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Literature summary for 6.1.1.15 extracted from

  • Ambrogelly, A.; Ahel, I.; Polycarpo, C.; Bunjun-Srihari, S.; Krett, B.; Jacquin-Becker, C.; Ruan, B.; Kohrer, C.; Stathopoulos, C.; RajBhandary, U.L.; Soll, D.
    Methanocaldococcus jannaschii prolyl-tRNA synthetase charges tRNA(Pro) with cysteine (2002), J. Biol. Chem., 277, 34749-34754.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and C-terminally truncated enzymes as His-tagged proteins in Escherichia coli Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
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 Methanocaldococcus jannaschii

Inhibitors

Inhibitors Comment Organism Structure
cysteamine inhibition of Cys-tRNAPro formation Methanocaldococcus jannaschii
D-cysteine-DL-homocysteine inhibition of Cys-tRNAPro formation Methanocaldococcus jannaschii
L-cysteine ethyl ester inhibition of Cys-tRNAPro formation Methanocaldococcus jannaschii
L-cysteine methyl ester inhibition of Cys-tRNAPro formation Methanocaldococcus jannaschii
additional information no inhibition of Cys-tRNAPro formation by L-sulfinic acid, L-cysteic acid, S-methyl L-cysteine, and homocysteine thiolactone Methanocaldococcus jannaschii
N-acetyl-L-cysteine inhibition of Cys-tRNAPro formation Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-proline + tRNAPro Methanocaldococcus jannaschii
-
AMP + diphosphate + L-prolyl-tRNAPro
-
?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
gene proS
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and C-terminally truncated enzymes from overexpressing Escherichia coli Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAPro misacetylation of tRNAPro, no editing Methanocaldococcus jannaschii AMP + diphosphate + L-alanyl-tRNAPro
-
?
ATP + L-cysteine + tRNAPro misacetylation of tRNAPro, no editing Methanocaldococcus jannaschii AMP + diphosphate + L-cysteinyl-tRNAPro
-
?
ATP + L-proline + tRNAPro
-
Methanocaldococcus jannaschii AMP + diphosphate + L-prolyl-tRNAPro
-
?
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 Methanocaldococcus jannaschii ?
-
?

Synonyms

Synonyms Comment Organism
Global RNA synthesis factor
-
Methanocaldococcus jannaschii
Pro-tRNA synthetase
-
Methanocaldococcus jannaschii
Proline translase
-
Methanocaldococcus jannaschii
Proline--tRNA ligase
-
Methanocaldococcus jannaschii
Prolyl RNA synthetase
-
Methanocaldococcus jannaschii
Prolyl-transfer ribonucleate synthetase
-
Methanocaldococcus jannaschii
Prolyl-transfer ribonucleic acid synthetase
-
Methanocaldococcus jannaschii
Prolyl-transfer RNA synthetase
-
Methanocaldococcus jannaschii
Prolyl-tRNA synthetase
-
Methanocaldococcus jannaschii
ProRS
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Methanocaldococcus jannaschii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
aminoacylation assay at Methanocaldococcus jannaschii
7.2
-
ATP-diphosphate exchange assay at Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Methanocaldococcus jannaschii