6.1.1.27: O-phospho-L-serine-tRNA ligase
This is an abbreviated version!
For detailed information about O-phospho-L-serine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.27
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6.1.1.27
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cys-trnacys
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methanogen
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aminoacylation
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archaea
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sepcyss
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cysteinyl-trna
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sep-trna:cys-trna
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o-phosphoserine
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anticodons
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aminoacyl-trnas
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maripaludis
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trna-dependent
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cysteinyl-trnacys
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selenocysteine
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methanocaldococcus
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jannaschii
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phosphoserylation
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pylrs
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aarss
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faithful
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mazei
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methanosarcina
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gca
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alpha4
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web-based
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biologists
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phenylalanyl-trna
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asnrs
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ilers
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biotechnology
- 6.1.1.27
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cys-trnacys
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methanogen
- aminoacylation
- archaea
- sepcyss
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cysteinyl-trna
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sep-trna:cys-trna
- o-phosphoserine
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anticodons
- aminoacyl-trnas
- maripaludis
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trna-dependent
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cysteinyl-trnacys
- selenocysteine
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methanocaldococcus
- jannaschii
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phosphoserylation
- pylrs
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aarss
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faithful
- mazei
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methanosarcina
- gca
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alpha4
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web-based
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biologists
- phenylalanyl-trna
- asnrs
- ilers
- biotechnology
Reaction
Synonyms
CysRS, Cysteinyl-tRNA synthetase, More, O-phosphoseryl-tRNA synthetase, phosphoseryl-tRNA synthetase, phosphoseryl-tRNA synthetases, SepRS, sepS
ECTree
6.1.1.27 O-phospho-L-serine-tRNA ligaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 6.1.1.27 - O-phospho-L-serine-tRNA ligase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + O-phospho-L-serine + m1G37-tRNACys
AMP + diphosphate + O-phospho-L-seryl-m1G37-tRNACys
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ATP + O-phospho-L-serine + tRNAAmber
AMP + diphosphate + O-phospho-L-serine-tRNAAmber
recognition of U34 and C35 of tRNAAmber by mutant E418N/E420N, no activity with wild-type SepRS, overview
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ATP + O-phospho-L-serine + tRNAAmber
AMP + diphosphate + O-phospho-L-seryl-tRNAAmber
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mutant D418N/D420N/T423V
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?
ATP + O-phospho-L-serine + tRNAOpal
AMP + diphosphate + O-phospho-L-serine-tRNAOpal
recognition of U34 and C35 of tRNAOpal by mutant E418N/E420N, no activity with wild-type SepRS, overview
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?
ATP + O-phospho-L-serine + tRNAOpal
AMP + diphosphate + O-phospho-L-seryl-tRNAOpal
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mutant D418N/D420N/T423V
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-serine-tRNACys
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-serine-tRNACys
tRNA substrate from Escherichia coli, wheat germ and Saccharomyces cerevisiae in a mixture, the catalytic domain of SepRS recognizes the negatively charged side chain of O-phosphoserine at a noncanonical site, using the dipole moment of a conserved alpha-helix, the unique C-terminal domain specifically recognizes the anticodon GCA of tRNACys, overview
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-serine-tRNACys
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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phosphoseryl-tRNA synthetase is a natural non-standard aminoacyl-tRNA synthetase, which charges a non-standard amino acid, phosphoserine, to tRNACys containing a GCA anticodon for tRNA-dependent cysteine biosynthesis in some archaea
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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cognate substrate is tRNACys with the GCA anticodon, tRNACys containing the (pyrrole-2-carbaldehyde)UA anticodon
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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Methanocaldococcus jannaschii synthesizes Cys-tRNACys by an indirect pathway, whereby O-phosphoseryltRNA synthetase (SepRS) acylates tRNACys with phosphoserine (Sep), and Sep-tRNACys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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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-PhosphoseryltRNA synthetase and Sep-tRNACys-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
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?
ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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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
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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Methanococcus maripaludis encodes both the direct and indirect paths for Cys-tRNACys synthesis. SepS (encoding SepRS) can be deleted when the organism is grown in the presence of Cys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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the enzyme charges tRNACys with a 3'-deoxyadenosine, but not tRNACys without A76 or with a 2'-deoxyadensosine
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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half-of-the-sites activity: the tetrameric enzyme binds two tRNAs. Only two of the four chemically equivalent subunits catalyze formation of phosphoseryl adenylate
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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some methanogenic archaea synthesize Cys-tRNACys needed for protein synthesis using both a canonical cysteinyl-tRNA synthetase as well as a set of two enzymes that operate via a separate indirect pathway. In the indirect route, Sep-tRNACys is first synthesized by SepRS, and this misacylated intermediate is then converted to Cys-tRNACys by Sep-tRNA:Cys-tRNA synthase via a pyridoxal phosphate-dependent mechanism, structural basis for the tRNACys isoacceptor preferences of SepRS and CysRS, detailed overview
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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efficient phosphoserylation by SepRS requires methylation of tRNACys at the N1 position of G37 in the anticodon loop. Comparative aminoacylation kinetics by CysRS (EC 6.1.1.16) and SepRS reveals that each enzyme prefers a distinct tRNACys isoacceptor or pair of isoacceptors
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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half-of-the-sites activity: the tetrameric enzyme binds two tRNAs. Only two of the four chemically equivalent subunits catalyze formation of phosphoseryl adenylate. Efficient phosphoserylation by SepRS requires methylation of tRNACys at the N1 position of G37 in the anticodon loop
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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recognition determinants distinguishing the tRNAs reside in the globular core of the molecule. The enzyme also requires the S-adenosylmethione-dependent formation of m1G37 in the anticodon loop for efficient aminoacylation
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ATP + O-phospho-L-serine + tRNACys
AMP + diphosphate + O-phospho-L-seryl-tRNACys
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the tetrameric enzyme binds two tRNAs and only two of the four chemically equivalent subunits catalyze formation of phosphoseryl adenylate. tRNACys binding to SepRS also enhances the capacity of the enzyme to discriminate among amino acids, indicating the existence of functional connectivity between the tRNA and amino acid binding sites of the enzyme
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ATP + O-phospho-L-threonine + tRNACys
AMP + diphosphate + O-phospho-L-threonyl-tRNACys
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low activity
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ATP + O-phospho-L-threonine + tRNACys
AMP + diphosphate + O-phospho-L-threonyl-tRNACys
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about 35% of the plateau aminoacylation observed with O-phospho-L-serine
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?
additional information
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two-step Cys-tRNACys formation: in organisms like Archaeoglobus fulgidus lacking a canonical cysteinyl-tRNA synthetase for the direct Cys-tRNACys formation, Cys-tRNACys is produced by the indirect pathway, in which the noncanonical O-phosphoseryl-tRNA synthetase, SepRS, ligates the noncanonical amino acid O-phosphoserine, Sep, to tRNACys, and the Sep-tRNA:Cys-tRNA synthase converts the produced Sep-tRNACys to Cys-tRNACys, overview, the SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism
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additional information
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substrate specificity, site-specific incorporation of phosphoserine into proteins by mutant D418N/D420N/T423V in response to the 7-(2-thienyl)-imidazo[4,5-b]pyridineUA or C7-(2-thienyl)-imidazo[4,5-b]pyridineA codons within mRNA, substrate binding structures and structural models for tRNA anticodon recognition, overview
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additional information
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two-step Cys-tRNACys formation: in organisms like Archaeoglobus fulgidus lacking a canonical cysteinyl-tRNA synthetase for the direct Cys-tRNACys formation, Cys-tRNACys is produced by the indirect pathway, in which the noncanonical O-phosphoseryl-tRNA synthetase, SepRS, ligates the noncanonical amino acid O-phosphoserine, Sep, to tRNACys, and the Sep-tRNA:Cys-tRNA synthase converts the produced Sep-tRNACys to Cys-tRNACys, overview, the SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism. RNA substrate specificity of wild-type and mutant enzymes, overview, structural insights into the first step of RNA-dependent cysteine biosynthesis, a two-step mechanism, in archaea
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additional information
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two-step Cys-tRNACys formation: in organisms like Methanococcus jannaschii lacking a canonical cysteinyl-tRNA synthetase for the direct Cys-tRNACys formation, Cys-tRNACys is produced by the indirect pathway, in which the noncanonical O-phosphoseryl-tRNA synthetase, SepRS, ligates the noncanonical amino acid O-phosphoserine, Sep, to tRNACys, and the Sep-tRNA:Cys-tRNA synthase converts the produced Sep-tRNACys to Cys-tRNACys, overview, the SepRS/SepCysS pathway is the sole route for cysteine biosynthesis in the organism
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additional information
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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
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additional information
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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
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additional information
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SepRS is able to discriminate against the noncognate amino acids glutamate, serine, and phosphothreonine without the need for a separate hydrolytic editing site
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additional information
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SepRS is able to discriminate against the noncognate amino acids glutamate, serine, and phosphothreonine without the need for a separate hydrolytic editing site. Determination of the ATP-diphosphate exchange activity. Serine and glutamate are poor substrates, overview
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