リボヌクレアーゼT1
- 関
- RNase T1
WordNet
- the 20th letter of the Roman alphabet (同)t
- a transferase that catalyzes the hydrolysis of ribonucleic acid (同)ribonucleinase, RNase
PrepTutorEJDIC
- tritiumの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/06 03:06:20」(JST)
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Not to be confused with ribonuclease T or ribonuclease T2.
| Ribonuclease T1 |
| Identifiers |
| EC number |
3.1.27.3 |
| CAS number |
9026-12-4 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
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| Ribonuclease T1 |
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Ribonuclease T1 from Aspergillus oryzae.[1]
|
| Identifiers |
| Symbol |
rntA |
| PDB |
1YGW |
| UniProt |
P00651 |
| Other data |
| EC number |
3.1.27.3 |
Ribonuclease T1 (EC 3.1.27.3, guanyloribonuclease, Aspergillus oryzae ribonuclease, RNase N1, RNase N2, ribonuclease N3, ribonuclease U1, ribonuclease F1, ribonuclease Ch, ribonuclease PP1, ribonuclease SA, RNase F1, ribonuclease C2, binase, RNase Sa, guanyl-specific RNase, RNase G, RNase T1, ribonuclease guaninenucleotido-2'-transferase (cyclizing), ribonuclease N3, ribonuclease N1) is a fungal endonuclease that cleaves single-stranded RNA after guanine residues, i.e., on their 3' end; the most commonly studied form of this enzyme is the version found in the mold Aspergillus oryzae. Owing to its specificity for guanine, RNase T1 is often used to digest denatured RNA prior to sequencing. Similar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for folding studies.[2]
Structurally, ribonuclease T1 is a small α+β protein (104 amino acids) with a four-stranded, antiparallel beta sheet covering a long alpha helix (almost five turns). RNase T1 has two disulfide bonds, Cys2-Cys10 and Cys6-Cys103, of which the latter contributes more to its folding stability;[3] complete reduction of both disulfides usually unfolds the protein, although its folding can be rescued with high salt concentrations.[4]
RNase T1 also has four prolines, two of which (Pro39 and Pro55) have cis isomers of their X-Pro peptide bonds. Nonnative isomers of these prolines can retard conformational folding dramatically,[5] folding on a characteristic time scale of 7,000 seconds (almost two hours) at 10°C and pH 5.[6]
References
- ^ PDB: 1ygw ; Pfeiffer S, Karimi-Nejad Y, Rüterjans H (1997). "Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study". Journal of Molecular Biology 266 (2): 400–423. doi:10.1006/jmbi.1996.0784. PMID 9047372.
- ^ Pace CN, Heinemann U, Hahn U, Saenger W (1991). "Ribonuclease T1: Structure, Function, and Stability". Angewandte Chemie 30 (4): 343–360. doi:10.1002/anie.199103433.
- ^ Pace CN, Grimsley GR, Thomson JA, Barnett BJ (1988). "Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds". Journal of Biological Chemistry 263 (24): 11820–11825. PMID 2457027.
- ^ Oobatake M, Takahashi S, Ooi T (1979). "Conformational stability of ribonuclease T1. II. Salt-induced renaturation". Journal of Biochemistry 86: 65–70.
- ^ Mayr LM, Odefey CO, Schutkowski M, Schmid FX (1996). "Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique". Biochemistry 35 (17): 5550–5561. doi:10.1021/bi953035y. PMID 8611546.
- ^ Mullins LS, Pace CN, Raushel FM (1997). "Conformational stability of ribonuclease T1 measured by hydrogen-deuterium exchange". Protein Science 6 (7): 1387–1395. doi:10.1002/pro.5560060702. PMC 2143755. PMID 9232639.
External links
- Ribonuclease T1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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Hydrolase: esterases (EC 3.1)
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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
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|
| 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
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| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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| 3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
| 3.1.11-16: Exonuclease |
| Exodeoxyribonuclease |
|
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| Exoribonuclease |
|
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| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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|
| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Poly A tail length analysis of in vitro transcribed mRNA by LC-MS.
- Beverly M1, Hagen C2, Slack O2.
- Analytical and bioanalytical chemistry.Anal Bioanal Chem.2018 Feb;410(6):1667-1677. doi: 10.1007/s00216-017-0840-6. Epub 2018 Jan 8.
- PMID 29313076
- Molecular Interpretation of Preferential Interactions in Protein Solvation: A Solvent-Shell Perspective by Means of Minimum-Distance Distribution Functions.
- Martínez L1, Shimizu S2.
- Journal of chemical theory and computation.J Chem Theory Comput.2017 Dec 12;13(12):6358-6372. doi: 10.1021/acs.jctc.7b00599. Epub 2017 Nov 21.
- PMID 29120639
- The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity.
- Taylor AJ1, Zakai SA2, Kelly DJ1.
- Frontiers in microbiology.Front Microbiol.2017 Mar 28;8:531. doi: 10.3389/fmicb.2017.00531. eCollection 2017.
- PMID 28400767
Japanese Journal
- X-Ray Crystallographic Structure of RNase Po1 That Exhibits Anti-tumor Activity
- Kobayashi Hiroko,Katsutani Takuya,Hara Yumiko,Motoyoshi Naomi,Itagaki Tadashi,Akita Fusamichi,Higashiura Akifumi,Yamada Yusuke,Inokuchi Norio,Suzuki Mamoru
- Biological and Pharmaceutical Bulletin 37(6), 968-978, 2014
- … RNase Po1 is a guanylic acid-specific ribonuclease member of the RNase T1 family from Pleurotus ostreatus. … We previously reported that RNase Po1 inhibits the proliferation of human tumor cells, yet RNase T1 and other T1 family RNases are non-toxic. … We determined the three-dimensional X-ray structure of RNase Po1 and compared it with that of RNase T1. …
- NAID 130004147340
- The Inhibition of Human Tumor Cell Proliferation by RNase Pol, a Member of the RNase T1 Family, from Pleurotus ostreatus
- KOBAYASHI Hiroko,MOTOYOSHI Naomi,ITAGAKI Tadashi [他],TABATA Keiichi,SUZUKI Takashi,INOKUCHI Norio
- Bioscience, biotechnology, and biochemistry 77(7), 1486-1491, 2013-07-23
- … RNase Po1 is a guanylic acid-specific ribonuclease (a RNase T1 family RNase) from Pleurotus ostreatus. … A comparison of the enzymatic properties of RNase Po1 and RNase T1 indicated that the optimum temperature for RNase Po1 activity was 20 °C higher than that for RNase T1. …
- NAID 10031190457
- Structure and function studies on enzymes with a catalytic carboxyl group(s) : from ribonuclease T₁ to carboxyl peptidases
- TAKAHASHI Kenji
- Proceedings of the Japan Academy, Series B 89(6), 201-225, 2013
- … This review follows mainly the trail of studies performed by the author and his colleagues on the structure and function of such enzymes, starting from ribonuclease T1, then extending to three major types of carboxyl peptidases including aspartic peptidases, glutamic peptidases and serine-carboxyl peptidases.<BR><BR>(Communicated by Shigekazu NAGATA, M.J.A.) …
- NAID 130003365117
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- ChemicalBook あなたのためにRIBONUCLEASE T1(9026-12-4)の化学的性質を提供して、融点、価格、蒸気圧、沸点、毒性、比重、沸点、密度、分子式、分子量、物理的な性質、毒性 税関のコードなどの情報、同時にあなたは更に ...
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- 関
- ribonuclease T1
[★]
- 英
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リボヌクレアーゼ