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Literature summary extracted from

  • Zhang, C.M.; Liu, C.; Slater, S.; Hou, Y.M.
    Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNA(Cys) (2008), Nat. Struct. Mol. Biol., 15, 507-514.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.73 expressed in Escherichia coli BL21(DE3)-RIL cells Methanocaldococcus jannaschii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.27 additional information
-
 additional information steady-state and single-turnover kinetics, kinetic analysis, overview Methanocaldococcus jannaschii
6.1.1.27 0.00097
-
 m1G37-tRNACys 60°C, pH 6.0, steady-state kinetics Methanocaldococcus jannaschii
6.1.1.27 0.0011
-
 tRNACys 60°C, pH 6.0, steady-state kinetics Methanocaldococcus jannaschii
6.1.1.27 0.007
-
 tRNACys pH 7.5, 37°C, recombinant enzyme, native tRNACys Methanocaldococcus jannaschii
6.1.1.27 0.0097
-
 tRNACys pH 7.5, 37°C, recombinant enzyme, m1G37 tRNACys Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.27 Mg2+
-
 Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide Methanocaldococcus jannaschii Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl–tRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNA–Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine L-cysteinyl-tRNACys + phosphate
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys Methanocaldococcus jannaschii
-
 AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys Methanocaldococcus jannaschii Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl–tRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNA–Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 additional information Methanocaldococcus jannaschii Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl-tRNA synthetase acylates tRNACys with phosphoserine, and Sep-tRNA-Cys-tRNA synthase converts the tRNA-bound phosphoserine to cysteine. Methanocaldococcus jannaschii SepRS differs from CysRS by recruiting the m1G37 modification as a determinant for aminoacylation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.73 Methanocaldococcus jannaschii
-
-
-
2.5.1.73 Methanocaldococcus jannaschii Q59072
-
-
6.1.1.16 Escherichia coli
-
-
-
6.1.1.27 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.73 Q Sepharose FF column chromatography and FPLC Mono Q column chromatography Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide
-
 Methanocaldococcus jannaschii L-cysteinyl-tRNACys + phosphate
-
 ?
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl–tRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNA–Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine Methanocaldococcus jannaschii L-cysteinyl-tRNACys + phosphate
-
 ?
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl–tRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNA–Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine. O-Phosphoseryl–tRNA synthetase and Sep-tRNA–Cys-tRNA synthase bind the reaction intermediate O-phospho-L-serine-tRNACys tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1a or infiltrating into the ribosome Methanocaldococcus jannaschii L-cysteinyl-tRNACys + phosphate
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACys
-
 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACys
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACysA36G relative activity compared to wild-type tRNACys as a substrate: 0.01 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACysA36G
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACysC35U relative activity compared to wild-type tRNACys as a substrate: 0.005 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACysC35U
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACysG15C/C48G relative activity compared to wild-type tRNACys as a substrate: 0.03 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACysG15C/C48G
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACysG34C relative activity compared to wild-type tRNACys as a substrate: 0.001 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACysG34C
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACysU73G relative activity compared to wild-type tRNACys as a substrate: 0.00002 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACysU73G
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + m1G37-tRNACys
-
 Methanocaldococcus jannaschii AMP + diphosphate + O-phospho-L-seryl-m1G37-tRNACys
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys
-
 Methanocaldococcus jannaschii AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl–tRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNA–Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine Methanocaldococcus jannaschii AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys SepRS differs from CysRS (EC 6.1.1.16) by recruiting the m1G37 modification as a determinant for aminoacylation, and in showing limited discrimination against mutations of conserved nucleotides. O-Phosphoseryl–tRNA synthetase and Sep-tRNA–Cys-tRNA synthase bind the reaction intermediate O-phospho-L-serine-tRNACys tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1a or infiltrating into the ribosome Methanocaldococcus jannaschii AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 ATP + O-phospho-L-serine + tRNACys SepRS differs from CysRS by recruiting the m1G37 modification as a determinant for aminoacylation, and in showing limited discrimination against mutations of conserved nucleotides. The enzyme requires the S-adenosylmethione-dependent formation of m1G37 in the anticodon loop for efficient aminoacylation Methanocaldococcus jannaschii AMP + diphosphate + O-phospho-L-seryl-tRNACys
-
 ?
6.1.1.27 additional information Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryl-tRNA synthetase acylates tRNACys with phosphoserine, and Sep-tRNA-Cys-tRNA synthase converts the tRNA-bound phosphoserine to cysteine. Methanocaldococcus jannaschii SepRS differs from CysRS by recruiting the m1G37 modification as a determinant for aminoacylation Methanocaldococcus jannaschii ?
-
 ?
6.1.1.27 additional information kinetic and binding measurements show that both SepRS and Sep-tRNA-Cys-tRNA synthase, SepCysS, bind the reaction intermediate Sep-tRNACys tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1alpha or infiltrating into the ribosome, mechanism of the binary complex, detailed overview Methanocaldococcus jannaschii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.73 More both SepRS and SepCysS are active as a monomer in theSepRS–SepCysS binary complex Methanocaldococcus jannaschii
6.1.1.27 More both SepRS and SepCysS are active as a monomer in theSepRS–SepCysS binary complex Methanocaldococcus jannaschii
6.1.1.27 tetramer SepRS contains two tRNACys molecules per tetramer indicating an asymmetry of the four identical subunits Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
2.5.1.73 Sep-tRNA-Cys-tRNA synthase both SepRS and SepCysS bind the reaction intermediate Sep-tRNACys tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1alpha or infiltrating into the ribosome Methanocaldococcus jannaschii
2.5.1.73 SepCysS
-
 Methanocaldococcus jannaschii
2.5.1.73 SepCysS SepRS–SepCysS binary complex Methanocaldococcus jannaschii
6.1.1.16 CysRS
-
 Escherichia coli
6.1.1.16 Cysteinyl-tRNA synthetase
-
 Escherichia coli
6.1.1.27 SepRS SepRS–SepCysS binary complex Methanocaldococcus jannaschii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.27 0.07
-
 tRNACys 60°C, pH 6.0, steady-state kinetics Methanocaldococcus jannaschii
6.1.1.27 0.24
-
 m1G37-tRNACys 60°C, pH 6.0, steady-state kinetics Methanocaldococcus jannaschii
6.1.1.27 0.24
-
 tRNACys pH 7.5, 37°C, recombinant enzyme, m1G37 tRNACys Methanocaldococcus jannaschii
6.1.1.27 1
-
 tRNACys pH 7.5, 37°C, recombinant enzyme, native tRNACys Methanocaldococcus jannaschii

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.27 ATP
-
 Methanocaldococcus jannaschii