Endonuclease V - Misplaced Pages

This article is about an enzyme. For a different enzyme also sometimes referred to as endonuclease V, see deoxyribodipyrimidine endonucleosidase.

Endonuclease V

Crystallographic structure of Thermotoga maritima endoV (blue) in complex with DNA (green and orange). The deamidated base is shown in yellow.

Identifiers

Symbol

ENDOV

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Endonuclease V (endoV) is a highly conserved endonuclease enzyme family. The primary function of endoV differs significantly in prokaryotes and eukaryotes, as suggested by studies on the E. coli and human orthologs.

In prokaryotes endoV is primarily a deoxyribonuclease involved in DNA repair of deoxyinosine introduced into the genome by deamidation of adenine bases (EC 3.1.21.7). However, it has broad substrate specificity and can also act on other types of DNA lesions as well as on inosine-containing RNA.

In eukaryotes endoV is primarily a ribonuclease and cleaves single-stranded RNA at the 3' position relative to an inosine base, which may be present due to RNA editing by deaminase enzymes (EC 3.1.26.-). The human endoV localizes to the cytoplasm and nucleoli, suggesting a possible role in processes involving ribosomal RNA. The human gene symbol is ENDOV.

References

Dalhus B, Arvai AS, Rosnes I, Olsen ØE, Backe PH, Alseth I, Gao H, Cao W, Tainer JA, Bjørås M (February 2009). "Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair". Nature Structural & Molecular Biology. 16 (2): 138–43. doi:10.1038/nsmb.1538. PMC 3560532. PMID 19136958.
^ Vik ES, Nawaz MS, Strøm Andersen P, Fladeby C, Bjørås M, Dalhus B, Alseth I (2013). "Endonuclease V cleaves at inosines in RNA". Nature Communications. 4: 2271. Bibcode:2013NatCo...4.2271S. doi:10.1038/ncomms3271. PMC 3741635. PMID 23912683.
^ Fladeby C, Vik ES, Laerdahl JK, Gran Neurauter C, Heggelund JE, Thorgaard E, Strøm-Andersen P, Bjørås M, Dalhus B, Alseth I (2012). "The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures". PLOS ONE. 7 (11): e47466. Bibcode:2012PLoSO...747466F. doi:10.1371/journal.pone.0047466. PMC 3489907. PMID 23139746.
Morita Y, Shibutani T, Nakanishi N, Nishikura K, Iwai S, Kuraoka I (2013). "Human endonuclease V is a ribonuclease specific for inosine-containing RNA". Nature Communications. 4: 2273. Bibcode:2013NatCo...4.2273M. doi:10.1038/ncomms3273. PMC 3741642. PMID 23912718.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: 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;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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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