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Literature summary for 6.1.1.18 extracted from

  • Deniziak, M.; Sauter, C.; Becker, H.D.; Paulus, C.A.; Giege, R.; Kern, D.
    Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation (2007), Nucleic Acids Res., 35, 1421-1431.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of full length and C-terminal truncated GlnRS, lacking the the Yqey domain, and of the isolated Yqey protein, in Escherichia coli strain ER2566 Deinococcus radiodurans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant full-length GlnRS grown in microbatch in the presence of PEG 3350, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement Deinococcus radiodurans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information effect of the isolated Yqey domain on the kinetic properties of GlnRS, overview Deinococcus radiodurans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + tRNAGln Deinococcus radiodurans
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
?
ATP + L-glutamine + tRNAGln Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
AMP + diphosphate + L-glutaminyl-tRNAGln
-
?

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans P56926
-
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 P56926
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln structure–function relationship, overview Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
Deinococcus radiodurans AMP + diphosphate + L-glutaminyl-tRNAGln
-
?
ATP + L-glutamine + tRNAGln
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 AMP + diphosphate + L-glutaminyl-tRNAGln
-
?
ATP + L-glutamine + tRNAGln(CUG)
-
Deinococcus radiodurans AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
-
?
ATP + L-glutamine + tRNAGln(CUG)
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 AMP + diphosphate + L-glutaminyl-tRNAGln(CUG)
-
?
ATP + L-glutamine + tRNAGln(UUG)
-
Deinococcus radiodurans AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
-
?
ATP + L-glutamine + tRNAGln(UUG)
-
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 AMP + diphosphate + L-glutaminyl-tRNAGln(UUG)
-
?
additional information the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structure–function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview Deinococcus radiodurans ?
-
?
additional information the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structure–function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 ?
-
?

Subunits

Subunits Comment Organism
More the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview Deinococcus radiodurans

Synonyms

Synonyms Comment Organism
GlnRS
-
Deinococcus radiodurans
Glutaminyl-tRNA synthetase
-
Deinococcus radiodurans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Deinococcus radiodurans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Deinococcus radiodurans

Cofactor

Cofactor Comment Organism Structure
ATP
-
Deinococcus radiodurans