tyrosine-tRNA ligase

チロシンtRNAリガーゼ

関

tyrosyl-tRNA synthetase

WordNet

1. an amino acid found in most proteins; a precursor of several hormones

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/11/27 09:27:43」(JST)

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tyrosine-tRNA ligase
Identifiers
EC number	6.1.1.1
CAS number	9023-45-4
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

In enzymology, a tyrosine-tRNA ligase (EC 6.1.1.1) is an enzyme that catalyzes the chemical reaction

ATP + L-tyrosine + RNA AMP + diphosphate + L-tyrosyl-tRNATyr

The 3 substrates of this enzyme are ATP, L-tyrosine, and RNA, whereas its 3 products are AMP, diphosphate, and L-tyrosyl-tRNA(Tyr).

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-tyrosine:tRNATyr ligase (AMP-forming). This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis and aminoacyl-trna biosynthesis.

Structural studies

As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes 1H3E, 1J1U, 1JH3, 1JII, 1JIJ, 1JIK, 1JIL, 1N3L, 1NTG, 1Q11, 1TYA, 1TYB, 1TYC, 1TYD, 1U7D, 1U7X, 1VBM, 1VBN, 1WQ3, 1WQ4, 1X8X, 1Y42, 1ZH0, 1ZH6, 2AG6, 2CYA, 2CYB, 2CYC, 2DLC, 2HGZ, 2J5B, 2TS1, 3TS1, and 4TS1.

References

• ALLEN EH, GLASSMAN E, SCHWEET RS (1960). "Incorporation of amino acids into ribonucleic acid. I. The role of activating enzymes". J. Biol. Chem. 235: 1061–7. PMID 13792726. 
• Cowles JR, Key JL (1972). "Demonstration of two tyrosyl-tRNA synthetases of pea roots". Biochim. Biophys. Acta. 281 (1): 33–44. doi:10.1016/0005-2787(72)90185-2. PMID 4563531. 
• HOLLEY RW, BRUNNGRABER EF, SAAD F, WILLIAMS HH (1961). "Partial purification of the threonine- and tyrosine-activating enzymes from rat liver, and the effect of patassium ions on the activity of the tyrosine enzyme". J. Biol. Chem. 236: 197–9. PMID 13715350. 
• Schweet RS and Allen EH (1958). "Purification and properties of tyrosine-activating enzyme of hog pancreas". J. Biol. Chem. 233: 1104–1108. PMID 13598741. 
• Brick P, Bhat TN, Blow DM (1989). "Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution Interaction of the enzyme with the tyrosyl adenylate intermediate". J. Mol. Biol. 208 (1): 83–98. doi:10.1016/0022-2836(89)90090-9. PMID 2504923. 

UpToDate Contents

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English Journal

• Altering the Enantioselectivity of Tyrosyl-tRNA Synthetase by Insertion of a Stereospecific Editing Domain.

• Richardson CJ1, First EA1.
• Biochemistry.Biochemistry.2016 Mar 15;55(10):1541-53. doi: 10.1021/acs.biochem.5b01167. Epub 2016 Mar 2.
• Translation of mRNAs by the ribosome is stereospecific, with only l-amino acids being incorporated into the nascent polypeptide chain. This stereospecificity results from the exclusion of d-amino acids at three steps during protein synthesis: (1) the aminoacylation of tRNA by aminoacyl-tRNA syntheta
• PMID 26890980

• Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase.

• Wei Z1, Xu Z2, Liu X3, Lo WS2, Ye F3, Lau CF2, Wang F2, Zhou JJ2, Nangle LA4, Yang XL5, Zhang M6, Schimmel P7.
• Nucleic acids research.Nucleic Acids Res.2016 Feb 18;44(3):1247-55. doi: 10.1093/nar/gkw002. Epub 2016 Jan 14.
• Many human tRNA synthetases evolved alternative functions outside of protein synthesis. These functions are associated with over 200 splice variants (SVs), most of which are catalytic nulls that engender new biology. While known to regulate non-translational activities, little is known about structu
• PMID 26773056

• Protein:Ligand binding free energies: A stringent test for computational protein design.

• Druart K1, Palmai Z1, Omarjee E1, Simonson T1.
• Journal of computational chemistry.J Comput Chem.2016 Feb 5;37(4):404-15. doi: 10.1002/jcc.24230. Epub 2015 Oct 27.
• A computational protein design method is extended to allow Monte Carlo simulations where two ligands are titrated into a protein binding pocket, yielding binding free energy differences. These provide a stringent test of the physical model, including the energy surface and sidechain rotamer definiti
• PMID 26503829

Japanese Journal

• Purification of tyrosine;tRNA ligase from Saccharomyces cerevisiae αS288C

• Kucan Zeljko [他]
• Journal of Biochemistry 73(4), 811-819, 1973-04
• NAID 40018673551

• Purification of Tyrosine: tRNA Ligase from <I>Saccharomyces cerevisiae</I> αS288C

• KUCAN Zeljko,CHAMBERS Robert W.
• The Journal of Biochemistry 73(4), 811-819, 1973
• … L-Tyrosine: tRNA ligase (AMP)[EC 6. … The kinetic constants for tRNA<SUP>Tyr</SUP> …
• NAID 130003539019

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★リンクテーブル★

リンク元	「tyrosyl-tRNA synthetase」「チロシンtRNAリガーゼ」
関連記事	「tRNA」「ligase」「tRNAs」「tRNA ligase」

「tyrosyl-tRNA synthetase」

　　[★]

チロシルtRNA合成酵素、チロシルtRNAシンテターゼ

関

tyrosine-tRNA ligase

「チロシンtRNAリガーゼ」

　　[★]

英

tyrosine-tRNA ligase

関

チロシルtRNA合成酵素

「tRNA」

　　[★] トランスファーRNA, transfer RNA, 転位RNA

「ligase」

　　[★]

リガーゼ、連結酵素

関

synthetase

「tRNAs」

　　[★] トランスファーRNA transfer RNAs

「tRNA ligase」

　　[★]

tRNAリガーゼ

関

RNA ligase