2.6.1.97: archaeosine synthase
This is an abbreviated version!
For detailed information about archaeosine synthase, go to the full flat file.
Word Map on EC 2.6.1.97
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2.6.1.97
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trna
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trna-guanine
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nucleoside
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transglycosylase
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7-cyano-7-deazaguanine
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preq0
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arctgts
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crenarchaeota
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euryarchaeota
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nitrile
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7-deazaguanosine
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queuosine
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formamidine
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d-loop
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euryarchaeal
- 2.6.1.97
- trna
- trna-guanine
- nucleoside
- transglycosylase
- 7-cyano-7-deazaguanine
- preq0
- arctgts
- crenarchaeota
- euryarchaeota
- nitrile
- 7-deazaguanosine
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queuosine
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formamidine
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d-loop
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euryarchaeal
Reaction
Synonyms
ARChaeosine synthase, archaeosine synthase subunit alpha, ArcS, ATP-independent amidinotransferase, lysine transferase, MA_4632, MJ1022, QueF-L, QueF-like, SSO0016, Ta0924, TaArcS, TgtA2, TK2156, TkArcS, tRNA-guanine transglycosylase
ECTree
Advanced search results
General Information
General Information on EC 2.6.1.97 - archaeosine synthase
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evolution
malfunction
metabolism
physiological function
additional information
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specific Archaea such as Sulfolobus tokodaii have retained ArcS in addition to GAT-QueC, overview
evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
evolution
structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
evolution
the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
evolution
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the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
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evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
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evolution
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structure-based alignments comparing arcTGT and TgtA2 reveal that TgtA2 lacks key arcTGT catalytic residues and contains an additional module. Members of the TgtA2 and arcTGT family do not perfectly co-distribute
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evolution
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the hyperthermophilic euryarchaeon Thermococcus kodakarensis lacks an arcTGT orthologue
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a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
malfunction
a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
malfunction
recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
malfunction
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recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
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malfunction
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a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
-
malfunction
-
a Haloferax volcanii DELTAtgtA2 derivative demonstrates that tRNA from the mutant strain lacks G+ and instead accumulates preQ0
-
malfunction
-
recombinant expression of the arcTGT orthologue from Thermoplasma acidophilum in the hyperthermophilic euryarchaeon Thermococcus kodakarensis arcS-deletion strain and functional complementation. Less TkRaSEA is obtained from the extract containing TaArcS compared to TkArcS
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GAT-QueC also catalyzes biosynthesis of G+-tRNA, pathways, overview
metabolism
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TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
metabolism
TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
metabolism
the enzyme is responsible for the final step in the biosynthesis of archaeosine in the D-loop of tRNA
metabolism
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TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
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metabolism
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TgtA2 is involved in archaeosine biosynthesis in vivo. Archaeosine biosynthesis is especially complex, involving the initial production of 7-cyano-7-deazaguanine (preQ0), an advanced precursor that is produced in a tRNA-independent portion of the biosynthesis, followed by its insertion into the tRNA by the enzyme tRNA-guanine transglycosylase, which replaces the target guanine base yielding preQ0-tRNA
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metabolism
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the enzyme is responsible for the final step in the biosynthesis of archaeosine in the D-loop of tRNA
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ArcS catalyzes the final step in the G+ pathway, the conversion of preQ0-tRNA to G+-tRNA, in Euryarchaeota
physiological function
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ArcS catalyzes the final step in the G+ pathway, the conversion of preQ0-tRNA to G+-tRNA, in Euryarchaeota
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
-
physiological function
-
archaeosine (G+), 7-formamidino-7-deazaguanosine, is an archaea-specific modified nucleoside found at the 15th position of tRNAs. In Euryarchaeota, 7-cyano-7-deazaguanine (preQ0)-containing tRNA (q0N-tRNA), synthesized by archaeal tRNA-guanine transglycosylase (ArcTGT), is converted to G+-containing tRNA (G+-tRNA) by the paralogue of ArcTGT, ArcS. Several euryarchaeal ArcSs have lysine transfer activity to q0N-tRNA to form q0kN-tRNA, which has a preQ0 lysine adduct as a base. ArcS forms a robust complex with a radical S-adenosylmethionine (SAM) enzyme named RaSEA. The ArcS-RaSEA complex anaerobically converts q0N-tRNA to G+-tRNA in the presence of SAM and lysine via q0kN-tRNA. It is proposed that ArcS and RaSEA should be considered an archaeosine synthase alpha-subunit (lysine transferase) and beta-subunit (q0kN-tRNA lyase), respectively
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G+ can be tolerated in Escherichia coli at position 34 in normally Q-containing tRNA when recombinant GAT-QueC and QueF are introduced
additional information
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presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
-
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
additional information
the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
additional information
the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
additional information
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
additional information
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the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
-
additional information
-
the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
-
additional information
-
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
-
additional information
-
the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-
additional information
-
the archaeosine synthases from Methanosarcina acetivorans is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex. The MaArcS-MaRaSEA complex formation is inducible by arabinose. Interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-
additional information
-
presence of the 7-deazaguanosine derivative archaeosine, i.e. G+, at position 15 in tRNA is one of the diagnostic molecular characteristics of the archaea
-
additional information
-
the archaeosine synthases from Thermococcus kodakarensis is composed of ArcS (subunit alpha) and a radical SAM enzyme TkRaSEA (q0kN-tRNA lyase, subunit beta) both forming a robust complex, but the interaction between TkRaSEA and Thermoplasma acidophilum ArcS is considerably weaker. Interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-
additional information
-
Thermoplasma acidophilum ArcS also interacts with the q0kN-tRNA lyase TkRaSEA from Thermococcus kodakarensis, interaction analysis, overview
-