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Literature summary extracted from

  • Hati, S.; Ziervogel, B.; Sternjohn, J.; Wong, F.C.; Nagan, M.C.; Rosen, A.E.; Siliciano, P.G.; Chihade, J.W.; Musier-Forsyth, K.
    Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in 'selective release' of noncognate amino acids (2006), J. Biol. Chem., 281, 27862-27872.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.15 gene proS, expression in Escherichia coli strain BL21(DE3) Methanothermobacter thermautotrophicus
6.1.1.15 gene proS, expression in Escherichia coli strain BL21(DE3) Methanocaldococcus jannaschii
6.1.1.15 gene proS, expression in Escherichia coli strain SG13009 Methanococcus maripaludis
6.1.1.15 gene proS, overexpression of His-tagged wild-type ProRS and truncation mutant ScDELTA183 Saccharomyces cerevisiae
6.1.1.15 gene proS, overexpression of wild-type and mutant His-tagged ProRS Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.15 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 Saccharomyces cerevisiae
6.1.1.15 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 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.15 5'-O-[N-(L-alanyl)-sulfamoyl]adenosine a non-hydrolyzable adenylate analogue, a potent inhibitor of the ATP-diphosphate exchange reaction Escherichia coli
6.1.1.15 5'-O-[N-(L-Prolyl)-sulfamoyl]adenosine a non-hydrolyzable adenylate analogue Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.15 0.000131
-
tRNAPro pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation Escherichia coli
6.1.1.15 0.01414
-
tRNAPro pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation Escherichia coli
6.1.1.15 0.25
-
L-proline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 2 37 trans-4-hydroxyproline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 50
-
L-proline pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation Escherichia coli
6.1.1.15 53
-
cis-4-hydroxyproline pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation Escherichia coli
6.1.1.15 55
-
cis-4-hydroxyproline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 140
-
L-alanine pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.15 Mg2+
-
Escherichia coli
6.1.1.15 Mg2+
-
Saccharomyces cerevisiae
6.1.1.15 Mg2+
-
Methanothermobacter thermautotrophicus
6.1.1.15 Mg2+
-
Methanocaldococcus jannaschii
6.1.1.15 Mg2+
-
Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.15 ATP + L-proline + tRNAPro Escherichia coli
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro Saccharomyces cerevisiae
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro Methanothermobacter thermautotrophicus
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro Methanocaldococcus jannaschii
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro Methanococcus maripaludis
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.15 Escherichia coli
-
-
-
6.1.1.15 Methanocaldococcus jannaschii
-
gene proS
-
6.1.1.15 Methanococcus maripaludis
-
gene proS
-
6.1.1.15 Methanothermobacter thermautotrophicus
-
gene proS
-
6.1.1.15 Saccharomyces cerevisiae
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.1.1.15 additional information
-
-
Saccharomyces cerevisiae
6.1.1.15 additional information
-
-
Methanothermobacter thermautotrophicus
6.1.1.15 additional information
-
-
Methanocaldococcus jannaschii
6.1.1.15 additional information
-
-
Methanococcus maripaludis
6.1.1.15 additional information
-
activities of wild-type and mutant enzymes, pre-transfer editing activity, overview Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.15 ATP + cis-4-hydroxyproline + tRNAPro
-
Escherichia coli AMP + diphosphate + cis-4-hydroxyprolyl-tRNAPro
-
?
6.1.1.15 ATP + L-alanine + tRNAPro L-alanine is a poor substrate Escherichia coli AMP + diphosphate + L-alanyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro
-
Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro
-
Saccharomyces cerevisiae AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro
-
Methanothermobacter thermautotrophicus AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro
-
Methanocaldococcus jannaschii AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + tRNAPro
-
Methanococcus maripaludis AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + L-proline + 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 Escherichia coli AMP + diphosphate + L-prolyl-tRNAPro
-
?
6.1.1.15 ATP + trans-4-hydroxyproline + tRNAPro
-
Escherichia coli AMP + diphosphate + trans-4-hydroxyprolyl-tRNAPro
-
?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.15 class II prolyl-tRNA synthetase
-
Escherichia coli
6.1.1.15 class II prolyl-tRNA synthetase
-
Saccharomyces cerevisiae
6.1.1.15 class II prolyl-tRNA synthetase
-
Methanothermobacter thermautotrophicus
6.1.1.15 class II prolyl-tRNA synthetase
-
Methanocaldococcus jannaschii
6.1.1.15 class II prolyl-tRNA synthetase
-
Methanococcus maripaludis
6.1.1.15 Prolyl-tRNA synthetase
-
Escherichia coli
6.1.1.15 Prolyl-tRNA synthetase
-
Saccharomyces cerevisiae
6.1.1.15 Prolyl-tRNA synthetase
-
Methanothermobacter thermautotrophicus
6.1.1.15 Prolyl-tRNA synthetase
-
Methanocaldococcus jannaschii
6.1.1.15 Prolyl-tRNA synthetase
-
Methanococcus maripaludis
6.1.1.15 ProRS
-
Escherichia coli
6.1.1.15 ProRS
-
Saccharomyces cerevisiae
6.1.1.15 ProRS
-
Methanothermobacter thermautotrophicus
6.1.1.15 ProRS
-
Methanocaldococcus jannaschii
6.1.1.15 ProRS
-
Methanococcus maripaludis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.15 37
-
assay at Saccharomyces cerevisiae
6.1.1.15 37
-
assay at Methanothermobacter thermautotrophicus
6.1.1.15 37
-
assay at Methanocaldococcus jannaschii
6.1.1.15 37
-
assay at Methanococcus maripaludis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.15 0.0091
-
tRNAPro pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, aminoacylation Escherichia coli
6.1.1.15 0.056
-
cis-4-hydroxyproline pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation Escherichia coli
6.1.1.15 0.239
-
tRNAPro pH 7.0, 37°C, recombinant wild-type enzyme, aminoacylation Escherichia coli
6.1.1.15 1.7
-
L-alanine pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 12
-
L-proline pH 7.0, 37°C, recombinant mutant EcDELTAINS Gly12Ser4, amino acid activation Escherichia coli
6.1.1.15 15
-
trans-4-hydroxyproline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 21
-
cis-4-hydroxyproline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli
6.1.1.15 70
-
L-proline pH 7.0, 37°C, recombinant wild-type enzyme, amino acid activation Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.15 7
-
assay at Saccharomyces cerevisiae
6.1.1.15 7
-
assay at Methanothermobacter thermautotrophicus
6.1.1.15 7
-
assay at Methanocaldococcus jannaschii
6.1.1.15 7
-
assay at Methanococcus maripaludis

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.15 ATP
-
Escherichia coli
6.1.1.15 ATP
-
Saccharomyces cerevisiae
6.1.1.15 ATP
-
Methanothermobacter thermautotrophicus
6.1.1.15 ATP
-
Methanocaldococcus jannaschii
6.1.1.15 ATP
-
Methanococcus maripaludis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.15 0.0000043 0.000088 5'-O-[N-(L-alanyl)-sulfamoyl]adenosine ATP-diphosphate exchange reaction, pH 7.0, 37°C, recombinant wild-type enzyme Escherichia coli