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Literature summary extracted from
- tRNase Z (2007), Protein Pept. Lett., 14, 137-145.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.1.26.11 | crystal structure of different tRNase Z enzymes with regard to canonical sequence motifs reviewed, overview about substrate recognition and cleavage sites of tRNase Z given | Bacillus subtilis |
| 3.1.26.11 | crystal structure of different tRNase Z enzymes with regard to canonical sequence motifs reviewed, overview about substrate recognition and cleavage sites of tRNase Z given | Escherichia coli |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.26.11 | additional information | metal binding sites in tRNase Z and metallo-beta-lactamases described | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.26.11 | Arabidopsis thaliana | - |
tRNase Z, overview | - |
| 3.1.26.11 | Bacillus subtilis | - |
tRNase Z, overview | - |
| 3.1.26.11 | Escherichia coli | - |
tRNase Z, overview | - |
| 3.1.26.11 | Homo sapiens | - |
tRNase Z, overview | - |
| 3.1.26.11 | Methanocaldococcus jannaschii | - |
tRNase Z, overview | - |
| 3.1.26.11 | Synechocystis sp. | - |
PCC6803, tRNase Z, overview | - |
| 3.1.26.11 | Thermotoga maritima | - |
tRNase Z, overview | - |
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 reviewed | Escherichia coli |
| 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 reviewed, involvement in potential futile cycles in tRNA 3'-processing shown | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.26.11 | bis(p-nitrophenyl)phosphate + H2O | bpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated | Escherichia coli | p-nitrophenol + p-nitrophenyl phosphate | - |
? |  |
| 3.1.26.11 | thymidine-5-p-nitrophenyl phosphate + H2O | TpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated | Escherichia coli | p-nitrophenol + TMP | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.26.11 | tRNase Z | - |
Bacillus subtilis |
| 3.1.26.11 | tRNase Z | - |
Escherichia coli |
| 3.1.26.11 | tRNase Z | - |
Homo sapiens |
| 3.1.26.11 | tRNase Z | - |
Arabidopsis thaliana |
| 3.1.26.11 | tRNase Z | - |
Methanocaldococcus jannaschii |
| 3.1.26.11 | tRNase Z | - |
Synechocystis sp. |
| 3.1.26.11 | tRNase Z | - |
Thermotoga maritima |
| 3.1.26.11 | Trz | - |
Bacillus subtilis |
| 3.1.26.11 | Trz | - |
Escherichia coli |
| 3.1.26.11 | Trz | - |
Homo sapiens |
| 3.1.26.11 | Trz | - |
Arabidopsis thaliana |
| 3.1.26.11 | Trz | - |
Methanocaldococcus jannaschii |
| 3.1.26.11 | Trz | - |
Synechocystis sp. |
| 3.1.26.11 | Trz | - |
Thermotoga maritima |
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