Literature summary for 6.1.1.3 extracted from

Caillet, J.; Nogueira, T.; Masquida, B.; Winter, F.; Graffe, M.; Dock-Bregeon, A.C.; Torres-Larios, A.; Sankaranarayanan, R.; Westhof, E.; Ehresmann, B.; Ehresmann, C.; Romby, P.; Springer, M.
The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression (2003), Mol. Microbiol., 47, 961-974.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutants in the null mutant strain	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D549A	modified interation of anticodon loop/C-ter domain, activity similar to the wild-type	Escherichia coli
E258K	modified interation with the superrepressor, no activity	Escherichia coli
E259K	modified interation with the superrepressor, unaltered activity	Escherichia coli
E600A	modified interation of anticodon loop/C-ter domain, 710fold increased activity	Escherichia coli
K246A	modified interation of acceptor stem and catalytic domain, 2.9fold increased activity	Escherichia coli
K249A	modified interation of acceptor stem and catalytic domain, 3.5fold increased activity	Escherichia coli
K577A	modified interation of anticodon loop/C-ter domain, 118fold increased activity	Escherichia coli
additional information	construction of chromosomal disruption null mutant strain with no activity, construction of a truncated mutant lacking the N1 and N2 domains, 93.5fold increased activity	Escherichia coli
N324A	modified interation of cross-subunit contacts, 3.5fold increased activity	Escherichia coli
N502A	modified interation of cross-subunit contacts, 2.1fold increased activity	Escherichia coli
N575A	modified interation of anticodon loop/C-ter domain, 9.4fold increased activity	Escherichia coli
R349A	modified interation of cross-subunit contacts, 42fold increased activity	Escherichia coli
R583H	modified interation of anticodon loop/C-ter domain, no activity	Escherichia coli
R609A	modified interation of anticodon loop/C-ter domain, 35fold activity	Escherichia coli
S347A	modified interation of cross-subunit contacts, similar to the wild-type	Escherichia coli
S367A	modified interation of acceptor stem and catalytic domain, 11fold increased activity	Escherichia coli
Y205F	modified interation of acceptor stem and N-terminal domain, 7.7fold increased activity	Escherichia coli
Y219F	modified interation of acceptor stem and N-terminal domain, similar to the wild-type	Escherichia coli
Y348F	modified interation of cross-subunit contacts, 6.5fold increased activity	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	mutant enzymes complementing the null mutant	Escherichia coli
0.00003	-	L-threonine	wild-type enzyme complementing the null mutant	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-threonine + tRNAThr	Escherichia coli	-	AMP + diphosphate + L-threonyl-tRNAThr	-	?
additional information	Escherichia coli	regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr	the catalytic domain is located at the C-terminus of the enzyme	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-threonine + tRNAThr	-	Escherichia coli	AMP + diphosphate + L-threonyl-tRNAThr	-	?
ATP + L-threonine + tRNAThr	tRNA aminoacylation	Escherichia coli	AMP + diphosphate + L-threonyl-tRNAThr	-	?
additional information	enzyme also has a regulatory function by binding the so-called operator site located in the leader of its own mRNA and thereby inhibits translational initiation by competing with ribosome binding	Escherichia coli	?	-	?
additional information	regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
Synthetase, threonyl-transfer ribonucleate	-	Escherichia coli
Threonine translase	-	Escherichia coli
Threonine--tRNA ligase	-	Escherichia coli
Threonine-transfer ribonucleate synthetase	-	Escherichia coli
Threonyl-ribonucleic synthetase	-	Escherichia coli
Threonyl-transfer ribonucleate synthetase	-	Escherichia coli
Threonyl-transfer ribonucleic acid synthetase	-	Escherichia coli
Threonyl-transfer RNA synthetase	-	Escherichia coli
Threonyl-tRNA synthetase	-	Escherichia coli
ThrRS	-	Escherichia coli
TRS	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	mutant enzymes complementing the null mutant	Escherichia coli
0.64	-	L-threonine	wild-type enzyme complementing the null mutant	Escherichia coli
6.08	-	L-threonine	wild-type enzyme complementing the null mutant	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)