General Stability | Organism |
---|---|
in absence of protease inhibitors and/or dithioerythritol, the enzyme rapidly loses its activity | Saccharomyces cerevisiae |
protectors of SH groups at concentrations of 20 mM are required to obtain an optimal aminoacylation rate | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000088 | - |
tRNAGly | - |
Saccharomyces cerevisiae | |
0.021 | - |
ATP | - |
Saccharomyces cerevisiae | |
0.25 | - |
Gly | - |
Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae | |
Mg2+ | optimal MgCl2/ATP ratio is 1.5 | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
57500 | - |
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE | Saccharomyces cerevisiae |
67600 | - |
2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE | Saccharomyces cerevisiae |
135000 | 142000 | sucrose density gradient centrifugation, dimeric enzyme form | Saccharomyces cerevisiae |
158000 | 160000 | PAGE under nondenaturing conditions, gel filtration, dimeric enzyme form | Saccharomyces cerevisiae |
210000 | - |
sucrose density gradient centrifugation, tetrameric enzyme form | Saccharomyces cerevisiae |
250000 | - |
PAGE under nondenaturing conditions, gel filtration, tetrameric enzyme form | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0074 | - |
tetrameric enzyme form | Saccharomyces cerevisiae |
0.55 | - |
dimeric enzyme form | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + glycine + tRNAGly | - |
Saccharomyces cerevisiae | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
additional information | catalyzes glycine-dependent ATP-diphosphate exchange | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 70000-80000 (alpha), SDS-PAGE, enzyme form isolated in presence of high concentrations of protease inhibitors and dithioerythritol. A tetrameric enzyme form is isolated in presence of minimal concentrations of dithioerythritol | Saccharomyces cerevisiae |
tetramer | 2 * 67600 (alpha) + 2 * 57500 (beta), enzyme form isolated in presence of minimal concentrations of dithioerythritol. A dimeric enzyme form is isolated in presence of high concentrations of protease inhibitors and dithioerythritol, SDS-PAGE | Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | 40 | aminoacylation of tRNAGly | Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
aminoacylation of tRNAGly | Saccharomyces cerevisiae |