ファニルアラニンtRNAリガーゼ
- 関
- phenylalanyl-tRNA synthetase
WordNet
- an essential amino acid found in proteins and needed for growth of children and for protein metabolism in children and adults; abundant in milk and eggs; it is normally converted to tyrosine in the human body
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/19 01:30:46」(JST)
[Wiki en表示]
| phenylalanine-tRNA ligase |
| Identifiers |
| EC number |
6.1.1.20 |
| CAS number |
9055-66-7 |
| 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 |
|
| Ferredoxin-fold anticodon binding domain |
|
the crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNAPhe
|
| Identifiers |
| Symbol |
FDX-ACB |
| Pfam |
PF03147 |
| InterPro |
IPR005121 |
| SCOP |
1pys |
| SUPERFAMILY |
1pys |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
In enzymology, a phenylalanine-tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction
- ATP + L-phenylalanine + tRNAPhe AMP + diphosphate + L-phenylalanyl-tRNAPhe
The 3 substrates of this enzyme are ATP, L-phenylalanine, and tRNAPhe, whereas its 3 products are AMP, diphosphate, and L-phenylalanyl-tRNAPhe.
This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. The systematic name of this enzyme class is L-phenylalanine:tRNAPhe ligase (AMP-forming). Other names in common use include phenylalanyl-tRNA synthetase, phenylalanyl-transfer ribonucleate synthetase, phenylalanine-tRNA synthetase, phenylalanyl-transfer RNA synthetase, phenylalanyl-tRNA ligase, phenylalanyl-transfer RNA ligase, L-phenylalanyl-tRNA synthetase, and phenylalanine translase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-tRNA biosynthesis.
Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it.[1][2][3][4][5]
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1B70, 1B7Y, 1EIY, 1JJC, 1PYS, 2AKW, 2ALY, 2AMC, 2CXI, and 2IY5.
References
- ^ Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG (July 1995). "Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus". Nat. Struct. Biol. 2 (7): 537–47. doi:10.1038/nsb0795-537. PMID 7664121.
- ^ Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M (January 1997). "The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe". Structure 5 (1): 59–68. doi:10.1016/s0969-2126(97)00166-4. PMID 9016717.
- ^ Rodova M, Ankilova V, Safro MG (February 1999). "Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells". Biochem. Biophys. Res. Commun. 255 (3): 765–73. doi:10.1006/bbrc.1999.0141. PMID 10049785.
- ^ Moor N, Lavrik O, Favre A, Safro M (September 2003). "Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end". Biochemistry 42 (36): 10697–708. doi:10.1021/bi034732q. PMID 12962494.
- ^ Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M (July 2008). "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase". Structure 16 (7): 1095–104. doi:10.1016/j.str.2008.03.020. PMID 18611382.
Further reading
- Stulberg MP (1967). "The isolation and properties of phenylalanyl ribonucleic acid synthetase from Escherichia coli B". J. Biol. Chem. 242 (5): 1060–4. PMID 5335910.
|
Enzymes: CO CS and CN ligases (EC 6.1-6.3)
|
|
| 6.1: Carbon-Oxygen |
- Aminoacyl tRNA synthetase
- Alanine
- Arginine
- Asparagine
- Aspartate
- Cysteine
- D-alanine—poly(phosphoribitol) ligase
- Glutamate
- Glutamine
- Glycine
- Histidine
- Isoleucine
- Leucine
- Lysine
- Methionine
- Phenylalanine
- Proline
- Serine
- Threonine
- Tryptophan
- Tyrosine
- Valine
|
|
| 6.2: Carbon-Sulfur |
- Succinyl coenzyme A synthetase
- Acetyl—CoA synthetase
- Long-chain-fatty-acid—CoA ligase
|
|
| 6.3: Carbon-Nitrogen |
- Glutamine synthetase
- Ubiquitin ligase
- Cullin
- Von Hippel–Lindau tumor suppressor
- UBE3A
- Mdm2
- Anaphase-promoting complex
- UBR1
- Glutathione synthetase
- CTP synthetase
- Adenylosuccinate synthase
- Argininosuccinate synthase
- Holocarboxylase synthetase
- GMP synthase
- Asparagine synthetase
- Carbamoyl phosphate synthetase
- Glutamate–cysteine ligase
|
|
- 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
|
|
|
|
|
Ligases: carbon-carbon ligases (EC 6.4)
|
|
| Biotin dependent carboxylation |
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- Propionyl-CoA carboxylase
- Methylcrotonyl-CoA carboxylase
|
|
| Other |
|
|
- 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
|
|
|
|
|
Enzymes: Phosphoric ester and nitrogen-metal ligases (EC 6.5-6.6)
|
|
| 6.5: Phosphoric Ester |
|
|
| 6.6: Nitrogen-Metal |
- Magnesium chelatase
- Cobalt chelatase
|
|
- 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
|
|
|
|
This article incorporates text from the public domain Pfam and InterPro IPR005121
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.
- Englander MT1, Avins JL2, Fleisher RC2, Liu B3, Effraim PR1, Wang J2, Schulten K4, Leyh TS5, Gonzalez RL Jr6, Cornish VW6.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 May 12;112(19):6038-43. doi: 10.1073/pnas.1424712112. Epub 2015 Apr 27.
- The cellular translational machinery (TM) synthesizes proteins using exclusively L- or achiral aminoacyl-tRNAs (aa-tRNAs), despite the presence of D-amino acids in nature and their ability to be aminoacylated onto tRNAs by aa-tRNA synthetases. The ubiquity of L-amino acids in proteins has led to the
- PMID 25918365
- Universal pathway for posttransfer editing reactions: insights from the crystal structure of TtPheRS with puromycin.
- Tworowski D1, Klipcan L2, Peretz M1, Moor N3, Safro MG4.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Mar 31;112(13):3967-72. doi: 10.1073/pnas.1414852112. Epub 2015 Mar 16.
- At the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge of discrimination between cognate phenylalanine and closely similar noncognate tyrosine. Resampling of Tyr-tRNA(Phe) to PheRS increasing the number of correctly charged tRNA molecules has recentl
- PMID 25775602
- Plasmodium falciparum mitochondria import tRNAs along with an active phenylalanyl-tRNA synthetase.
- Sharma A1, Sharma A1.
- The Biochemical journal.Biochem J.2015 Feb 1;465(3):459-69. doi: 10.1042/BJ20140998.
- The Plasmodium falciparum protein translation enzymes aminoacyl-tRNA synthetases (aaRSs) are an emergent family of drug targets. The aaRS ensemble catalyses transfer of amino acids to cognate tRNAs, thus providing charged tRNAs for ribosomal consumption. P. falciparum proteome expression relies on a
- PMID 25391660
Japanese Journal
- L-Phenylalanine: tRNA ligase of Escherichia coli K10.A rapid kinetic investigation of the catalytic reaction.
Related Links
- Phenylalanine--tRNA ligase antibody comparison selector. A list of Phenylalanine--tRNA ligase antibodies and Phenylalanine--tRNA ligase antibody suppliers to help you quickly choose the most appropriate Phenylalanine--tRNA ...
- References for "Phenylalanine-tRNA ligase" im Internet, an Universitäten und in der Literatur... cyclopaedia.net ... In enzymology, a phenylalanine-tRNA ligase (EC 6.1.1.20) is an enzyme that catalyzes the chemical reaction ATP + L ...
★リンクテーブル★
[★]
フェニルアラニルtRNA合成酵素、フェニルアラニルtRNAシンテターゼ
- 関
- phenylalanine-tRNA ligase
[★]
- 英
- phenylalanine-tRNA ligase
- 関
- フェニルアラニルtRNA合成酵素
[★]
トランスファーRNA, transfer RNA, 転位RNA
[★]
リガーゼ、連結酵素
- 関
- synthetase
[★]
トランスファーRNA transfer RNAs
[★]
tRNAリガーゼ
- 関
- RNA ligase
[★]
フェニルアラニン