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Literature summary extracted from

  • Lesjak, S.; Boko, D.; Weygand-Durasevic, I.
    Seryl-tRNA synthetases from methanogenic archaea: suppression of bacterial amber mutation and heterologous toxicity (2010), Food Technol. Biotechnol., 48, 512-518.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.11 expression of the archaeal SerRS in Escherichia coli, wild-type strain KL229 and derivatives, and Saccharomyces cerevisiae. Although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae. But coexpression of methanogenic-type SerRS with its cognate tRNA leads to complementation suppressing the bacterial amber mutation Methanocaldococcus jannaschii
6.1.1.11 expression of wild type or mutant C315A archaeal SerRS in Escherichia coli, wild-type strain KL229 and derivatives, and Saccharomyces cerevisiae. Although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae. But coexpression of methanogenic-type SerRS with its cognate tRNA leads to complementation suppressing the bacterial amber mutation Methanococcus maripaludis

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.11 C315A site-directed mutagenesis Methanococcus maripaludis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.11 Mg2+ required Methanocaldococcus jannaschii
6.1.1.11 Mg2+ required Methanococcus maripaludis
6.1.1.11 Zn2+ catalytic zinc ion in the active site Methanocaldococcus jannaschii
6.1.1.11 Zn2+ catalytic zinc ion in the active site Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.11 ATP + L-serine + tRNASer Methanocaldococcus jannaschii
-
 AMP + diphosphate + L-seryl-tRNASer
-
 ?
6.1.1.11 ATP + L-serine + tRNASer Methanococcus maripaludis
-
 AMP + diphosphate + L-seryl-tRNASer
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.11 Methanocaldococcus jannaschii
-
-
-
6.1.1.11 Methanococcus maripaludis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.11 ATP + L-serine + tRNASer
-
 Methanocaldococcus jannaschii AMP + diphosphate + L-seryl-tRNASer
-
 ?
6.1.1.11 ATP + L-serine + tRNASer
-
 Methanococcus maripaludis AMP + diphosphate + L-seryl-tRNASer
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.11 More the enzyme has a idiosyncratic N-terminal domain, structure analysis, overview Methanocaldococcus jannaschii
6.1.1.11 More the enzyme has a idiosyncratic N-terminal domain, structure analysis, overview Methanococcus maripaludis

Synonyms

EC Number Synonyms Comment Organism
6.1.1.11 SerRS
-
 Methanocaldococcus jannaschii
6.1.1.11 SerRS
-
 Methanococcus maripaludis
6.1.1.11 Seryl-tRNA synthetase
-
 Methanocaldococcus jannaschii
6.1.1.11 Seryl-tRNA synthetase
-
 Methanococcus maripaludis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.11 30
-
 assay at Methanocaldococcus jannaschii
6.1.1.11 30
-
 assay at Methanococcus maripaludis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.11 7.5
-
 assay at Methanocaldococcus jannaschii
6.1.1.11 7.5
-
 assay at Methanococcus maripaludis

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.11 ATP
-
 Methanocaldococcus jannaschii
6.1.1.11 ATP
-
 Methanococcus maripaludis

General Information

EC Number General Information Comment Organism
6.1.1.11 evolution although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae Methanocaldococcus jannaschii
6.1.1.11 evolution although SerRSs from methanogenic archaea recognize tRNAsSer from all three domains of life in vitro, the toxicity presumably precludes the complementation of endogenous SerRS function in both, Escherichia coli and Saccharomyces cerevisiae Methanococcus maripaludis
6.1.1.11 additional information expression of methanogenic-type SerRSs is toxic for Escherichia coli cells Methanocaldococcus jannaschii
6.1.1.11 additional information expression of methanogenic-type SerRSs is toxic for Escherichia coli cells Methanococcus maripaludis