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adenosine 5'-(beta,gamma-imido)triphosphate + L-proline + tRNAPro
?
ATP + 2-selenaproline + tRNAPro
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
ATP + 3-thiaproline + tRNAPro
?
ATP + 4-amino-L-proline + tRNAPro
?
-
-
-
-
?
ATP + 4-difluoro-L-proline + tRNAPro
?
-
-
-
-
?
ATP + 4-fluoro-L-proline + tRNAPro
?
-
-
-
-
?
ATP + 4-hydroxy-L-proline + tRNAPro
?
-
-
-
-
?
ATP + azetidine-2-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + beta-thia-L-proline + tRNAPro
?
-
-
-
-
?
ATP + cis(exo)-3,4-methano-L-proline + tRNAPro
?
ATP + cis-4-hydroxyproline + tRNAPro
AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
-
-
-
-
?
ATP + dehydro-L-proline + tRNAPro
?
-
-
-
-
?
ATP + gamma-thia-L-proline + tRNAPro
?
-
-
-
-
?
ATP + gamma-thiaproline + tRNAPro
?
-
-
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
ATP + L-azetidine-2-carboxylic acid + tRNAPro
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
ATP + L-cysteine + tRNACys
AMP + diphosphate + L-cysteinyl-tRNACys
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
ATP + L-cysteine + tRNAs
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
ATP + L-proline + L-tRNAAla
AMP + diphosphate + L-prolyl-tRNAAla
-
-
-
?
ATP + L-proline + L-tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + L-tRNAProAla
AMP + diphosphate + L-prolyl-tRNAProAla
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
ATP + L-thiazolidine-4-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + N-methyl-L-alanine + tRNAPro
?
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
ATP + thiazolidine-4-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + trans-4-hydroxyproline + tRNAPro
AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
-
-
-
-
?
additional information
?
-
adenosine 5'-(beta,gamma-imido)triphosphate + L-proline + tRNAPro
?
-
-
-
?
adenosine 5'-(beta,gamma-imido)triphosphate + L-proline + tRNAPro
?
-
-
-
-
?
ATP + 2-selenaproline + tRNAPro
?
-
-
-
-
?
ATP + 2-selenaproline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3,4-dehydro-DL-proline + tRNAPro
?
-
-
-
-
?
ATP + 3-thiaproline + tRNAPro
?
-
-
-
-
?
ATP + 3-thiaproline + tRNAPro
?
-
-
-
-
?
ATP + cis(exo)-3,4-methano-L-proline + tRNAPro
?
-
-
-
-
?
ATP + cis(exo)-3,4-methano-L-proline + tRNAPro
?
-
-
-
-
?
ATP + cis(exo)-3,4-methano-L-proline + tRNAPro
?
-
-
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
-
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
-
-
-
r
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
very low activity
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
enzyme possesses both pre- and post-transfer hydrolytic editing activity to prevent from misincorporation of alanine into proteins
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
the enzyme performs 1. misacetylation of tRNAPro, 2. hydrolysis of the misactivated Ala-AMP, i.e. pre-transfer editing, independent of tRNA, and 3. deacetylation of the mischarged Ala-tRNAPro, i.e. post-transfer editing
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
L-alanine is a poor substrate
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
mutant K279A, low activity
-
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
very low activity
-
?
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
misacetylation of tRNAPro, no editing
-
?
ATP + L-azetidine-2-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + L-azetidine-2-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + L-azetidine-2-carboxylic acid + tRNAPro
?
-
-
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity. Addition of tRNA has a small threefold stimulatory effect on cysteine activation. The lack of a major role of tRNA in activation of cysteine suggests that the dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity. Addition of tRNA has a small threefold stimulatory effect on cysteine activation. The lack of a major role of tRNA in activation of cysteine suggests that the dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-cysteine + tRNA
AMP + diphosphate + L-cysteinyl-tRNA
in later work it is shown that cysteine is attached to tRNA(Pro) and thus constitutes a misaminoacylation event and not a dual specificity
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
-
-
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
dual-specificity enzyme
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
two-step reaction
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation of tRNAPro, no editing
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
two-step reaction, both steps are dependent on tRNACys
-
r
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
dual-specificity enzyme
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
dual-specificity enzyme, enzyme contains a discrete cysteine binding pocket
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
misacetylation, no editing of the misactivated Cys-tRNAPro
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
recognition elements of Aeropyrum pernix tRNAPro are determined to be G35 and G36 of anticodon, discriminator base A73, and G1-C72 base pair at acceptor stem end
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
recognition elements of Aeropyrum pernix tRNAPro are determined to be G35 and G36 of anticodon, discriminator base A73, and G1-C72 base pair at acceptor stem end
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
cis(exo)-3,4-methano-L-proline can replace proline on ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
a two-step reaction
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
cis(exo)-3,4-methano-L-proline can replace proline on ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
ir
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
no deacetylation by the wild-type enzyme, but mutants H369C and H369A is able to deacetylate Pro-tRNAPro
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
editing mechanism, the aminoacylation active site plays a significant role in preserving the fidelity of translation by acting as a filter that selectively releases non-cognate adenylates into solution, while protecting the cognate adenylate from hydrolysis, overview, scheme showing proposed pre-transfer and posttransfer editing pathways, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the enzyme recognizes specific bases of tRNAPro in both the anticodon domain, which mediate initial complex formation, and in the acceptor stem, which is proximal to the site of catalysis, analysis of the molecular interaction between ProRS and the acceptor stem of cognate tRNAPro interaction involves the critical residue R144 in the active site and G72 in the acceptor stem, aminoacylation of G72A-tRNAPro is reduced 170fold compared to wild-type tRNAPro when assayed with wild-type ProRS, whereas only a 2.6fold decrease is observed with mutant R144K ProRS, activity of wild-type and mutant enzymes with wild-type and mutant tRNAs, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
4-hydroxy-L-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
semi-synthetic human tRNAPro prepared by annealing a 5'-57-mer fragment to a 3'-16-mer. The 5'-57-mer is prepared by in vitro transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
two-step reaction
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
activation of proline does not require tRNA. The dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
mutations are introduced into the acceptor stem and the anticodon. Variants containing a single substitution of C72 or A73, or of one of the anticodon nucleotides, are created by site-directed mutagenesis. Substitution of A73 in Methanococcus jannaschii tRNAPro by any of the other three nucleotides has a small effect (about 10fold) on kcat/Km. The G73 substitution has the most severe effect (12.2fold), whereas the C73 or U73 substitution has a smaller effect (2-fold and 6-fold, respectively). A73 is much less significant for Methanococcus jannaschii tRNA recognition than it is for the Escherichia coli tRNA. The weak contribution of A73 to recognition by Methanococcus jannaschii ProRS, however, is comparable with that of C73 in the human system. Position 72 of Methanococcus jannaschii tRNAPro also has a minor role in aminoacylation. Substitution with any other nucleotide has a less than 10fold effect on kcat/Km. The U substitution results in the largest decrease (5.3fold), followed by the G substitution (2.2fold). The A substitution is well tolerated with only a 1.4fold decrease in kcat/Km. Substitution of U34 with A or G has no effect on aminoacylation, whereas substitution with C results in only a 1.3fold decrease. The anticodon nucleotide G35 of tRNAPro is a minor determinant for aminoacylation. Substitution of G35 with A has the largest effect (9fold), followed by the C substitution (8fold), and the U substitution (1.5fold). The most important specificity determinant in Methanococcus jannaschii tRNAPro is G36. Substitution with C alone reduces the kcat/Km of aminoacylation by 250fold, and substitution with A results in a nearly 40fold decrease. The exception is the U substitution, which maintains a kcat/Km that is similar to that of the wild-type tRNA. A representative aminoacylation assay of the C36, A36, and U36 mutants relative to that of the wild-type is shown
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the enzyme mischarges tRNAPro with alanine at a rate that is 6800fold reduced relative to charging with proline. The enzyme is able to hydrolyze misactivated alanine via both pretransfer and post-transfer editing pathways. Mischarging of a tRNAPro transcript with cysteine is also detected. The enzyme stimulates ATP hydrolysis activity with the noncognate amino acid alanine but not in the presence of proline
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
the unmodified transcript of Methanococcus jannaschii tRNAPro is mis-acylated with cysteine. The origin of mischarging is not at the anticodon or acceptor stem. Replacement of the D loop in the tRNA core with that of tRNACys suppresses mischarging with cysteine without compromising the activity of aminoacylation with proline. Prevention of mis-placement by alteration of the core structure or by nucleotide modifications in the tRNA illustrates a novel strategy of the dual-specificity synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
mutations are introduced into the acceptor stem and the anticodon. Variants containing a single substitution of C72 or A73, or of one of the anticodon nucleotides, are created by site-directed mutagenesis. Substitution of A73 in Methanococcus jannaschii tRNAPro by any of the other three nucleotides has a small effect (about 10fold) on kcat/Km. The G73 substitution has the most severe effect (12.2fold), whereas the C73 or U73 substitution has a smaller effect (2-fold and 6-fold, respectively). A73 is much less significant for Methanococcus jannaschii tRNA recognition than it is for the Escherichia coli tRNA. The weak contribution of A73 to recognition by Methanococcus jannaschii ProRS, however, is comparable with that of C73 in the human system. Position 72 of Methanococcus jannaschii tRNAPro also has a minor role in aminoacylation. Substitution with any other nucleotide has a less than 10fold effect on kcat/Km. The U substitution results in the largest decrease (5.3fold), followed by the G substitution (2.2fold). The A substitution is well tolerated with only a 1.4fold decrease in kcat/Km. Substitution of U34 with A or G has no effect on aminoacylation, whereas substitution with C results in only a 1.3fold decrease. The anticodon nucleotide G35 of tRNAPro is a minor determinant for aminoacylation. Substitution of G35 with A has the largest effect (9fold), followed by the C substitution (8fold), and the U substitution (1.5fold). The most important specificity determinant in Methanococcus jannaschii tRNAPro is G36. Substitution with C alone reduces the kcat/Km of aminoacylation by 250fold, and substitution with A results in a nearly 40fold decrease. The exception is the U substitution, which maintains a kcat/Km that is similar to that of the wild-type tRNA. A representative aminoacylation assay of the C36, A36, and U36 mutants relative to that of the wild-type is shown
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
the unmodified transcript of Methanococcus jannaschii tRNAPro is mis-acylated with cysteine. The origin of mischarging is not at the anticodon or acceptor stem. Replacement of the D loop in the tRNA core with that of tRNACys suppresses mischarging with cysteine without compromising the activity of aminoacylation with proline. Prevention of mis-placement by alteration of the core structure or by nucleotide modifications in the tRNA illustrates a novel strategy of the dual-specificity synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
activation of proline does not require tRNA. The dual specificity enzyme must distinguish cysteine from proline directly, without the assistance of each cognate tRNA, to achieve the necessary specificity required for protein synthesis
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
cis(exo)-3,4-methano-L-proline can replace proline on ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the chloroplastic-specific tRNAPro is not recognized by the cytoplasmic enzyme but can be charged by organellar or E. coli enzyme
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the two tRNAsPro in the cytoplasm can be charged by the cytoplasmic enzyme, but not by the organellar enzyme or the E. coli enzyme
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
mitochondria-specific tRNAPro is not recognized by the cytoplasmic enzyme, but can be charged by the organellar or the E. coli enzyme
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
N-methylglycine can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-azetidine-2-carboxylic acid can replace proline in ATP-diphosphate exchange (not)
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
3,4-dehydro-DL-proline can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
L-thiazolidine-4-carboxylic acid can replace proline in ATP-diphosphate exchange
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
small-substrate recognition by the prokaryote-type ProRS, model for posttransfer editing conformation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
binding of L-proline and ATP causes conformational changes in the proline binding loop and motif 2 loop, formation of an activated prolyl-adenylate reaction intermediate, required for the final conformational ordering of a ten residue peptide, the ordered loop, close to the active site
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
initial docking state of the tRNAPro in which the anticodon stem-loop is engaged, particularly via the tRNAPro-specific bases G35 and G36, but the 3'-end does not enter the active site
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the C-terminal anticodon binding domain with an alpha/beta fold binds to the anticodon stem-loop from the major groove side
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
Thermus thermophilus prolyl-tRNA synthetase exhibits a cysteinyl-tRNA synthetase activity although the organism also encodes a canonical cysteinyl-tRNA synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
Thermus thermophilus prolyl-tRNA synthetase exhibits a cysteinyl-tRNA synthetase activity although the organism also encodes a canonical cysteinyl-tRNA synthetase
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the C-terminal anticodon binding domain with an alpha/beta fold binds to the anticodon stem-loop from the major groove side
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
-
-
-
-
?
ATP + N-methylglycine + tRNAPro
?
-
-
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
?
additional information
?
-
-
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
3-thiaproline, 4-thiaproline and 4-selenaproline can replace proline in the ATP-diphosphate exchange. 4-Thiaproline and 4-selenaproline show a much higher Km
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, no activity with L-cysteine
-
?
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
no activity with 3,4-phenyl-L-proline and pipecolic acid
-
-
?
additional information
?
-
-
no activity with L-cysteine, the enzyme also performs the ATP-diphosphate exchange reaction, enzyme possesses no editing activity against L-alanine and to prevent from misincorporation of alanine into proteins
-
?
additional information
?
-
-
in addition to enzymic activity, glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma, binds the ceruloplasmin 3'-untranslated region in an mRNP containing three additional proteins, and silences ceruloplasmin mRNA translation
-
-
?
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
-
-
?
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities, overview
-
-
?
additional information
?
-
-
substrate specificity, reducing effects of diverse different phosphorothioate substitutions in the 3'-strand of human tRNAPro on aminoacylation efficiency, mechanism, overview
-
-
?
additional information
?
-
-
the upstream WHEP pair of EPRS directs high-affinity binding to GAIT element-bearing mRNAs, while the overlapping, downstream pair binds NSAP1, which inhibits mRNA binding. Interaction of EPRS with ribosomal protein L13a and GAPDH induces a conformational witch that rescues mRNA binding and restores translational control, interaction analysis, overview
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme does not perform deacetylation reaction of mischarged Cys-tRNAPro and Ala-tRNAPro, the enzyme also performs the ATP-diphosphate exchange reaction, no charging of tRNACys with L-cysteine
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction, the enzyme possesses a pre- and post-editing mechanism for alanine
-
?
additional information
?
-
-
phylogenetic analysis
-
?
additional information
?
-
-
aminoacylation specificity, the archaeal prolyl-tRNA synthetase that can aminoacylate archaeal tRNAPro with proline or cysteine, but does not aminoacylate archaeal tRNACys with cysteine, overview
-
-
?
additional information
?
-
-
determination of Pro-AMP and Ala-AMP hydrolysis activities, overview
-
-
?
additional information
?
-
-
aminoacylation specificity, the archaeal prolyl-tRNA synthetase that can aminoacylate archaeal tRNAPro with proline or cysteine, but does not aminoacylate archaeal tRNACys with cysteine, overview
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
aminoacylation specificity, the archaeal prolyl-tRNA synthetase that can aminoacylate archaeal tRNAPro with proline or cysteine, but does not aminoacylate archaeal tRNACys with cysteine, overview
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
ATP-diphosphate exchange
-
-
?
additional information
?
-
-
3-thiaproline, 4-thiaproline and 4-selenaproline can replace proline in the ATP-diphosphate exchange. 4-Thiaproline and 4-selenaproline show a much higher Km
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
?
additional information
?
-
-
comparison of the overall enzyme structure and binding mode of ATP and prolyl-adenylate with those of the archael/eukaryote-type ProRS from Thermus thermophilus, overview
-
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
the enzyme also performs the ATP-diphosphate exchange reaction
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + L-alanine + tRNAPro
AMP + diphosphate + L-alanyl-tRNAPro
-
-
-
-
?
ATP + L-cysteine + tRNAPro
AMP + diphosphate + L-cysteinyl-tRNAPro
-
two-step reaction
-
r
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
additional information
?
-
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAGlu
AMP + diphosphate + L-prolylyl-tRNAGlu
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
r
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
a complex between ProRS and leucyl-tRNA synthetase, LeuRS, in Methanothermobacter thermautotrophicus enhances tRNAPro aminoacylation, overview
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
neither GagPol nor prolyl-tRNA synthetase are required for packaging of tRNAPro into MuLV, tRNAPro is used as primer for reverse transcription
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
?
ATP + L-proline + tRNAPro
AMP + diphosphate + L-prolyl-tRNAPro
-
-
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
in addition to enzymic activity, glutamyl-prolyl-tRNA synthetase is phosphorylated in response to interferon-gamma, binds the ceruloplasmin 3'-untranslated region in an mRNP containing three additional proteins, and silences ceruloplasmin mRNA translation
-
-
?
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
-
-
?
additional information
?
-
-
phylogenetic analysis
-
?
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2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-alkenyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-amino-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-bromo-8-(trifluoromethyl)-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-7-bromo-8-methyl-4-quinolinecarboxylic acid
2-(4-bromo-phenyl)-7-fluoro-8-methyl-4-quinolinecarboxylic acid
2-(4-methoxy-phenyl)-4-quinolinecarboxylic acid
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acid
2-furyl-4-quinolinecarboxylic acid
2-naphthyl-4-quinolinecarboxylic acid
2-phenyl-4-quinolinecarboxylic acid
2-pyridyl-4-quinolinecarboxylic acid
2-[4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-3-(trifluoromethyl)-1H-pyrazol-1-yl]acetamide
-
3-(3,3-dimethylbutanamido)-N-[(naphthalen-1-yl)methyl]pyrazine-2-carboxamide
-
3-[(cyclohexanecarbonyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)pyrazine-2-carboxamide
-
3-[4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-1H-pyrazol-3-yl]propanamide
-
4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-amine
-
4-(4-fluorophenyl)-5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-1H-pyrazole-3-carboxamide
-
4-Methylene-DL-proline
-
weak
5'-O-(N-[prolyl]-sulphamoyl) adenosine
5'-O-[N-(L-alanyl)-sulfamoyl]adenosine
-
a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
7-bromo-6-chloro-3-[3-[3-hydroxy-2-piperidinyl]-2-oxopropyl]-4-quinazolinone
azetidine-2-carboxylic acid
-
at 0.2 mM isozyme ProRS-Org is inhibited by 25%
cis(exo)-3,4-Methano-L-proline
cysteamine
-
inhibition of Cys-tRNAPro formation
cysteinyl-sulfamoyl-adenylate
-
i.e. Cys-AMS, intermediate analogue, competitive inhibition
D-cysteine-DL-homocysteine
-
inhibition of Cys-tRNAPro formation
iodoacetamide
-
more than 90% protection by 10 mM ATP or 10 mM ATP + 10 mM Pro
L-azetidine-2-carboxylic acid
L-cysteine
competitive inhibition of prolylation. A 40fold excess over L-proline concentration reduces the prolylation activity by 80%, no inhibition of mutant P100A
L-cysteine ethyl ester
-
inhibition of Cys-tRNAPro formation
L-cysteine methyl ester
-
inhibition of Cys-tRNAPro formation
L-proline
competitive inhibition of cysteinylation. A 40fold excess over L-cysteine concentration reduces the cysteinylation activity by over 80%, no inhibition of mutant E103A
L-thiazolidine-4-carboxylic acid
N-(2,4-difluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(3-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[1-methyl-3-(trifluoromethyl)-4-[3-(trifluoromethyl)phenyl]-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-(2-hydroxyethyl)-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-1-methyl-3-[2-(morpholin-4-yl)ethyl]-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-3-(2-hydroxyethyl)-1-methyl-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-(4-fluorophenyl)-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-[2-(2-hydroxyethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-[2-(hydroxymethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-(4-fluorophenyl)-N'-[4-[3-(2-hydroxyethyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]urea
-
N-([3-[5-[[(4-fluorophenyl)carbamoyl]amino]-1-methyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]phenyl]methyl)methanesulfonamide
-
N-acetyl-L-cysteine
-
inhibition of Cys-tRNAPro formation
N-Boc-halofuginone
less than 20% inhibition at 1 mM
N-Methyl-L-alanine
-
weak
N-[(4-chlorophenyl)methyl]-3-[(cyclohexanecarbonyl)amino]pyrazine-2-carboxamide
-
N-[3-(2-cyanoethyl)-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
N-[3-(cyanomethyl)-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
N-[3-cyano-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
N-[3-[2-(dimethylamino)ethyl]-4-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
N-[4-(3,4-difluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
N-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-methoxyphenyl)urea
-
N-[4-(4-fluorophenyl)-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-[2-(morpholin-4-yl)pyridin-4-yl]urea
-
N-[4-bromo-1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-N'-(4-fluorophenyl)urea
-
prolyl-sulfamoyl-adenylate
-
i.e. Pro-AMS, intermediate analogue, competitive inhibition
TCMDC-124506
competitive inhibitor
2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
-
-
2-(2-chloro-thiophene)-4-quinolinecarboxylic acid
-
weak inhibition
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
-
-
2-(3,4-dichloro-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-5,7-dichloro-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-5-methyl-7-chloro-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6,8-dimethyl-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-(4-hydroxyphenyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-(trifluoromethoxy)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-alkenyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-alkenyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-amino-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-amino-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-bromo-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-bromo-8-(trifluoromethyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-bromo-8-(trifluoromethyl)-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-chloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-chloro-8-hydroxymethyl-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
-
best inhibitor, species-selective
2-(4-bromo-phenyl)-6-chloro-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-iodo-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acid
-
strong inhibition
2-(4-bromo-phenyl)-6-methyl-8-chloro-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-7-bromo-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-7-bromo-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-7-fluoro-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-bromo-phenyl)-7-fluoro-8-methyl-4-quinolinecarboxylic acid
-
-
2-(4-methoxy-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-methoxy-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-(4-[trifluoromethyl]-phenyl)-4-quinolinecarboxylic acid
-
weak inhibition
2-furyl-4-quinolinecarboxylic acid
-
weak inhibition
2-furyl-4-quinolinecarboxylic acid
-
weak inhibition
2-naphthyl-4-quinolinecarboxylic acid
-
-
2-naphthyl-4-quinolinecarboxylic acid
-
weak inhibition
2-phenyl-4-quinolinecarboxylic acid
-
weak inhibition
2-phenyl-4-quinolinecarboxylic acid
-
weak inhibition
2-pyridyl-4-quinolinecarboxylic acid
-
weak inhibition
2-pyridyl-4-quinolinecarboxylic acid
-
weak inhibition
3,4-Dehydroproline
-
-
3,4-Dehydroproline
-
competitive inhibition of proline transfer to tRNA, no inhibition of proline-dependent ATP-diphosphate exchange
3-pyrroline
-
-
3-Selenaproline
-
competitive
3-Selenaproline
-
competitive
5'-O-(N-[prolyl]-sulphamoyl) adenosine
i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate
5'-O-(N-[prolyl]-sulphamoyl) adenosine
i.e. ProAMS, a nonhydrolyzable analogue of the prolyl-adenylate
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
-
-
5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine
-
a non-hydrolyzable adenylate analogue
6-fluoro-febrifugine
-
7-bromo-6-chloro-3-[3-[3-hydroxy-2-piperidinyl]-2-oxopropyl]-4-quinazolinone
-
7-bromo-6-chloro-3-[3-[3-hydroxy-2-piperidinyl]-2-oxopropyl]-4-quinazolinone
-
-
cis(exo)-3,4-Methano-L-proline
-
-
cis(exo)-3,4-Methano-L-proline
-
-
cis-3-hydroxy-L-proline
-
weak
cis-3-hydroxy-L-proline
-
weak
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.5 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.51 M
CsCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.7 M
febrifugine
-
-
halofuginone
strong inhibition at 0.001 mM
halofuginone
-
competitive inhibitor
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: above 2 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.37 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.4 M
KCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 2.1 M
L-azetidine-2-carboxylic acid
-
-
L-azetidine-2-carboxylic acid
-
-
L-thiazolidine-4-carboxylic acid
-
-
L-thiazolidine-4-carboxylic acid
-
-
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.25 M
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.23 M
LiCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.2 M
N-methylglycine
-
weak
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.5 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.3 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.27 M
NaCl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.43 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.0 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.35 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 0.38 M
NH4Cl
-
concentration required to inhibit ATP-diphosphate exchange by 50%: 1.1 M
p-chloromercuribenzoate
-
ATP, tRNA, Pro or several analogues of Pro, protect against inhibition. Reactivation by sulfhydryl-reducing reagents, reactivation of Delonix enzyme is markedly temperature-dependent, Phaseolus enzyme is reactivated equally efficiently at all temperatures tested
p-chloromercuribenzoate
-
ATP, tRNA, Pro or several analogues of Pro, protect against inhibition. Reactivation by sulfhydryl-reducing reagents, reactivation of Delonix enzyme is markedly temperature-dependent, Phaseolus enzyme is reactivated equally efficiently at all temperatures tested
p-chloromercuribenzoate
-
-
Pyrrole
-
-
Pyrrolidine
-
-
tetrahydrofebrifugine
-
tetrahydrofebrifugine
-
-
tetrahydrofuran
-
-
Tetrahydrothiophen
-
-
additional information
-
MAZ1310 has no inhibitory effect on enzyme activity
-
additional information
-
no inhibition of Cys-tRNAPro formation by L-sulfinic acid, L-cysteic acid, S-methyl L-cysteine, and homocysteine thiolactone
-
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6.25 - 55
2-selenaproline
-
0.28 - 2.2
3,4-dehydro-DL-proline
66
4-thiaproline
-
ATP-diphosphate exchange
2 - 7.1
cis(exo)-3,4-Methano-L-proline
53 - 55
cis-4-hydroxyproline
12.5
gamma-thiaproline
-
ATP-diphosphate exchange
1.43 - 5.3
L-azetidine-2-carboxylic acid
20 - 50
L-thiazolidine-4-carboxylic acid
-
ATP-diphosphate exchange
68
N-Methyl-L-alanine
-
ATP-diphosphate exchange
20
thiazolidine-4-carboxylic acid
-
ATP-diphosphate exchange
2 - 37
trans-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.00003 - 0.01414
tRNAPro
additional information
additional information
-
6.25
2-selenaproline
-
ATP-diphosphate exchange
-
55
2-selenaproline
-
ATP-diphosphate exchange
-
0.28
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.364
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.5
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.74
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
0.78
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
2.2
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange
2.2
3,4-dehydro-DL-proline
-
ATP-diphosphate exchange, L-azetidine-2-carboxylic acid
1.4
3-thiaproline
-
ATP-diphosphate exchange
1.4
3-thiaproline
-
3,4-dehydro-DL-proline, , ATP-diphosphate exchange
0.049
ATP
aminoacylation reaction with L-proline, recombinant wild-type enzyme, pH 7.0, 70°C
0.06
ATP
aminoacylation reaction with L-cysteine, recombinant wild-type enzyme, pH 7.0, 70°C
2 - 3
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
4.6
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
7.1
cis(exo)-3,4-Methano-L-proline
-
ATP-diphosphate exchange
53
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
55
cis-4-hydroxyproline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
79
L-alanine
-
37°C
140
L-alanine
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
454
L-alanine
mutant enzyme G217A, at pH 7.0 and 22°C
685
L-alanine
wild type enzyme, at pH 7.0 and 22°C
1360
L-alanine
mutant enzyme E218A, at pH 7.0 and 22°C
1.43
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
2
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
5.3
L-azetidine-2-carboxylic acid
-
ATP-diphosphate exchange
0.01
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.01
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.02
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
0.022
L-cysteine
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C
0.03
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.05
L-cysteine
-
ATP-diphosphate exchange, pH 7.5, 35°C
0.05
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
0.05
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
0.0745
L-cysteine
pH 7.0, 37°C
0.09
L-cysteine
-
ATP-diphosphate exchange reaction, pH 7.5, 35°C
0.09
L-cysteine
-
recombinant enzyme, pH 7.2, 60°C
0.17
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.17
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.18
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.19
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.2
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.26
L-cysteine
-
recombinant enzyme, pH 7.2, 37°C
0.137
L-Pro
-
ATP-diphosphate exchange
0.182
L-Pro
-
ATP-diphosphate exchange
0.29
L-Pro
-
ATP-diphosphate exchange
0.43
L-Pro
-
ATP-diphosphate exchange
0.45
L-Pro
-
ATP-diphosphate exchange
0.45
L-Pro
-
ATP-diphosphate exchange
0.625
L-Pro
-
ATP-diphosphate exchange
0.0046
L-proline
pH 7.0, 37°C
0.012
L-proline
-
60°C, pH not specified in the publication, ATP-diphosphate exchange assay
0.027
L-proline
aminoacylation reaction, recombinant wild-type enzyme, pH 7.0, 70°C
0.05
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.06
L-proline
-
recombinant enzyme, pH 7.2, 60°C
0.06
L-proline
-
isozyme ProRS-Cyt, at pH 7.2 and 30°C
0.061
L-proline
-
presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5
0.067
L-proline
-
ATP-diphosphate exchange reaction, pH 7.5, 35°C
0.067
L-proline
-
presence of bovine serum albumine, 50°C, pH 7.5
0.08
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.1
L-proline
-
isozyme ProRS-Org, at pH 7.2 and 30°C
0.11
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.14
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.14
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.15
L-proline
-
recombinant enzyme, pH 7.2, 60°C
0.15
L-proline
-
pH 7.5, 37°C, mutant K279A
0.16
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.17
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.18
L-proline
-
wild type enzyme, at pH 7.5 and 22°C
0.18
L-proline
-
wild type enzyme, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.19
L-proline
-
mutant enzyme K297E/E303K, at pH 7.5 and 22°C
0.199
L-proline
-
mutant enzyme E303D, at pH 7.5 and 22°C
0.216
L-proline
-
mutant enzyme E303A, at pH 7.5 and 22°C
0.22
L-proline
-
mutant enzyme H302A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.22
L-proline
-
mutant enzyme K297E, at pH 7.5 and 22°C
0.228
L-proline
wild type enzyme, at pH 7.0 and 22°C
0.25
L-proline
-
pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation
0.26
L-proline
-
recombinant enzyme, pH 7.2, 60°C
0.28
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.28
L-proline
-
recombinant enzyme, pH 7.2, 60°C
0.285
L-proline
-
ATP-diphosphate exchange reaction, pH 7.5, 35°C
0.29
L-proline
-
recombinant enzyme, pH 7.2, 37°C
0.3
L-proline
-
mutant enzyme E303K, at pH 7.5 and 22°C
0.3
L-proline
-
mutant enzyme G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.33
L-proline
-
mutant enzyme D198A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.427
L-proline
mutant enzyme G217A, at pH 7.0 and 22°C
0.45
L-proline
-
mutant enzyme N305A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.62
L-proline
-
mutant enzyme H302A/G412A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
0.76
L-proline
-
mutant enzyme F415A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
1.03
L-proline
-
mutant enzyme E234A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
3.4
L-proline
mutant enzyme E218A, at pH 7.0 and 22°C
3.4
L-proline
-
mutant enzyme E218A, in 50 mM HEPES (pH 7.5), 20 mM KCl, 25 mM MgCl2, at 37°C
31
L-proline
-
pH 7.5, 37°C, mutant K279A
50
L-proline
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation
45
N-methylglycine
-
ATP-diphosphate exchange
67
N-methylglycine
-
ATP-diphosphate exchange
100
N-methylglycine
-
ATP-diphosphate exchange
140
N-methylglycine
-
ATP-diphosphate exchange
300
N-methylglycine
-
approximate value, , ATP-diphosphate exchange
0.12
Pro
-
-
0.4
Pro
-
ATP-diphosphate exchange
0.8
Pro
-
3-thiaproline, , ATP-diphosphate exchange
0.00003
tRNAPro
pH 7.0, 37°C
0.000131
tRNAPro
-
pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation
0.0014
tRNAPro
-
presence of bovine serum albumine and leucyl-tRNA synthetase, 50°C, pH 7.5
0.002
tRNAPro
-
pH 7.0, 55°C, C-terminal deletion mutant
0.0022
tRNAPro
-
pH 7.0, 55°C, wild-type
0.0022
tRNAPro
-
presence of leucyl-tRNA synthetase, 50°C, pH 7.5
0.0024
tRNAPro
-
presence of bovine serum albumine, 50°C, pH 7.5
0.0041
tRNAPro
-
50°C, pH 7.5
0.01414
tRNAPro
-
pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
ProRS and leucyl-tRNA synthetase, LeuRS, interaction kinetics
-
additional information
additional information
-
single turnover and burst kinetics, steady-state kinetics, recombinant His-tagged enzyme, overview
-
additional information
additional information
-
wild-type and mutant enzyme kinetics
-
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G331A
the mutant shows 6.7fold increased activity compared to the wild type enzyme
G334A
the mutant shows 2.2fold increased activity compared to the wild type enzyme
H366A
the mutant shows 4.4fold increased activity compared to the wild type enzyme
I263A
the mutant shows 2.4fold increased activity compared to the wild type enzyme
I278A
the mutant shows 12.8fold increased activity compared to the wild type enzyme
I333A
the mutant shows 54.7fold increased activity compared to the wild type enzyme
K279A
the mutant shows 2006.3fold increased activity compared to the wild type enzyme
S280A
the mutant shows 2fold increased activity compared to the wild type enzyme
S332A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
T257A
the mutant shows 1.1fold increased activity compared to the wild type enzyme
C443A
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443G
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
C443S
-
mutagenesis of C443 to amino acids Ala, Gly and Ser results in significant decreases, 16fold to 225fold in kcat/KmPro, as measured by the ATP-diphosphate exchange assay. The Ala and Gly mutations have relatively small effect, 4fold to 7fold, on the overall aminoacylation reaction, while the activity of the C443 mutant in this same assay is substantially reduced, 80fold
D198A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
D350A
-
site-directed mutagenesis, subdomain III mutant, residual remaining aminoaclyation activity, no pre-transfer editing activity
D378A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D386A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
D394A
-
site-directed mutagenesis, subdomain III mutant, reduced aminoaclyation and pre-transfer editing activity
E218A
the mutant activates proline but with a decreased kcat (3fold) and elevated KM value (15fold). Overall proline activation efficiency of this mutant is decreased 45fold compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
E234A
-
the overall aminoacylation activity of the mutant is reduced 2fold
E303A
-
the mutation results in 3fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303D
-
the mutation results in 3.1fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
E303K
-
the mutation results in 4.2fold decrease in L-proline activation. The mutant exhibits a small decrease in the aminoacylation efficiency
F415A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
G217A
the kcat/KM of the mutant is reduced 7fold relative to the wild type enzyme. In contrast, alanine activation by the G217A mutant is not affected compared to the wild type enzyme. A 2fold decrease in alanine activation s observed for the mutant compared to the wild type enzyme. The mutant also can charge L-proline onto tRNAPro, albeit with 3fold reduced efficiency
G412A
-
the overall aminoacylation activity of the mutant is reduced 7fold
H302A
-
the overall aminoacylation activity of the mutant is reduced 2fold
H302A/G412A
-
the overall aminoacylation activity of the mutant is reduced 5.5fold
H366A
-
the mutant shows loss in L-alanine deacylation activity
H369A
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
H369C
-
site-directed mutagenesis, subdomain III mutant, highly reduced reduced aminoaclyation and pre-transfer editing activity, deacetylates Pro-tRNAPro
K279E
-
the mutation results in 2.7fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
K279E/E303K
-
the mutant shows 2.3fold reduced L-proline activation. The mutant exhibits wild type aminoacylation efficiency
L266A
-
the mutant shows negligible in L-alanine deacylation at room temperature
N305A
-
the aminoacylation activity of the mutant is nearly abolished with rates 70fold slower than the wild type
R144K
-
site-directed mutagenesis, the mutant shows 480fold reduced activity compared to the wild-type enzyme
R144L
-
site-directed mutagenesis, the mutant shows 870fold reduced activity compared to the wild-type enzyme
R146C
-
site-directed mutagenesis, the mutant shows 79fold reduced activity compared to the wild-type enzyme
T257A
-
site-directed mutagenesis, subdomain I mutant, reduced aminoaclyation and pre-transfer editing activity
V143C
-
site-directed mutagenesis, the mutant shows 3fold reduced activity compared to the wild-type enzyme
A57G
-
site-directed mutagenesis, the A57G mutation introduces a BstBI restriction site within the gene, but has no effect on catalytic activity
F1097A
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
F1097W
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152K
the mutant shows increased aminoacylation activity compared to the wild type enzyme
R1152L
the mutant shows strongly decreased aminoacylation activity compared to the wild type enzyme
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
E103A
-
unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme
-
P100A
-
unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme
-
R1152L
catalytically inactive
R201L/R395L/S434A/K435L
catalytic mutant
S886D
phosphomimetic mutant
S886D/S990D
phosphomimetic mutant
S886D/S999D
phosphomimetic mutant
S999D
phosphomimetic mutant
R1152L
-
catalytically inactive
-
S990A
-
phosphorylation-resistant mutant
-
K279A
-
site-directed mutagenesis
K279A
-
site-directed mutagenesis, subdomain II mutant, reduced aminoaclyation and pre-transfer editing activity
E103A
-
abolished activity with L-proline
E103A
unaltered thermostability, no remaining prolylation activity, 5% remaining cysteinylation activity compared to the wild-type enzyme
P100A
-
highly reduced activity with L-cysteine
P100A
unaltered thermostability, loss of 90% cysteinylation activity, unaltered prolylation activity compared to the wild-type enzyme
S990A
phosphorylation-resistant mutant
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
phosphomimetic mutant
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
S990D
-
phosphomimetic mutant
-
S990D
-
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
-
additional information
-
replacement of 163 residues of the INS domain, amino acids 232-394, with either an 8-residue Gly6Ser2 linker or a 16-residue Gly12Ser4 linker by PCR amplification of the full-length plasmid pCS-M1S
additional information
siRNA-mediated enzyme knockout in HEK-293T cells. Cells in which EPRS is knocked down show considerable attenuation of the production of antiviral cytokines (IFN-beta and interleukin-6) following viral infection or treatment with the synthetic double-stranded RNA poly(I:C). Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts
additional information
-
the C-terminally truncated enzyme is 3fold less active with L-cysteine and 10fold less active with L-alanine compared too the wild-type enzyme
additional information
-
C-terminal deletion mutant lacking last 50 amino acids, little effect on kinetic parameters
additional information
-
the dual-specific enzyme is sufficient for Cys-tRNACys production in a mutant disrupted in the gene encoing the canonical CysRS
additional information
siRNA-mediated enzyme knockout in RAW-264.7 cells. Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts . RAW-264.7 cells stably overexpressing EPRS show significantly less viral replication and more production of IFN-beta and interleukin-6 following infection with PR8 or VSV than those of their counterparts with basal expression of EPRS
additional information
-
transfection of MEF cells with the PTK-EPRS-Luc reporter followed by either halofuginone treatment or no treatment
additional information
-
siRNA-mediated enzyme knockout in RAW-264.7 cells. Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts . RAW-264.7 cells stably overexpressing EPRS show significantly less viral replication and more production of IFN-beta and interleukin-6 following infection with PR8 or VSV than those of their counterparts with basal expression of EPRS
-
additional information
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
additional information
-
generation of conditional expression strains, conditional expression plasmids are electroporated into Mycobacterium smegmatis strain mc2155, analysis of inducer dependency of conditional expression strains, overview
-
additional information
-
development of a heterologous archaeal prolyl-tRNA/prolyl-tRNA synthase pair, Archaeoglobus fulgidus tRNAPro (AftRNAPro)/Pyrococcus horikoshii ProRS (PhProRS), for UAA mutagenesis in Escherichia coli. Modification of the anticodon-binding pocket of Pyrococcus horikoshii prolyl-tRNA synthase reestablishes its functional binding interaction with multiple anticodon-variants of tRNAPro
additional information
-
construction of a truncated Sc ProRS mutant lacking the N-terminal 183 residues, ScDELTA183, which shows reduced enzyme activity compared to the wild-type enzyme, overview
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Ogata, K.; Kurahashi, A.; Tanaka, S.; Ohsue, H.; Terao, K.
Occurence of 5SrRNA in high molecular weight complexes of aminoacyl-tRNA synthetases in a rat liver supernatant
J. Biochem.
110
1030-1036
1991
Rattus norvegicus
brenda
Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.
Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes
Biochemistry
22
1934-1941
1983
Bos taurus
brenda
Norcum, M.T.
Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells
J. Biol. Chem.
264
15043-15051
1989
Mus musculus
brenda
Heacock, D.; Forsyth, C.J.; Shiba, K.; Musier-Forsyth, K.
Synthesis and aminoacyl-tRNA synthetase inhibitory activity of prolyl adenylate analogs
Bioorg. Chem.
24
273-289
1996
Escherichia coli
-
brenda
Kerjan, P.; Triconnet, M.; Waller, J.P.
Mammalian prolyl-tRNA synthetase corresponds to the approximately 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complex
Biochimie
74
195-205
1992
Homo sapiens, Mammalia, Ovis aries
brenda
Ting, S.M.; Bogner, P.; Dignam, J.D.
Isolation of prolyl-tRNA synthetase as a free form and as a form associated with glutamyl-tRNA synthetase
J. Biol. Chem.
267
17701-17709
1992
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