S1ヌクレアーゼ
WordNet
- the 19th letter of the Roman alphabet (同)s
- general term for enzymes that catalyze the hydrolysis of nucleic acid by cleaving chains of nucleotides into smaller units
PrepTutorEJDIC
- sulfurの化学記号 / {略}South[ern]
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/15 12:00:55」(JST)
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| Aspergillus nuclease S1 |
| Identifiers |
| EC number |
3.1.30.1 |
| CAS number |
37288-25-8 |
| 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 |
|
Aspergillus nuclease S1 is an endonuclease enzyme derived from Aspergillus oryzae that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. This enzyme catalyses the following chemical reaction
- Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
Although its primary substrate is single-stranded, it can also occasionally introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. The enzyme hydrolyses single stranded region in duplex DNA such as loops or gaps.
Contents
- 1 Nomenclature
- 2 Properties
- 3 Uses
- 4 References
Nomenclature
Alternative names include EC 3.1.30.1, endonuclease S1 (Aspergillus), single-stranded-nucleate endonuclease, deoxyribonuclease S1, deoxyribonuclease S1, nuclease S1, Neurospora crassa single-strand specific endonuclease, S1 nuclease, single-strand endodeoxyribonuclease, single-stranded DNA specific endonuclease, single-strand-specific endodeoxyribonuclease, single strand-specific DNase and Aspergillus oryzae S1 nuclease.
Properties
Aspergillus nuclease S1 is a monomeric protein of a molecular weight of 38 kilodalton. It requires Zn2+ as a cofactor and is relatively stable against denaturing agents like urea, SDS, or formaldehyde. The optimum pH for its activity lies between 4-4.5. Aspergillus nuclease S1 is known to be inhibited somewhat by 50 μM ATP and nearly completely by 1 mM ATP.[1][2] 50% inhibition has been shown at 85 μM dAMP and 1 μM dATP but uninhibited by cAMP.[3]
Uses
Aspergillus nuclease S1 is used in the laboratory as a reagent in nuclease protection assays. In molecular biology, it is used in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA.
References
- ^ Yang, Xinjian; Fang Pu; Jinsong Ren; Xiaogang Qu (2011). "DNA-templated ensemble for label-free and real-time fluoresence turn-on detection of enzymatic/oxidative cleavage of single-stranded DNA". Chemical Communications 47: 8133–8135. doi:10.1039/c1cc12216a.
- ^ Wrede, Paul; Alexander Rich (1979). "Stability of the unique anticodon loop conformation of E.Col tRNAMetf". Nucleic Acids Research 7 (6). doi:10.1093/nar/7.6.1457.
- ^ Wiegand, RC; GN Godson; CM Radding (1975). "Specificity of the S1 nuclease from Aspergilus oryzae". The Journal of Biological Chemistry 250 (22).
|
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
|
|
| 3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
- 4-hydroxybenzoyl-CoA thioesterase
|
|
| 3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
|
|
| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- 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 |
|
|
| Exoribonuclease |
|
|
|
| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
|
|
| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
|
| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
|
|
|
|
|
Proteins: enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
UpToDate Contents
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English Journal
- A novel and efficient assay for identification and quantification of Acidithiobacillus ferrooxidans in bioleaching samples.
- Feng S, Xin Y, Yang H, Zhang L, Kang W, Xia X, Wang W.SourceThe Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, 214122, People's Republic of China.
- Journal of industrial microbiology & biotechnology.J Ind Microbiol Biotechnol.2012 Aug;39(8):1161-8. Epub 2012 Mar 20.
- Acidithiobacillus ferrooxidans is a Gram-negative, acidophilic, and chemolithotrophic bacterium that is active in bioleaching. The leaching efficacy is directly influenced by the biomass changes of this specie in bioleaching microbial community. In order to perform a simple and sensitive assay on A.
- PMID 22430501
- Human dna damage by the synergistic action of 4-aminobiphenyl and nitric oxide: An immunochemical study.
- Moinuddin, Dixit K, Ahmad S, Shahab U, Habib S, Naim M, Alam K, Ali A.SourceDepartment of Biochemistry, Faculty of Medicine, J.N. Medical College, Aligarh Muslim University, Aligarh, Uttar Pradesh, India. moin_u@rediffmail.com.
- Environmental toxicology.Environ Toxicol.2012 May 19. doi: 10.1002/tox.21782. [Epub ahead of print]
- 4-Aminobiphenyl (4-ABP), an aromatic amine is a major environmental carcinogen found mainly in cigarette smoke. It has been vastly implicated in mutagenesis and cancer development. In this study, commercially available human placental DNA was exposed to 4-ABP (1.3 mM) in presence of sodium nitroprus
- PMID 22610904
Japanese Journal
- Use of S1 nuclease in deep sequencing for detection of double-stranded RNA viruses
- Use of S1 nuclease in deep sequencing for detection of double-stranded RNA viruses
- The Plant S1-Like Nuclease Family Has Evolved a Highly Diverse Range of Catalytic Capabilities
Related Links
- S1 Nuclease 100,000 U ￥52,000 製品説明 本酵素は、一本鎖特異的endonucleaseであり、DNA、RNA共に酸可溶性5’-Pのヌクレオチドに分解する。最終的に90％以上5’-Pモノヌクレオチドに分解する。また二本鎖核酸中の一本鎖部分に ...
- Thermo Scientific S1 Nuclease degrades single-stranded nucleic acids, releasing 5'-phosphoryl mono- or oligonucleotides. It is five times more active on DNA than on RNA. S1 Nuclease also cleaves dsDNA at the single-stranded ...
★リンクテーブル★
[★]
- 英
- S1 nuclease
- 関
- アスペルギルスヌクレアーゼS1 Aspergillus nuclease S1
[★]
ヌクレアーゼ、核酸分解酵素
[★]