tRNA aminoacylation (Homo sapiens)

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3037354, 53291210142, 3, 36292725171126113166133420-221581827, 281033191612723, 2415cytosolmitochondrial matrixATPtRNA(Asn)AMPNARS2aminoacyl-tRNA synthetase multienzyme complexATPAMPHARSAMPATPMet-tRNA(Met)AARSATPAMPtRNA(Phe)tRNA(Asp)tRNA(Ile)AMPpyrophosphateaminoacyl-tRNA synthetase multienzyme complexATPpyrophosphateAMPL-AsparagineAMPtRNA(Asn)pyrophosphateaminoacyl-tRNA synthetase multienzyme complexPARS2ATPAMPL-serineATPL-cysteineTyr-tRNA(Tyr)CARS dimerAMPGly-tRNA(Gly)Glu-tRNA(Glu)pyrophosphatetRNA(Pro)Trp-tRNA(Trp)AMPATPATPtRNA(Tyr)pyrophosphatetRNA(Gly)AMPOrthophosphateAMPtRNA(Ile)CARS2L-AlanineL-MethioninetRNA(Leu)ATPAMPpyrophosphatepyrophosphateL-Leucineaminoacyl-tRNA synthetase multienzyme complextRNA(Phe)NARSpyrophosphateLARS2pyrophosphateATPATPtRNA(Glu)Gly-tRNA(Gly)ATPL-IsoleucinepyrophosphateATPaminoacyl-tRNA synthetase multienzyme complexpyrophosphateATPATPAMPAMPATPCys-tRNA(Cys)L-TyrosineGARS dimerH2Oaminoacyl-tRNA synthetase multienzyme complextRNA(Ser)ATPAMPtRNA(Thr)ATPL-ArginineAla-tRNA(Ala)Pro-tRNA(Pro)AMPtRNA(Lys)Asn-tRNA(Asn)Val-tRNA(Val)tRNA(Cys)aminoacyl-tRNA synthetase multienzyme complexWARS dimerSer-tRNA(Ser)Thr-tRNA(Thr)GlycineATPAMPATPOrthophosphatetRNA(Asp)Asp-tRNA(Asp)ATPPhe-tRNA(Phe)TARS dimerGlu-tRNA(Glu)Met-tRNA(Met)SARS dimerLys-tRNA(Lys)ATPAla-tRNA(Ala)ATPpyrophosphateIARS2pyrophosphatetRNA(Ser)Leu-tRNA(Leu)Phe-tRNA(Phe)L-LeucinetRNA(Gln)pyrophosphatepyrophosphatePPA1 dimerVARS2WARS2L-ProlineAMPATPAMPpyrophosphatetRNA(Met)pyrophosphateArg-tRNA(Arg)AMPATPTyr-tRNA(Tyr)L-AlaninetRNA(Trp)pyrophosphateATPL-TryptophantRNA(Met)pyrophosphateATPAMPVal-tRNA(Val)His-tRNA(His)pyrophosphateL-ValinetRNA(Val)DARS2 dimerMg++KARS dimerYARS dimerL-LysineRARS2ATPL-AspartatepyrophosphatetRNA(Tyr)Lys-tRNA(Lys)pyrophosphatetRNA(Thr)tRNA(Lys)pyrophosphateFARS A2B2 tetramerQARSPPA2 dimerL-ThreonineGARS dimerL-ThreoninetRNA(Glu)AMPL-PhenylalanineAMPL-HistidineTrp-tRNA(Trp)aminoacyl-tRNA synthetase multienzyme complexATPATPCys-tRNA(Cys)AMPAMPpyrophosphatetRNA(Arg)aminoacyl-tRNA synthetase multienzyme complexFARS2Thr-tRNA(Thr)L-GlutamatepyrophosphateATPSARS2 dimerAMPL-serineAMPYARS2 dimerpyrophosphatepyrophosphatetRNA(His)pyrophosphatepyrophosphateL-ArginineAMPpyrophosphatepyrophosphateL-AspartateH2OATPL-cysteineATPtRNA(Gln)ATPpyrophosphatepyrophosphateAMPpyrophosphateAMPPro-tRNA(Pro)Gln-tRNA(Gln)tRNA(Ala)L-MethioninepyrophosphateATPAMPtRNA(Trp)Ile-tRNA(Ile)Ile-tRNA(Ile)tRNA(Pro)Ser-tRNA(Ser)ATPAMPL-HistidineMARS2pyrophosphateL-TyrosineVARSglycineAsp-tRNA(Asp)tRNA(Cys)HARS2L-LysinetRNA(His)AMPtRNA(Arg)pyrophosphatetRNA(Val)AMPATPtRNA(Ala)AMPAMPAARS2L-IsoleucineEARS2tRNA(Leu)L-ValineAsn-tRNA(Asn)MagnesiumpyrophosphateL-GlutamateAMPATPHis-tRNA(His)tRNA(Gly)pyrophosphateAMPTARS2ATPLeu-tRNA(Leu)pyrophosphateL-GlutamineL-AsparagineArg-tRNA(Arg)AMPpyrophosphateL-ProlineL-TryptophanL-PhenylalanineL-GlutamineGln-tRNA(Gln)pyrophosphate11112, 311111


Description

tRNA synthetases catalyze the ligation of tRNAs to their cognate amino acids in an ATP-dependent manner. The reaction proceeds in two steps. First, amino acid and ATP form an aminoacyl adenylate molecule, releasing pyrophosphate. The aminoacyl adenylate remains associated with the synthetase enzyme where, in the second step it reacts with tRNA to form aminoacyl tRNA and AMP. The rapid hydrolysis of pyrophosphate makes these reactions essentially irreversible under physiological conditions (Fersht and Kaethner 1976a). Specificity of the tRNA charging reactions is achieved both by specific recognition of amino acid and tRNA substrates by the synthetase, and by an editing process in which incorrect aminoacyl adenylate molecules (e.g., valyl adenylate associated with isoleucyl tRNA synthetase) are hydrolyzed rather than conjugated to tRNAs in the second step of the reaction (Baldwin and Berg 1966a,b; Fersht and Kaethner 1976b). The tRNA synthetases can be divided into two structural classes based on conserved amino acid sequence features (Burnbaum and Schimmel 1991).

A single synthetase mediates the charging of all of the tRNA species specific for any one amino acid but, with three exceptions, glycine, lysine, and glutamine, the synthetase that catalyzes aminoacylation of mitochondrial tRNAs is encoded by a different gene than the one that acts on mitochondrial tRNAs. Both mitochondrial and cytosolic tRNA synthetase enzymes are encoded by genes in the nuclear genome.<p>A number of tRNA synthetases are known to have functions distinct from tRNA charging (reviewed by Park et al. 2005). Additionally, mutations in several of the tRNA synthetases, often affecting protein domains that are dispensable in vitro for aminoacyl tRNA synthesis, are associated with a diverse array of neurological and other diseases (Antonellis and Green 2008; Park et al. 2008). These findings raise interest into the role of these enzymes in human development and disease.<p></div>

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Bibliography

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  1. Vilalta A, Donovan D, Wood L, Vogeli G, Yang DC.; ''Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  2. Kaminska M, Shalak V, Mirande M.; ''The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function.''; PubMed Europe PMC Scholia
  3. Spencer AC, Heck A, Takeuchi N, Watanabe K, Spremulli LL.; ''Characterization of the human mitochondrial methionyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  4. Burbaum JJ, Schimmel P.; ''Structural relationships and the classification of aminoacyl-tRNA synthetases.''; PubMed Europe PMC Scholia
  5. O'Hanlon TP, Raben N, Miller FW.; ''A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS.''; PubMed Europe PMC Scholia
  6. Bullard JM, Cai YC, Spremulli LL.; ''Expression and characterization of the human mitochondrial leucyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  7. Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M.; ''Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer.''; PubMed Europe PMC Scholia
  8. Park SG, Schimmel P, Kim S.; ''Aminoacyl tRNA synthetases and their connections to disease.''; PubMed Europe PMC Scholia
  9. Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V.; ''Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.''; PubMed Europe PMC Scholia
  10. Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P.; ''Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition.''; PubMed Europe PMC Scholia
  11. Edvardson S, Shaag A, Kolesnikova O, Gomori JM, Tarassov I, Einbinder T, Saada A, Elpeleg O.; ''Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia.''; PubMed Europe PMC Scholia
  12. Curbo S, Lagier-Tourenne C, Carrozzo R, Palenzuela L, Lucioli S, Hirano M, Santorelli F, Arenas J, Karlsson A, Johansson M.; ''Human mitochondrial pyrophosphatase: cDNA cloning and analysis of the gene in patients with mtDNA depletion syndromes.''; PubMed Europe PMC Scholia
  13. Fersht AR, Kaethner MM.; ''Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12.''; PubMed Europe PMC Scholia
  14. Fisher RA, Turner BM, Dorkin HL, Harris H.; ''Studies on human erythrocyte inorganic pyrophosphatase.''; PubMed Europe PMC Scholia
  15. Scheper GC, van der Klok T, van Andel RJ, van Berkel CG, Sissler M, Smet J, Muravina TI, Serkov SV, Uziel G, Bugiani M, Schiffmann R, Krägeloh-Mann I, Smeitink JA, Florentz C, Van Coster R, Pronk JC, van der Knaap MS.; ''Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.''; PubMed Europe PMC Scholia
  16. Wolfe CL, Warrington JA, Davis S, Green S, Norcum MT.; ''Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII.''; PubMed Europe PMC Scholia
  17. Degoul F, Brulé H, Cepanec C, Helm M, Marsac C, Leroux J, Giegé R, Florentz C.; ''Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene.''; PubMed Europe PMC Scholia
  18. Jorgensen R, Søgaard TM, Rossing AB, Martensen PM, Justesen J.; ''Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  19. Baldwin AN, Berg P.; ''Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase.''; PubMed Europe PMC Scholia
  20. Antonellis A, Ellsworth RE, Sambuughin N, Puls I, Abel A, Lee-Lin SQ, Jordanova A, Kremensky I, Christodoulou K, Middleton LT, Sivakumar K, Ionasescu V, Funalot B, Vance JM, Goldfarb LG, Fischbeck KH, Green ED.; ''Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.''; PubMed Europe PMC Scholia
  21. Park SG, Ewalt KL, Kim S.; ''Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.''; PubMed Europe PMC Scholia
  22. Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED.; ''The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex.''; PubMed Europe PMC Scholia
  23. Moor N, Linshiz G, Safro M.; ''Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes.''; PubMed Europe PMC Scholia
  24. Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L.; ''Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.''; PubMed Europe PMC Scholia
  25. Beaulande M, Tarbouriech N, Härtlein M.; ''Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen.''; PubMed Europe PMC Scholia
  26. Vincent C, Tarbouriech N, Härtlein M.; ''Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase.''; PubMed Europe PMC Scholia
  27. Pan F, Lee HH, Pai SH, Lo KY.; ''Purification and subunit structure studies of human placental threonyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  28. Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J.; ''Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity.''; PubMed Europe PMC Scholia
  29. Escalante C, Yang DC.; ''Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix.''; PubMed Europe PMC Scholia
  30. Bange FC, Flohr T, Buwitt U, Böttger EC.; ''An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  31. Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T.; ''Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit.''; PubMed Europe PMC Scholia
  32. Pynes GD, Younathan ES.; ''Purification and some properties of inorganic pyrophosphatase from human erythrocytes.''; PubMed Europe PMC Scholia
  33. Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP.; ''Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts.''; PubMed Europe PMC Scholia
  34. Davidson E, Caffarella J, Vitseva O, Hou YM, King MP.; ''Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  35. Baldwin AN, Berg P.; ''Purification and properties of isoleucyl ribonucleic acid synthetase from Escherichia coli.''; PubMed Europe PMC Scholia
  36. Thuillier L.; ''Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphatase.''; PubMed Europe PMC Scholia
  37. Lee JW, Beebe K, Nangle LA, Jang J, Longo-Guess CM, Cook SA, Davisson MT, Sundberg JP, Schimmel P, Ackerman SL.; ''Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration.''; PubMed Europe PMC Scholia
  38. Bullard JM, Cai YC, Demeler B, Spremulli LL.; ''Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  39. Kaiser E, Hu B, Becher S, Eberhard D, Schray B, Baack M, Hameister H, Knippers R.; ''The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase.''; PubMed Europe PMC Scholia
  40. Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M.; ''Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.''; PubMed Europe PMC Scholia
  41. Fersht AR, Kaethner MM.; ''Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing.''; PubMed Europe PMC Scholia
  42. Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K.; ''Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase.''; PubMed Europe PMC Scholia
  43. Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S.; ''Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.''; PubMed Europe PMC Scholia
  44. Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P.; ''Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant.''; PubMed Europe PMC Scholia
  45. Antonellis A, Green ED.; ''The role of aminoacyl-tRNA synthetases in genetic diseases.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
116664view12:24, 9 May 2021EweitzModified title
114669view16:14, 25 January 2021ReactomeTeamReactome version 75
113116view11:18, 2 November 2020ReactomeTeamReactome version 74
112350view15:27, 9 October 2020ReactomeTeamReactome version 73
101251view11:14, 1 November 2018ReactomeTeamreactome version 66
100790view20:42, 31 October 2018ReactomeTeamreactome version 65
100332view19:19, 31 October 2018ReactomeTeamreactome version 64
99877view16:02, 31 October 2018ReactomeTeamreactome version 63
99434view14:36, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93779view13:35, 16 August 2017ReactomeTeamreactome version 61
93309view11:20, 9 August 2017ReactomeTeamreactome version 61
86391view09:17, 11 July 2016ReactomeTeamreactome version 56
83310view10:45, 18 November 2015ReactomeTeamVersion54
81449view12:59, 21 August 2015ReactomeTeamVersion53
76923view08:19, 17 July 2014ReactomeTeamFixed remaining interactions
76628view12:00, 16 July 2014ReactomeTeamFixed remaining interactions
75959view10:01, 11 June 2014ReactomeTeamRe-fixing comment source
75661view10:56, 10 June 2014ReactomeTeamReactome 48 Update
75016view13:53, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74660view08:43, 30 April 2014ReactomeTeamReactome46
74093view12:42, 29 March 2014EgonwFixed the Uniprot-TrEMBL data sources.
45057view19:53, 6 October 2011KhanspersOntology Term : 'translation pathway' added !
42153view22:00, 4 March 2011MaintBotAutomatic update
39964view05:58, 21 January 2011MaintBotNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
AARS ProteinP49588 (Uniprot-TrEMBL)
AARS2 ProteinQ5JTZ9 (Uniprot-TrEMBL)
AMP Metabolite16027 (ChEBI)
ATP Metabolite15422 (ChEBI)
Ala-tRNA

(Ala)

Metabolite17732 (ChEBI)
Arg-tRNA

(Arg)

Metabolite18366 (ChEBI)
Asn-tRNA

(Asn)

Metabolite29265 (ChEBI)
Asp-tRNA

(Asp)

Metabolite29158 (ChEBI)
CARS

dimer

ComplexREACT_17681 (Reactome)
CARS2 ProteinQ9HA77 (Uniprot-TrEMBL)
Cys-tRNA

(Cys)

Metabolite29152 (ChEBI)
DARS2

dimer

ComplexREACT_15709 (Reactome)
EARS2 ProteinQ5JPH6 (Uniprot-TrEMBL)
FARS

A2B2 tetramer

ComplexREACT_16104 (Reactome)
FARS2 ProteinO95363 (Uniprot-TrEMBL)
GARS

dimer

ComplexREACT_15693 (Reactome)
GARS dimer ComplexREACT_17609 (Reactome)
Gln-tRNA

(Gln)

Metabolite29166 (ChEBI)
Glu-tRNA

(Glu)

Metabolite29157 (ChEBI)
Gly-tRNA

(Gly)

Metabolite29156 (ChEBI)
Glycine Metabolite15428 (ChEBI)
H2O Metabolite15377 (ChEBI)
HARS ProteinP12081 (Uniprot-TrEMBL)
HARS2 ProteinP49590 (Uniprot-TrEMBL)
His-tRNA

(His)

Metabolite29155 (ChEBI)
IARS2 ProteinQ9NSE4 (Uniprot-TrEMBL)
Ile-tRNA

(Ile)

Metabolite29160 (ChEBI)
KARS

dimer

ComplexREACT_15848 (Reactome)
L-Alanine Metabolite16977 (ChEBI)
L-Arginine Metabolite16467 (ChEBI)
L-Asparagine Metabolite17196 (ChEBI)
L-Aspartate Metabolite17053 (ChEBI)
L-Glutamate Metabolite16015 (ChEBI)
L-Glutamine Metabolite18050 (ChEBI)
L-Histidine Metabolite15971 (ChEBI)
L-Isoleucine Metabolite17191 (ChEBI)
L-Leucine Metabolite15603 (ChEBI)
L-Lysine Metabolite18019 (ChEBI)
L-Methionine Metabolite16643 (ChEBI)
L-Phenylalanine Metabolite17295 (ChEBI)
L-Proline Metabolite17203 (ChEBI)
L-Threonine Metabolite16857 (ChEBI)
L-Tryptophan Metabolite16828 (ChEBI)
L-Tyrosine Metabolite17895 (ChEBI)
L-Valine Metabolite16414 (ChEBI)
L-cysteine Metabolite17561 (ChEBI)
L-serine Metabolite17115 (ChEBI)
LARS2 ProteinQ15031 (Uniprot-TrEMBL)
Leu-tRNA

(Leu)

Metabolite16624 (ChEBI)
Lys-tRNA

(Lys)

Metabolite16047 (ChEBI)
MARS2 ProteinQ96GW9 (Uniprot-TrEMBL)
Magnesium Metabolite18420 (ChEBI)
Met-tRNA

(Met)

Metabolite16635 (ChEBI)
Mg++ Metabolite18420 (ChEBI)
NARS ProteinO43776 (Uniprot-TrEMBL)
NARS2 ProteinQ96I59 (Uniprot-TrEMBL)
Orthophosp

hate

Metabolite18367 (ChEBI)
PARS2 ProteinQ7L3T8 (Uniprot-TrEMBL)
PPA1

dimer

ComplexREACT_3635 (Reactome)
PPA2

dimer

ComplexREACT_21920 (Reactome)
Phe-tRNA

(Phe)

Metabolite29153 (ChEBI)
Phe-tRNA(Phe) Metabolite29153 (ChEBI)
Pro-tRNA

(Pro)

Metabolite29154 (ChEBI)
QARS ProteinP47897 (Uniprot-TrEMBL)
RARS2 ProteinQ5T160 (Uniprot-TrEMBL)
SARS

dimer

ComplexREACT_18078 (Reactome)
SARS2

dimer

ComplexREACT_15712 (Reactome)
Ser-tRNA

(Ser)

Metabolite29162 (ChEBI)
TARS

dimer

ComplexREACT_16019 (Reactome)
TARS2 ProteinQ9BW92 (Uniprot-TrEMBL)
Thr-tRNA

(Thr)

Metabolite29163 (ChEBI)
Trp-tRNA

(Trp)

Metabolite29159 (ChEBI)
Tyr-tRNA

(Tyr)

Metabolite29161 (ChEBI)
VARS ProteinP26640 (Uniprot-TrEMBL)
VARS2 ProteinQ5ST30 (Uniprot-TrEMBL)
Val-tRNA

(Val)

Metabolite29164 (ChEBI)
WARS

dimer

ComplexREACT_15987 (Reactome)
WARS2 ProteinQ9UGM6 (Uniprot-TrEMBL)
YARS

dimer

ComplexREACT_16005 (Reactome)
YARS2

dimer

ComplexREACT_18046 (Reactome)
aminoacyl-tRNA

synthetase multienzyme complex

ComplexREACT_15869 (Reactome)
glycine Metabolite15428 (ChEBI)
pyrophosp

hate

Metabolite29888 (ChEBI)
tRNA(Ala) Metabolite17732 (ChEBI)
tRNA(Arg) Metabolite29171 (ChEBI)
tRNA(Asn) Metabolite29172 (ChEBI)
tRNA(Asp) Metabolite29186 (ChEBI)
tRNA(Cys) Metabolite29167 (ChEBI)
tRNA(Gln) Metabolite29168 (ChEBI)
tRNA(Glu) Metabolite29175 (ChEBI)
tRNA(Gly) Metabolite29176 (ChEBI)
tRNA(His) Metabolite29178 (ChEBI)
tRNA(Ile) Metabolite29174 (ChEBI)
tRNA(Leu) Metabolite29169 (ChEBI)
tRNA(Lys) Metabolite29185 (ChEBI)
tRNA(Met) Metabolite29173 (ChEBI)
tRNA(Phe) Metabolite29184 (ChEBI)
tRNA(Pro) Metabolite29177 (ChEBI)
tRNA(Ser) Metabolite29179 (ChEBI)
tRNA(Thr) Metabolite29180 (ChEBI)
tRNA(Trp) Metabolite29181 (ChEBI)
tRNA(Tyr) Metabolite29182 (ChEBI)
tRNA(Val) Metabolite29183 (ChEBI)

Annotated Interactions

No annotated interactions

Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP1938"
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