Deoxyribonuclease II: Difference between revisions
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'''Deoxyribonuclease II''' ({{EC number|3.1.22.1}}, ''[[DNase]] II'', ''pancreatic DNase II'', ''deoxyribonucleate 3'-nucleotidohydrolase'', ''pancreatic DNase II'', ''acid deoxyribonuclease'', ''acid DNase'') hydrolyzes [[deoxyribonucleotide]] | '''Deoxyribonuclease II''' ({{EC number|3.1.22.1}}, ''[[DNase]] II'', ''pancreatic DNase II'', ''deoxyribonucleate 3'-nucleotidohydrolase'', ''pancreatic DNase II'', ''acid deoxyribonuclease'', ''acid DNase'') is an endonuclease that hydrolyzes phosphodiester linkages of [[deoxyribonucleotide]] in native and denatured [[DNA]], yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism.<ref name = "Bernardi_1971">{{cite book | vauthors = Bernardi G | chapter = Chapter 11: Spleen Acid Deoxyribonuclease| veditors = Boyer PD | title = The Enzymes | volume = 4 |date=1971|publisher=Elsevier Science|location=New York|isbn=978-0-12-122704-3|edition=3rd|doi=10.1016/S1874-6047(08)60371-6 | pages = 271–287 }}</ref> As the name implies, it functions optimally at [[acid]] [[pH]] because it is commonly found in low pH environment of [[Lysosome|lysosomes]]. | ||
The action of DNase occurs in three phases. The initial phase introduces multiple nicks in the [[phosphodiester backbone]]. The second phase produces acid-soluble nucleotides. The third phase, which is the terminal phase, consists of [[hyperchromic shift]] resulting from reduction of oligonucleotides. <ref name="Bernardi_1971" /> | |||
There are several known [[DNase]]s II, including: | There are several known [[DNase]]s II, including: | ||
* DNase II alpha (usually | * DNase II alpha (usually known as DNase II), which is thought to be ubiquitously expressed in human tissue<ref>{{cite journal | vauthors = Yasuda T, Takeshita H, Iida R, Tsutsumi S, Nakajima T, Hosomi O, Nakashima Y, Mori S, Kishi K | title = Structure and organization of the human deoxyribonuclease II (DNase II) gene | journal = Annals of Human Genetics | volume = 62 | issue = Pt 4 | pages = 299–305 | date = July 1998 | pmid = 9924608 | doi = 10.1046/j.1469-1809.1998.6240299.x }}</ref>. It has been shown that a mutation in this enzyme of mice leads to DNA degradation by apoptosis.<ref name="pmid28369538">{{cite journal | vauthors = Varela-Ramirez A, Abendroth J, Mejia AA, Phan IQ, Lorimer DD, Edwards TE, Aguilera RJ | title = Structure of acid deoxyribonuclease | journal = Nucleic Acids Research | volume = 45 | issue = 10 | pages = 6217–6227 | date = June 2017 | pmid = 28369538 | pmc = 5449587 | doi = 10.1093/nar/gkx222 }}</ref> | ||
* DNase II beta (also called DLAD, or DNase II-Like Acid DNase) | * DNase II beta (also called DLAD, or DNase II-Like Acid DNase), which is mainly expressed in the [[eye lens]] and [[salivary glands]]. One of its functions is to clear DNA from eye lens. Low levels have also been detected in the lung, prostate and lymph nodes.<ref>{{UniProt Full|Q8WZ79|DNASE2B - Deoxyribonuclease-2-beta precursor - Homo sapiens (Human) - DNASE2B gene & protein}}</ref> Deficiency of this enzyme in mice lead to the development of cataracts. | ||
==References== | |||
<references /> | |||
==External links== | ==External links== | ||
Latest revision as of 08:12, 17 May 2018
| deoxyribonuclease II alpha | |
|---|---|
| Identifiers | |
| Symbol | DNASE2 |
| Alt. symbols | DNASE2A, DRN2, DNL, DNL2 |
| Entrez | 1777 |
| HUGO | 2960 |
| OMIM | 126350 |
| RefSeq | NM_001375 |
| UniProt | O00115 |
| Other data | |
| EC number | 3.1.22.1 |
| Locus | Chr. 19 p13.2 |
| deoxyribonuclease II beta | |
|---|---|
| Identifiers | |
| Symbol | DNASE2B |
| Entrez | 58511 |
| HUGO | 28875 |
| OMIM | 608057 |
| RefSeq | NM_021233 |
| UniProt | Q8WZ79 |
| Other data | |
| EC number | 3.1.22.1 |
| Locus | Chr. 1 p22.3 |
Deoxyribonuclease II (EC 3.1.22.1, DNase II, pancreatic DNase II, deoxyribonucleate 3'-nucleotidohydrolase, pancreatic DNase II, acid deoxyribonuclease, acid DNase) is an endonuclease that hydrolyzes phosphodiester linkages of deoxyribonucleotide in native and denatured DNA, yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism.[1] As the name implies, it functions optimally at acid pH because it is commonly found in low pH environment of lysosomes.
The action of DNase occurs in three phases. The initial phase introduces multiple nicks in the phosphodiester backbone. The second phase produces acid-soluble nucleotides. The third phase, which is the terminal phase, consists of hyperchromic shift resulting from reduction of oligonucleotides. [1]
There are several known DNases II, including:
- DNase II alpha (usually known as DNase II), which is thought to be ubiquitously expressed in human tissue[2]. It has been shown that a mutation in this enzyme of mice leads to DNA degradation by apoptosis.[3]
- DNase II beta (also called DLAD, or DNase II-Like Acid DNase), which is mainly expressed in the eye lens and salivary glands. One of its functions is to clear DNA from eye lens. Low levels have also been detected in the lung, prostate and lymph nodes.[4] Deficiency of this enzyme in mice lead to the development of cataracts.
References
- ↑ 1.0 1.1 Bernardi G (1971). "Chapter 11: Spleen Acid Deoxyribonuclease". In Boyer PD. The Enzymes. 4 (3rd ed.). New York: Elsevier Science. pp. 271–287. doi:10.1016/S1874-6047(08)60371-6. ISBN 978-0-12-122704-3.
- ↑ Yasuda T, Takeshita H, Iida R, Tsutsumi S, Nakajima T, Hosomi O, Nakashima Y, Mori S, Kishi K (July 1998). "Structure and organization of the human deoxyribonuclease II (DNase II) gene". Annals of Human Genetics. 62 (Pt 4): 299–305. doi:10.1046/j.1469-1809.1998.6240299.x. PMID 9924608.
- ↑ Varela-Ramirez A, Abendroth J, Mejia AA, Phan IQ, Lorimer DD, Edwards TE, Aguilera RJ (June 2017). "Structure of acid deoxyribonuclease". Nucleic Acids Research. 45 (10): 6217–6227. doi:10.1093/nar/gkx222. PMC 5449587. PMID 28369538.
- ↑ Universal protein resource accession number Q8WZ79 for "DNASE2B - Deoxyribonuclease-2-beta precursor - Homo sapiens (Human) - DNASE2B gene & protein" at UniProt.
External links
- deoxyribonuclease+II at the US National Library of Medicine Medical Subject Headings (MeSH)
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