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 | 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 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 | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine + tRNAThr | Escherichia coli | - |
AMP + diphosphate + L-threonyl-tRNAThr | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A8M3 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr | active site structure | Escherichia coli |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |