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Literature summary for 6.1.1.3 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
Search for more literature for 6.1.1.3

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A8M3
-
-

Reaction

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

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli