, D.R.
    A protein-only RNase P in human mitochondria (2008), Cell, 135, 412-414.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.5

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the human mitochondrial RNase P is an entirely protein-based enzyme, protein MRPP1, a probable tRNA methylase, provides tRNA-binding specificity to the RNase P enzyme, protein MRPP2 binds tightly to MRPP1 and is a member of the short chain dehydrogenase/reductase protein family, protein MRPP3 may provide the enzymatic cleavage activity for the patchwork enzyme Homo sapiens ?
-
 ?
pre-tRNA + H2O
-
 Homo sapiens tRNA + 5'-oligoribonucleotide
-
 ?

Synonyms

Synonyms Comment Organism
RNase P the human mitochondrial RNase P is an entirely protein-based enzyme Homo sapiens