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Literature summary extracted from

  • Sankaranarayanan, R.; Dock-Bregeon, A.C.; Rees, B.; Bovee, M.; Caillet, J.; Romby, P.; Francklyn, C.S.; Moras, D.
    Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase (2000), Nat. Struct. Biol., 7, 461-465.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.3 X-ray structure determination at 2.9 A resolution, structure analysis of the wild-type enzyme and truncated mutant lamdaN in complex with L-threonine and L-serine Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 additional information truncated lamdaN-enzyme mutant, lacking the N-terminal domains N1 and N2, produces Ser-tRNAThr, reduced activity and altered substrate recognition compared to the wild-type which does nearly not incorporate serine Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 0.11
-
 L-threonine pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 0.18
-
 L-threonine pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli
6.1.1.3 1.95
-
 hydroxynorvaline pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 7
-
 hydroxynorvaline pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli
6.1.1.3 81.5
-
 L-serine pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 142
-
 L-serine pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Zn2+ mediates amino acid discrimination of the enzyme, located in the active site, formation of a pentacoordinate intermediatewith both the amino group and the side chain hydroxyl of L-threonine Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Escherichia coli P0A8M3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.3 ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr active site structure Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + hydroxynorvaline + tRNAThr 10-70% less active than with L-threonine Escherichia coli AMP + diphosphate + hydroxynorvalyl-tRNAThr
-
 ?
6.1.1.3 ATP + L-serine + tRNAThr 1000fold less active than with L-threonine Escherichia coli AMP + diphosphate + L-seryl-tRNAThr
-
 ?
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
6.1.1.3 additional information no activity with L-valine, determination of amino acid activation and discriminating editing mechanism Escherichia coli ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 3 6 L-threonine pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 21
-
 hydroxynorvaline pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli
6.1.1.3 22
-
 hydroxynorvaline pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 26
-
 L-serine pH 7.2, 37°C, wild-type enzyme Escherichia coli
6.1.1.3 30
-
 L-serine pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli
6.1.1.3 37
-
 L-threonine pH 7.2, 37°C, truncated enzyme DELTAN Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 7.2
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP
-
 Escherichia coli