グアニリルトランスフェラーゼ、グアニル酸転移酵素
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/06/30 20:33:08」(JST)
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Guanylyl transferases are enzymes that transfer a guanosine monophosphate (GMP; also known as guanylic acid) group, usually from GTP to another molecule, releasing pyrophosphate. Many eukaryotic guanylyl transferases are capping enzymes that catalyze the formation of the 5' cap in the co-transcriptional modification of messenger RNA. Because the 5' end of the RNA molecule ends in a phosphate group, the bond formed between the RNA and the GTP molecule is an unusual 5'-5' triphosphate linkage, instead of the 3'-5' linkages between the other nucleotides that form an RNA strand. In capping enzymes, a highly conserved lysine residue serves as the catalytic residue that forms a covalent enzyme-GMP complex.[1]
The transfer RNA (tRNA) for histidine is unique among eukaryotic tRNAs in requiring the addition of a guanine nucleotide before being aminoacylated by the histidine tRNA synthetase. The yeast guanylyl transferase specific to tRNAHis is unique in being the only known non-tRNA synthetase enzyme that specifically recognizes the tRNA anticodon.[2]
Guanylyl transferases also exist for transferring guanosine nucleotides to sugar molecules, such as mannose and fucose.
See also
External links
- EC number 2.7.7.- - nucleotidyltransferases
References
- ^ Fresco LD, Buratowski S. (1994). Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases. Proc Natl Acad Sci USA 91(14): 6624–6628.
- ^ Jackman JE, Phizicky EM. (2006). tRNAHis guanylyltransferase adds G–1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. RNA 12:1007-1014.
Transferases: phosphorus-containing groups (EC 2.7)
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2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
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|
2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate kinase
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2.7.3: N acceptor |
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2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
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|
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2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
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2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
Polymerase |
DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
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|
RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
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Phosphorolytic
3' to 5' exoribonuclease |
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Nucleotidyltransferase |
- UTP—glucose-1-phosphate uridylyltransferase
- Galactose—1-phosphate uridylyltransferase
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Guanylyltransferase |
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Other |
- Recombinase (Integrase)
- Transposase
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2.7.8: miscellaneous |
Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
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Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
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2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
2.7.10: protein-tyrosine |
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2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
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2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
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2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
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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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English Journal
- Genome sequence and analysis of a broad-host range lytic bacteriophage that infects the Bacillus cereus group.
- El-Arabi TF, Griffiths MW, She YM, Villegas A, Lingohr EJ, Kropinski AM.SourcePublic Health Agency of Canada, Laboratory for Foodborne Zoonoses, Guelph, ON, N1G 3W4, Canada.
- Virology journal.Virol J.2013 Feb 7;10:48. doi: 10.1186/1743-422X-10-48.
- BACKGROUND: Comparatively little information is available on members of the Myoviridae infecting low G+C content, Gram-positive host bacteria of the family Firmicutes. While numerous Bacillus phages have been isolated up till now only very few Bacillus cereus phages have been characterized in detail
- PMID 23388049
- In vitro capping and transcription of rhabdoviruses.
- Ogino T.SourceDepartment of Molecular Genetics, Section of Virology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA. oginot@ccf.org
- Methods (San Diego, Calif.).Methods.2013 Feb;59(2):188-98. doi: 10.1016/j.ymeth.2012.05.013. Epub 2012 Jun 8.
- The RNA-dependent RNA polymerase L protein of vesicular stomatitis virus (VSV), a prototypic nonsegmented negative strand (NNS) RNA virus classified into the Rhabdoviridae family, has been used to investigate the fundamental molecular mechanisms of NNS RNA viral mRNA synthesis and processing. In vit
- PMID 22687619
- Absence of a universal element for tRNAHis identity in Acanthamoeba castellanii.
- Rao BS, Mohammad F, Gray MW, Jackman JE.SourceDepartment of Chemistry and Biochemistry and Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
- Nucleic acids research.Nucleic Acids Res.2013 Feb 1;41(3):1885-94. doi: 10.1093/nar/gks1242. Epub 2012 Dec 14.
- The additional G(-1) nucleotide on tRNA(His) is a nearly universal feature that specifies tRNA(His) identity in all three domains of life. In eukaryotes, the G(-1) identity element is obtained by a post-transcriptional pathway, through the unusual 3'-5' polymerase activity of the highly conserved tR
- PMID 23241387
Japanese Journal
- ヌクレオチドを3末端から5末端方向へと伸長する酵素の作用原理
- 中村 彰良
- 日本結晶学会誌 56(6), 399-404, 2014
- … During tRNA maturation tRNAHis guanylyltransferase (Thg1) catalyzes the untemplated 3-5 addition of a G to the tRNA 5-end. …
- NAID 130004799695
- Sequence Analysis and GTP-Binding Ability of the Minor Core Protein P5 of Rice Gall Dwarf Virus
- ICHIMI Kenzaburo,KIKUCHI Akira,MORIYASU Yusuke,ZHONG Boxiong,HAGIWARA Kyoji,KAMIUNTEN Hiroshi,OMURA Toshihiro
- Japan Agricultural Research Quarterly: JARQ 36(2), 83-87, 2002
- … Although no overall homology was found to any other proteins, including those of animal-infecting reoviruses, P5 of RGDV exhibited a significant homology to P5 of Rice dwarf virus (50%), which might be a guanylyltransferase, and to P5 of Wound tumor virus (55%). …
- NAID 130004886238
- Studies on Dinucleoside Polyphosphates: Some Intriguing Biochemical, Physiological, and Medical Aspects.:Some Intriguing Biochemical, Physiological, and Medical Aspects
- GURANOWSKI Andrzej
- Journal of Clinical Biochemistry and Nutrition 28(3), 177-189, 2000
- … So far, the only known specific enzyme that catalyzes the synthesis of these polyphosphates is GTP:GTP guanylyltransferase. …
- NAID 130003670529
Related Links
- BARTLETT GR. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar; 234 (3):466–468. [PubMed] Itoh N, Mizumoto K, Kaziro Y. Partial purification and characterization of mRNA guanylyltransferase from ...
- Proc. Natl. Acad. Sci. USA Vol. 78, No. 1, pp. 187-191, January 1981 Biochemistry Mechanism of mRNA capping by vaccinia virus guanylyltransferase: Characterization of an enzyme-guanylate intermediate (covalent catalysis)
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