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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
-
?