Literature summary for 6.1.1.23 extracted from

Blaise, M.; Bailly, M.; Frechin, M.; Behrens, M.A.; Fischer, F.; Oliveira, C.L.; Becker, H.D.; Pedersen, J.S.; Thirup, S.; Kern, D.
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation (2010), EMBO J., 29, 3118-3129.

Search for more literature for 6.1.1.23

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified 520 kDa transamidosome complex formed by two dimeric nondiscriminating-AspRSs, two trimeric GatCABs, and four tRNAsAsn molecules, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement	Thermus thermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	pre-steady-state and steady-state aminoacylation kinetics of the ND-AspRSK-tRNAAsn complex and of the transamidosome, overview	Thermus thermophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-aspartate + tRNAAsn	Thermus thermophilus	-	AMP + diphosphate + L-aspartyl-tRNAAsn	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-aspartate + tRNAAsn	-	Thermus thermophilus	AMP + diphosphate + L-aspartyl-tRNAAsn	-	?
ATP + L-aspartate + tRNAAsn	ND-AspRSKtRNAAsn complex and of the transamidosome and mechanism of transamidation, overview. A scaffold tRNAAsn mediates stability and integrity of the complex	Thermus thermophilus	AMP + diphosphate + L-aspartyl-tRNAAsn	-	?

Subunits

Subunits	Comment	Organism
More	comparison of three-dimensional transamidosome complex structures in crystals and in solution, overview	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
non-discriminating aspartyl-tRNA synthetase	-	Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Thermus thermophilus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
10	85	transamidosome complex: ND-AspRS is thermostable up to 70°C, but its thermostability increases when complexed to tRNAAsn. tRNAAsn is very stable, as its melting temperature is 85°C. the GatCAB is poorly protected against heat inactivation, as its denaturation starts at 40°C, but when complexed in the transamidosome, the GatCAB becomes fully thermostable at 85°C	Thermus thermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Thermus thermophilus

General Information

General Information	Comment	Organism
physiological function	during tRNA-dependent asparagine formation, tRNAAsn promotes assembly of a ribonucleoprotein particle called transamidosome that allows channelling of the aa-tRNA from non-discriminating aspartyl-tRNA synthetase active site to the GatCAB amidotransferase site. A transamidosome particle is formed by two GatCABs, two dimeric nondiscriminating-AspRSs and four tRNAsAsn molecules. In the complex, only two tRNAs are bound in a functional state, whereas the two other ones act as an RNA scaffold enabling release of the asparaginyl-tRNAAsn without dissociation of the complex. The transamidosome constitutes a transfer-ribonucleoprotein particle in which tRNAs serve the function of both substrate and structural foundation for a large molecular machine	Thermus thermophilus

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Release 2023.1 (January 2023)