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Literature summary extracted from

  • Korencic, D.; Ahel, I.; Schelert, J.; Sacher, M.; Ruan, B.; Stathopoulos, C.; Blum, P.; Ibba, M.; Soll, D.
    A freestanding proofreading domain is required for protein synthesis quality control in archaea (2004), Proc. Natl. Acad. Sci. USA, 101, 10260-10265.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 gene thrS, expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Saccharolobus solfataricus
6.1.1.3 gene thrS, expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 additional information construction of mutants consisting of catalytic or editing enzyme domains, overview Methanocaldococcus jannaschii
6.1.1.3 additional information construction of mutants consisting of catalytic or editing enzyme domains, overview, construction of mutant strain PBL205 with a disruption of gene thrS, i.e. SSO3004-3050 Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 additional information
-
 additional information kinetics of recombinant wild-type and mutant enzymes with threonine and serine Saccharolobus solfataricus
6.1.1.3 additional information
-
 additional information kinetics of recombinant wild-type and mutant enzymes with threonine and serine Methanocaldococcus jannaschii
6.1.1.3 0.1
-
 L-threonine pH 7.2, 60°C, recombinant wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 0.11
-
 L-threonine pH 7.2, 60°C, recombinant wild-type enzyme Saccharolobus solfataricus
6.1.1.3 25
-
 L-serine pH 7.2, 60°C, recombinant wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 55
-
 L-serine pH 7.2, 60°C, recombinant wild-type enzyme Saccharolobus solfataricus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+
-
 Saccharolobus solfataricus
6.1.1.3 Mg2+
-
 Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr Saccharolobus solfataricus
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 additional information Saccharolobus solfataricus a freestanding proofreading domain is required for protein synthesis quality control in archaea ?
-
 ?
6.1.1.3 additional information Methanocaldococcus jannaschii a freestanding proofreading domain is required for protein synthesis quality control in archaea ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Methanocaldococcus jannaschii Q58597
-
-
6.1.1.3 Saccharolobus solfataricus Q980D1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + L-serine + tRNAThr
-
 Saccharolobus solfataricus AMP + diphosphate + L-seryl-tRNAThr
-
 ?
6.1.1.3 ATP + L-serine + tRNAThr L-serine is a poor substrate for the wild-type enzyme Methanocaldococcus jannaschii AMP + diphosphate + L-seryl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Saccharolobus solfataricus AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-threonyl-tRNAThr
-
 r
6.1.1.3 additional information a freestanding proofreading domain is required for protein synthesis quality control in archaea Saccharolobus solfataricus ?
-
 ?
6.1.1.3 additional information a freestanding proofreading domain is required for protein synthesis quality control in archaea Methanocaldococcus jannaschii ?
-
 ?
6.1.1.3 additional information L-serine is a poor substrate for the wild-type enzyme, the N-terminal enzyme domain is responsible for editing Saccharolobus solfataricus ?
-
 ?
6.1.1.3 additional information the N-terminal enzyme domain is responsible for editing Methanocaldococcus jannaschii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.3 More the N-terminal enzyme domain is responsible for editing Saccharolobus solfataricus
6.1.1.3 More the N-terminal enzyme domain is responsible for editing Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 ThrRS
-
 Saccharolobus solfataricus
6.1.1.3 ThrRS
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 60
-
 assay at Saccharolobus solfataricus
6.1.1.3 60
-
 assay at Methanocaldococcus jannaschii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 1.3
-
 L-serine pH 7.2, 60°C, recombinant wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 1.9
-
 L-threonine pH 7.2, 60°C, recombinant wild-type enzyme Methanocaldococcus jannaschii
6.1.1.3 12.3
-
 L-serine pH 7.2, 60°C, recombinant wild-type enzyme Saccharolobus solfataricus
6.1.1.3 13.5
-
 L-threonine pH 7.2, 60°C, recombinant wild-type enzyme Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 7.2
-
 assay at Saccharolobus solfataricus
6.1.1.3 7.2
-
 assay at Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 AMP
-
 Saccharolobus solfataricus
6.1.1.3 AMP
-
 Methanocaldococcus jannaschii
6.1.1.3 ATP
-
 Saccharolobus solfataricus
6.1.1.3 ATP
-
 Methanocaldococcus jannaschii