Ribonuclease Z

TRNase Z

Identifiers
EC number| 3.1.26.11
CAS number| 98148-84-6
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
| Search

PMC| articles
PubMed| articles
NCBI| proteins

TRNase Z (EC 3.1.26.11, 3 tRNase, tRNA 3 endonuclease, RNase Z, 3' tRNase) is an enzyme[1][2][3][4][5][6][7] that, among other things, catalyses the reactions involved in the maturation of tRNAs. Here, it endonucleolytically cleaves the RNA and removes extra 3' nucleotides from the tRNA precursor, generating the 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule. Similarly, it processes tRNA-like molecules such as mascRNA.[8]

## References

1. ↑ "Assigning a function to a conserved group of proteins: the tRNA 3'-processing enzymes". The EMBO Journal 21 (11): 2769–77. June 2002. doi:10.1093/emboj/21.11.2769. PMID 12032089.
2. ↑ "tRNA 3' processing in plants: nuclear and mitochondrial activities differ". Biochemistry 39 (8): 2096–105. February 2000. doi:10.1021/bi992253e. PMID 10684660.
3. ↑ "The plant tRNA 3' processing enzyme has a broad substrate spectrum". Biochemistry 40 (28): 8264–72. July 2001. doi:10.1021/bi0101953. PMID 11444972.
4. ↑ "5' end maturation and RNA editing have to precede tRNA 3' processing in plant mitochondria". Proceedings of the National Academy of Sciences of the United States of America 95 (1): 108–13. January 1998. doi:10.1073/pnas.95.1.108. PMID 9419337.
5. ↑ "The final cut. The importance of tRNA 3'-processing". EMBO Reports 2 (1): 17–20. January 2001. doi:10.1093/embo-reports/kve006. PMID 11252717.
6. ↑ "A novel endonucleolytic mechanism to generate the CCA 3' termini of tRNA molecules in Thermotoga maritima". The Journal of Biological Chemistry 279 (15): 15688–97. April 2004. doi:10.1074/jbc.M313951200. PMID 14749326.
7. ↑ "A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease". Nucleic Acids Research 31 (9): 2272–8. May 2003. doi:10.1093/nar/gkg337. PMID 12711671.
8. ↑ "3' end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA". Cell 135 (5): 919–32. November 2008. doi:10.1016/j.cell.2008.10.012. PMID 19041754.

## External links

* TRNase+Z at the US National Library of Medicine Medical Subject Headings (MeSH)

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Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases|

* Cholinesterase
* Acetylcholinesterase
* Butyrylcholinesterase
* Pectinesterase
* 6-phosphogluconolactonase
* PAF acetylhydrolase

* Lipase
* Bile salt-dependent
* Gastric/Lingual
* Pancreatic
* Lysosomal
* Hormone-sensitive
* Endothelial
* Hepatic
* Lipoprotein
* Monoacylglycerol
* Diacylglycerol

* Phospholipase
* A1
* A2
* B

* Cutinase
* PETase

3.1.2: Thioesterase|

* Palmitoyl protein thioesterase
* Ubiquitin carboxy-terminal hydrolase L1
* 4-hydroxybenzoyl-CoA thioesterase

3.1.3: Phosphatase|

* Alkaline phosphatase
* ALPI
* ALPL
* ALPP
* Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
* Nucleotidase
* Glucose 6-phosphatase
* Fructose 1,6-bisphosphatase
* Calcineurin
* Protein phosphatase
* PP2A
* OCRL
* Pyruvate dehydrogenase phosphatase
* fructose 2,6-bisphosphatase
* PTEN
* Phytase
* Beta-propeller phytase
* Inositol-phosphate phosphatase
* IMPA1, IMPA2, IMPA3
* Protein phosphatase: Protein tyrosine phosphatase
* Protein serine/threonine phosphatase
* Dual-specificity phosphatase

3.1.4:
Phosphodiesterase|

* Autotaxin
* Phospholipase
* C
* D
* Sphingomyelin phosphodiesterase
* 1
* PDE1
* PDE2
* PDE3
* PDE4A/PDE4B
* PDE5
* Lecithinase (Clostridium perfringens alpha toxin)
* Cyclic nucleotide phosphodiesterase

3.1.6: Sulfatase|

* arylsulfatase
* Arylsulfatase A
* Arylsulfatase B
* Arylsulfatase E
* Steroid sulfatase
* Galactosamine-6 sulfatase
* Iduronate-2-sulfatase
* N-acetylglucosamine-6-sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)|

| 3.1.11-16:
Exonuclease|

| Exodeoxyribonuclease|

* RecBCD

|

Exoribonuclease|

* Oligonucleotidase

3.1.21-31:
Endonuclease|

| Endodeoxyribonuclease|

* Deoxyribonuclease I
* Deoxyribonuclease II
* Deoxyribonuclease IV
* Restriction enzyme
* UvrABC endonuclease

|

Endoribonuclease|

* RNase III
* RNase H
* 1
* 2A
* 2B
* 2C
* RNase P
* RNase A
* 1
* 2
* 3
* 4/5
* RNase T1
* RNA-induced silencing complex

either deoxy- or ribo-  |

* Nuclease S1
* Mung bean nuclease
* Serratia marcescens nuclease
* Micrococcal nuclease

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Catalytically perfect enzyme
* Coenzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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