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Literature summary extracted from

  • Spaeth, B.; Canino, G.; Marchfelder, A.
    tRNase Z: the end is not in sight (2007), Cell. Mol. Life Sci., 64, 2404-2412.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.26.11 additional information variants of tRNase Z enzymes generated by mutagenesis and properties of variants reviewed Arabidopsis thaliana

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.11 additional information overview of the metal ion content in the active sites of tRNase Z and metallo-beta-lactamases, metal ion requirement by cleavage of bis(p-nitrophenyl)phosphate indicated, structure of metal binding site described, key residues of the zinc site identified by mutational studies summarized Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.11 Arabidopsis thaliana
-
 features of tRNase Z reviewed
-
3.1.26.11 Caenorhabditis elegans
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Danio rerio
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Drosophila melanogaster Q8MKW7 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Gallus gallus
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Homo sapiens
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Mus musculus
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Neurospora crassa
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Saccharomyces cerevisiae
-
 distribution of short and long forms of tRNase Z reviewed
-
3.1.26.11 Schizosaccharomyces pombe
-
 distribution of short and long forms of tRNase Z reviewed
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.26.11 additional information
-
 in vitro processing activities of different recombinant tRNase Z enzymes with respect to CCA-containing and CCA-less pre-tRNAs summarized Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.11 bis(p-nitrophenyl)phosphate + H2O differentiation of tRNase Z variants by the substrate bis(p-nitrophenyl)phosphate (bpNPP) described, smallest known tRNase Z substrate Arabidopsis thaliana p-nitrophenol + p-nitrophenyl phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.26.11 tRNase Z
-
 Gallus gallus
3.1.26.11 tRNase Z
-
 Mus musculus
3.1.26.11 tRNase Z
-
 Homo sapiens
3.1.26.11 tRNase Z
-
 Saccharomyces cerevisiae
3.1.26.11 tRNase Z
-
 Neurospora crassa
3.1.26.11 tRNase Z
-
 Arabidopsis thaliana
3.1.26.11 tRNase Z
-
 Schizosaccharomyces pombe
3.1.26.11 tRNase Z
-
 Caenorhabditis elegans
3.1.26.11 tRNase Z
-
 Danio rerio
3.1.26.11 tRNase Z
-
 Drosophila melanogaster
3.1.26.11 Trz
-
 Gallus gallus
3.1.26.11 Trz
-
 Mus musculus
3.1.26.11 Trz
-
 Homo sapiens
3.1.26.11 Trz
-
 Saccharomyces cerevisiae
3.1.26.11 Trz
-
 Neurospora crassa
3.1.26.11 Trz
-
 Arabidopsis thaliana
3.1.26.11 Trz
-
 Schizosaccharomyces pombe
3.1.26.11 Trz
-
 Caenorhabditis elegans
3.1.26.11 Trz
-
 Danio rerio
3.1.26.11 Trz
-
 Drosophila melanogaster