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Literature summary for 6.1.1.14 extracted from
- Glycyl-tRNA synthetase (1996), Biol. Chem. Hoppe-Seyler, 377, 343-356.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | - |
Escherichia coli |
| additional information | - |
Homo sapiens |
| additional information | truncated enzyme forms with deletions of 12, 27, 46, and 55 N-terminal residues reduce the kcat value of the wild-type enzyme by a factor 5-10 in diphosphate exchange and aminoacylation activity, but does not significantly change the Km of the three substrates. Deletions of 108 N-terminal residues or the internal segments 111-164 and 110-309 cause complete loss of activity. Deletions from the C-terminus of 24, 38, 60, 163, and 328 residues result in inactive enzyme forms. Whereas the wild-type enzyme binds both tRNAGly and noncognate tRNAAla, the mutant lacking 55 N-terminal residues shows altered binding of tRNAGly and does not bind tRNAAla | Bombyx mori |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5,5'-dithiobis(2-nitrobenzoate) | - |
Bombyx mori |  |
| Inorganic sulfide | activity is restored by addition of glutathione, cysteine or cysteamine | Bombyx mori | |
| Nalidixic acid | - |
Saccharomyces cerevisiae | |
| Oxolinic acid | - |
Saccharomyces cerevisiae | |
| p-chloromercuribenzoate | - |
Gallus gallus | |
| p-chloromercuribenzoate | - |
Staphylococcus aureus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | overview | Salmonella enterica subsp. enterica serovar Typhimurium | |
| additional information | - |
additional information | overview | Staphylococcus aureus | |
| additional information | - |
additional information | overview | Escherichia coli | |
| additional information | - |
additional information | overview | Rattus norvegicus | |
| additional information | - |
additional information | overview | Saccharomyces cerevisiae | |
| additional information | - |
additional information | overview | Bombyx mori |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | can replace Mg2+ in activation | Staphylococcus aureus | |
| Co2+ | activates with 5% of the efficiency of ATP | Staphylococcus aureus | |
| Mg2+ | - |
Escherichia coli | |
| Mg2+ | required | Staphylococcus aureus | |
| Mg2+ | required | Saccharomyces cerevisiae | |
| Mg2+ | required | Bombyx mori | |
| Mg2+ | optimal Mg2+/ATP ratio is 5:1 | Staphylococcus aureus | |
| Mg2+ | cannot be effectively replaced by other bivalent cations or spermidine | Bombyx mori | |
| Mg2+ | can be replaced by Co2+ or Mn2+, with lower efficiency | Staphylococcus aureus | |
| Mn2+ | can replace Mg2+ in activation | Staphylococcus aureus | |
| Mn2+ | can replace Mg2+ in activation | Escherichia coli | |
| Mn2+ | stimulates | Gallus gallus | |
| Mn2+ | stimulates | Rattus norvegicus | |
| Mn2+ | activates with 77% of the efficiency of Mg2+ | Staphylococcus aureus | |
| PO43- | phosphorylation and dephosphorylation seem to be a means of regulation | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + glycine + tRNAGly | Salmonella enterica subsp. enterica serovar Typhimurium | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Gallus gallus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Staphylococcus aureus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Brevibacillus brevis | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Aliivibrio fischeri | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Alcaligenes faecalis | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | eukaryota | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Chlamydia trachomatis | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Haemophilus influenzae | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Mycoplasma genitalium | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Mus musculus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Thermus thermophilus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Escherichia coli | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Rattus norvegicus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Saccharomyces cerevisiae | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Bos taurus | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Bombyx mori | insertion of glycine into proteins | ? | - |
? | |
| ATP + glycine + tRNAGly | Geobacillus stearothermophilus | insertion of glycine into proteins | ? | - |
? | |
| additional information | Salmonella enterica subsp. enterica serovar Typhimurium | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Gallus gallus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Staphylococcus aureus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Brevibacillus brevis | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Aliivibrio fischeri | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Alcaligenes faecalis | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | eukaryota | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Chlamydia trachomatis | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Haemophilus influenzae | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Mycoplasma genitalium | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Mus musculus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Thermus thermophilus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Escherichia coli | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Rattus norvegicus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Saccharomyces cerevisiae | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Bos taurus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Bombyx mori | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
| additional information | Geobacillus stearothermophilus | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alcaligenes faecalis | - |
- |
- |
| Aliivibrio fischeri | - |
- |
- |
| Bombyx mori | - |
wild-type and truncated enzyme forms | - |
| Bos taurus | - |
- |
- |
| Brevibacillus brevis | - |
- |
- |
| Chlamydia trachomatis | - |
- |
- |
| Escherichia coli | - |
- |
- |
| eukaryota | - |
- |
- |
| Gallus gallus | - |
- |
- |
| Geobacillus stearothermophilus | - |
- |
- |
| Haemophilus influenzae | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
| Mycoplasma genitalium | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
| Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
| Staphylococcus aureus | - |
- |
- |
| Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly | `half-of-the-sites' mechanism in aminoacylation | Bombyx mori |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| Ehrlich ascites carcinoma cell | - |
Mus musculus | - |
| embryo | - |
Gallus gallus | - |
| liver | - |
Mus musculus | - |
| liver | - |
Rattus norvegicus | - |
| liver | - |
Bos taurus | - |
| skeletal muscle | - |
Rattus norvegicus | - |
| uterus | - |
Mus musculus | - |
| Yoshida AH-130 cell | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| AMP + ADP | - |
Escherichia coli | P1,P3-bis(5'-adenosyl) triphosphate | - |
? | |
| AMP + ATP | - |
Escherichia coli | P1,P4-bis(5'-adenosyl) tetraphosphate | - |
? | |
| AMP + phosphate | - |
Escherichia coli | ADP | - |
? | |
| ATP + glycine + tRNAGly | - |
Salmonella enterica subsp. enterica serovar Typhimurium | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Gallus gallus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Staphylococcus aureus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Brevibacillus brevis | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Aliivibrio fischeri | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Alcaligenes faecalis | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
eukaryota | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Chlamydia trachomatis | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Haemophilus influenzae | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Mycoplasma genitalium | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Mus musculus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Thermus thermophilus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Escherichia coli | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Homo sapiens | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Rattus norvegicus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Saccharomyces cerevisiae | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Bos taurus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | - |
Geobacillus stearothermophilus | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | the wild-type enzyme binds both tRNAGly and noncognate tRNAAla. The mutant lacking 55 N-terminal residues shows altered binding of tRNAGly and does not bind tRNAAla | Bombyx mori | AMP + diphosphate + glycyl-tRNAGly | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Gallus gallus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Staphylococcus aureus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Brevibacillus brevis | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Aliivibrio fischeri | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Alcaligenes faecalis | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | eukaryota | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Chlamydia trachomatis | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Haemophilus influenzae | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Mycoplasma genitalium | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Mus musculus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Thermus thermophilus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Escherichia coli | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Rattus norvegicus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Saccharomyces cerevisiae | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Bos taurus | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Bombyx mori | ? | - |
? | |
| ATP + glycine + tRNAGly | insertion of glycine into proteins | Geobacillus stearothermophilus | ? | - |
? | |
| additional information | - |
Staphylococcus aureus | ? | - |
? | |
| additional information | - |
Thermus thermophilus | ? | - |
? | |
| additional information | - |
Saccharomyces cerevisiae | ? | - |
? | |
| additional information | - |
Bombyx mori | ? | - |
? | |
| additional information | formation of glycine hydroxamate | Gallus gallus | ? | - |
? | |
| additional information | formation of glycine hydroxamate | Brevibacillus brevis | ? | - |
? | |
| additional information | catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate | Escherichia coli | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Gallus gallus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Staphylococcus aureus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Brevibacillus brevis | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Aliivibrio fischeri | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Alcaligenes faecalis | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | eukaryota | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Chlamydia trachomatis | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Haemophilus influenzae | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Mycoplasma genitalium | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Mus musculus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Thermus thermophilus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Escherichia coli | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Rattus norvegicus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Saccharomyces cerevisiae | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Bos taurus | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Bombyx mori | ? | - |
? | |
| additional information | in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function | Geobacillus stearothermophilus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Saccharomyces cerevisiae |
| dimer | alpha2 | Thermus thermophilus |
| dimer | alpha2 | Bombyx mori |
| More | - |
Homo sapiens |
| More | polypeptide is weakly associated with multienzyme complexes consisting of aminoacyl-tRNA synthetases | eukaryota |
| tetramer | - |
Saccharomyces cerevisiae |
| tetramer | alpha2,beta2 | Brevibacillus brevis |
| tetramer | alpha2,beta2 | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8 | - |
Rattus norvegicus |
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