BRENDA - Enzyme Database

Glycyl-tRNA synthetase

Freist, W.; Logan, D.T.; Gauss, D.H.; Biol. Chem. Hoppe-Seyler 377, 343-356 (1996)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
6.1.1.14
-
Escherichia coli
Crystallization (Commentary)
EC Number
Crystallization
Organism
6.1.1.14
-
Thermus thermophilus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
6.1.1.14
additional information
-
Escherichia coli
6.1.1.14
additional information
-
Homo sapiens
6.1.1.14
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
EC Number
Inhibitors
Commentary
Organism
Structure
6.1.1.14
5,5'-dithiobis(2-nitrobenzoate)
-
Bombyx mori
6.1.1.14
Inorganic sulfide
activity is restored by addition of glutathione, cysteine or cysteamine
Bombyx mori
6.1.1.14
Nalidixic acid
-
Saccharomyces cerevisiae
6.1.1.14
Oxolinic acid
-
Saccharomyces cerevisiae
6.1.1.14
p-chloromercuribenzoate
-
Gallus gallus
6.1.1.14
p-chloromercuribenzoate
-
Staphylococcus aureus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.1.1.14
additional information
-
additional information
overview
Bombyx mori
6.1.1.14
additional information
-
additional information
overview
Escherichia coli
6.1.1.14
additional information
-
additional information
overview
Rattus norvegicus
6.1.1.14
additional information
-
additional information
overview
Saccharomyces cerevisiae
6.1.1.14
additional information
-
additional information
overview
Salmonella enterica subsp. enterica serovar Typhimurium
6.1.1.14
additional information
-
additional information
overview
Staphylococcus aureus
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.14
Co2+
activates with 5% of the efficiency of ATP; can replace Mg2+ in activation
Staphylococcus aureus
6.1.1.14
Mg2+
cannot be effectively replaced by other bivalent cations or spermidine; required
Bombyx mori
6.1.1.14
Mg2+
-
Escherichia coli
6.1.1.14
Mg2+
required
Saccharomyces cerevisiae
6.1.1.14
Mg2+
can be replaced by Co2+ or Mn2+, with lower efficiency; optimal Mg2+/ATP ratio is 5:1; required
Staphylococcus aureus
6.1.1.14
Mn2+
can replace Mg2+ in activation
Escherichia coli
6.1.1.14
Mn2+
stimulates
Gallus gallus
6.1.1.14
Mn2+
stimulates
Rattus norvegicus
6.1.1.14
Mn2+
activates with 77% of the efficiency of Mg2+; can replace Mg2+ in activation
Staphylococcus aureus
6.1.1.14
PO43-
phosphorylation and dephosphorylation seem to be a means of regulation
Mus musculus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.14
ATP + glycine + tRNAGly
Salmonella enterica subsp. enterica serovar Typhimurium
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Gallus gallus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Staphylococcus aureus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Brevibacillus brevis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Aliivibrio fischeri
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Alcaligenes faecalis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
eukaryota
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Chlamydia trachomatis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Haemophilus influenzae
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Mycoplasma genitalium
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Mus musculus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Thermus thermophilus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Escherichia coli
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Rattus norvegicus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Saccharomyces cerevisiae
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Bos taurus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Bombyx mori
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Geobacillus stearothermophilus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
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
?
-
-
-
6.1.1.14
additional information
Gallus gallus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Staphylococcus aureus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Brevibacillus brevis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Aliivibrio fischeri
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Alcaligenes faecalis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
eukaryota
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Chlamydia trachomatis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Haemophilus influenzae
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Mycoplasma genitalium
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Mus musculus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Thermus thermophilus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Escherichia coli
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Rattus norvegicus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Saccharomyces cerevisiae
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Bos taurus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Bombyx mori
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Geobacillus stearothermophilus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.14
Alcaligenes faecalis
-
-
-
6.1.1.14
Aliivibrio fischeri
-
-
-
6.1.1.14
Bombyx mori
-
wild-type and truncated enzyme forms
-
6.1.1.14
Bos taurus
-
-
-
6.1.1.14
Brevibacillus brevis
-
-
-
6.1.1.14
Chlamydia trachomatis
-
-
-
6.1.1.14
Escherichia coli
-
-
-
6.1.1.14
eukaryota
-
-
-
6.1.1.14
Gallus gallus
-
-
-
6.1.1.14
Geobacillus stearothermophilus
-
-
-
6.1.1.14
Haemophilus influenzae
-
-
-
6.1.1.14
Homo sapiens
-
-
-
6.1.1.14
Mus musculus
-
-
-
6.1.1.14
Mycoplasma genitalium
-
-
-
6.1.1.14
Rattus norvegicus
-
-
-
6.1.1.14
Saccharomyces cerevisiae
-
-
-
6.1.1.14
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
6.1.1.14
Staphylococcus aureus
-
-
-
6.1.1.14
Thermus thermophilus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
6.1.1.14
-
Escherichia coli
Reaction
EC Number
Reaction
Commentary
Organism
6.1.1.14
ATP + glycine + tRNAGly = AMP + diphosphate + glycyl-tRNAGly
`half-of-the-sites' mechanism in aminoacylation
Bombyx mori
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
6.1.1.14
Ehrlich ascites carcinoma cell
-
Mus musculus
-
6.1.1.14
embryo
-
Gallus gallus
-
6.1.1.14
liver
-
Mus musculus
-
6.1.1.14
liver
-
Rattus norvegicus
-
6.1.1.14
liver
-
Bos taurus
-
6.1.1.14
skeletal muscle
-
Rattus norvegicus
-
6.1.1.14
uterus
-
Mus musculus
-
6.1.1.14
Yoshida AH-130 cell
-
Rattus norvegicus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.14
AMP + ADP
-
133
Escherichia coli
P1,P3-bis(5'-adenosyl) triphosphate
-
133
Escherichia coli
-
6.1.1.14
AMP + ATP
-
133
Escherichia coli
P1,P4-bis(5'-adenosyl) tetraphosphate
-
133
Escherichia coli
-
6.1.1.14
AMP + phosphate
-
133
Escherichia coli
ADP
-
133
Escherichia coli
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Salmonella enterica subsp. enterica serovar Typhimurium
AMP + diphosphate + glycyl-tRNAGly
-
133
Salmonella enterica subsp. enterica serovar Typhimurium
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Gallus gallus
AMP + diphosphate + glycyl-tRNAGly
-
133
Gallus gallus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Staphylococcus aureus
AMP + diphosphate + glycyl-tRNAGly
-
133
Staphylococcus aureus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Brevibacillus brevis
AMP + diphosphate + glycyl-tRNAGly
-
133
Brevibacillus brevis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Aliivibrio fischeri
AMP + diphosphate + glycyl-tRNAGly
-
133
Aliivibrio fischeri
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Alcaligenes faecalis
AMP + diphosphate + glycyl-tRNAGly
-
133
Alcaligenes faecalis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
eukaryota
AMP + diphosphate + glycyl-tRNAGly
-
133
eukaryota
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Chlamydia trachomatis
AMP + diphosphate + glycyl-tRNAGly
-
133
Chlamydia trachomatis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Haemophilus influenzae
AMP + diphosphate + glycyl-tRNAGly
-
133
Haemophilus influenzae
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Mycoplasma genitalium
AMP + diphosphate + glycyl-tRNAGly
-
133
Mycoplasma genitalium
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Mus musculus
AMP + diphosphate + glycyl-tRNAGly
-
133
Mus musculus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Thermus thermophilus
AMP + diphosphate + glycyl-tRNAGly
-
133
Thermus thermophilus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Escherichia coli
AMP + diphosphate + glycyl-tRNAGly
-
133
Escherichia coli
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Homo sapiens
AMP + diphosphate + glycyl-tRNAGly
-
133
Homo sapiens
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Rattus norvegicus
AMP + diphosphate + glycyl-tRNAGly
-
133
Rattus norvegicus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Saccharomyces cerevisiae
AMP + diphosphate + glycyl-tRNAGly
-
133
Saccharomyces cerevisiae
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Bos taurus
AMP + diphosphate + glycyl-tRNAGly
-
133
Bos taurus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Geobacillus stearothermophilus
AMP + diphosphate + glycyl-tRNAGly
-
133
Geobacillus stearothermophilus
-
6.1.1.14
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
133
Bombyx mori
AMP + diphosphate + glycyl-tRNAGly
-
133
Bombyx mori
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Gallus gallus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Aliivibrio fischeri
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Alcaligenes faecalis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
eukaryota
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Chlamydia trachomatis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Haemophilus influenzae
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Mycoplasma genitalium
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Mus musculus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Escherichia coli
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Rattus norvegicus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Bos taurus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Bombyx mori
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Geobacillus stearothermophilus
?
-
-
-
-
6.1.1.14
additional information
-
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
additional information
-
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
additional information
-
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
additional information
-
133
Bombyx mori
?
-
-
-
-
6.1.1.14
additional information
formation of glycine hydroxamate
133
Gallus gallus
?
-
-
-
-
6.1.1.14
additional information
formation of glycine hydroxamate
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
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
133
Escherichia coli
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Gallus gallus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Aliivibrio fischeri
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Alcaligenes faecalis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
eukaryota
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Chlamydia trachomatis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Haemophilus influenzae
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Mycoplasma genitalium
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Mus musculus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Escherichia coli
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Rattus norvegicus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Bos taurus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Bombyx mori
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Geobacillus stearothermophilus
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
6.1.1.14
dimer
alpha2
Bombyx mori
6.1.1.14
dimer
-
Saccharomyces cerevisiae
6.1.1.14
dimer
alpha2
Thermus thermophilus
6.1.1.14
More
polypeptide is weakly associated with multienzyme complexes consisting of aminoacyl-tRNA synthetases
eukaryota
6.1.1.14
More
-
Homo sapiens
6.1.1.14
tetramer
alpha2,beta2
Brevibacillus brevis
6.1.1.14
tetramer
alpha2,beta2
Escherichia coli
6.1.1.14
tetramer
-
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.14
7
8
-
Rattus norvegicus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.1.1.14
-
Escherichia coli
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
6.1.1.14
-
Thermus thermophilus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
6.1.1.14
additional information
-
Escherichia coli
6.1.1.14
additional information
-
Homo sapiens
6.1.1.14
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 (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
6.1.1.14
5,5'-dithiobis(2-nitrobenzoate)
-
Bombyx mori
6.1.1.14
Inorganic sulfide
activity is restored by addition of glutathione, cysteine or cysteamine
Bombyx mori
6.1.1.14
Nalidixic acid
-
Saccharomyces cerevisiae
6.1.1.14
Oxolinic acid
-
Saccharomyces cerevisiae
6.1.1.14
p-chloromercuribenzoate
-
Gallus gallus
6.1.1.14
p-chloromercuribenzoate
-
Staphylococcus aureus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.1.1.14
additional information
-
additional information
overview
Bombyx mori
6.1.1.14
additional information
-
additional information
overview
Escherichia coli
6.1.1.14
additional information
-
additional information
overview
Rattus norvegicus
6.1.1.14
additional information
-
additional information
overview
Saccharomyces cerevisiae
6.1.1.14
additional information
-
additional information
overview
Salmonella enterica subsp. enterica serovar Typhimurium
6.1.1.14
additional information
-
additional information
overview
Staphylococcus aureus
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
6.1.1.14
Co2+
activates with 5% of the efficiency of ATP; can replace Mg2+ in activation
Staphylococcus aureus
6.1.1.14
Mg2+
cannot be effectively replaced by other bivalent cations or spermidine; required
Bombyx mori
6.1.1.14
Mg2+
-
Escherichia coli
6.1.1.14
Mg2+
required
Saccharomyces cerevisiae
6.1.1.14
Mg2+
can be replaced by Co2+ or Mn2+, with lower efficiency; optimal Mg2+/ATP ratio is 5:1; required
Staphylococcus aureus
6.1.1.14
Mn2+
can replace Mg2+ in activation
Escherichia coli
6.1.1.14
Mn2+
stimulates
Gallus gallus
6.1.1.14
Mn2+
stimulates
Rattus norvegicus
6.1.1.14
Mn2+
activates with 77% of the efficiency of Mg2+; can replace Mg2+ in activation
Staphylococcus aureus
6.1.1.14
PO43-
phosphorylation and dephosphorylation seem to be a means of regulation
Mus musculus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.14
ATP + glycine + tRNAGly
Salmonella enterica subsp. enterica serovar Typhimurium
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Gallus gallus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Staphylococcus aureus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Brevibacillus brevis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Aliivibrio fischeri
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Alcaligenes faecalis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
eukaryota
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Chlamydia trachomatis
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Haemophilus influenzae
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Mycoplasma genitalium
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Mus musculus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Thermus thermophilus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Escherichia coli
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Rattus norvegicus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Saccharomyces cerevisiae
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Bos taurus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Bombyx mori
insertion of glycine into proteins
?
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
Geobacillus stearothermophilus
insertion of glycine into proteins
?
-
-
-
6.1.1.14
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
?
-
-
-
6.1.1.14
additional information
Gallus gallus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Staphylococcus aureus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Brevibacillus brevis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Aliivibrio fischeri
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Alcaligenes faecalis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
eukaryota
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Chlamydia trachomatis
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Haemophilus influenzae
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Mycoplasma genitalium
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Mus musculus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Thermus thermophilus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Escherichia coli
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Rattus norvegicus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Saccharomyces cerevisiae
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Bos taurus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Bombyx mori
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
6.1.1.14
additional information
Geobacillus stearothermophilus
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
6.1.1.14
-
Escherichia coli
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
6.1.1.14
Ehrlich ascites carcinoma cell
-
Mus musculus
-
6.1.1.14
embryo
-
Gallus gallus
-
6.1.1.14
liver
-
Mus musculus
-
6.1.1.14
liver
-
Rattus norvegicus
-
6.1.1.14
liver
-
Bos taurus
-
6.1.1.14
skeletal muscle
-
Rattus norvegicus
-
6.1.1.14
uterus
-
Mus musculus
-
6.1.1.14
Yoshida AH-130 cell
-
Rattus norvegicus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.14
AMP + ADP
-
133
Escherichia coli
P1,P3-bis(5'-adenosyl) triphosphate
-
133
Escherichia coli
-
6.1.1.14
AMP + ATP
-
133
Escherichia coli
P1,P4-bis(5'-adenosyl) tetraphosphate
-
133
Escherichia coli
-
6.1.1.14
AMP + phosphate
-
133
Escherichia coli
ADP
-
133
Escherichia coli
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Salmonella enterica subsp. enterica serovar Typhimurium
AMP + diphosphate + glycyl-tRNAGly
-
133
Salmonella enterica subsp. enterica serovar Typhimurium
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Gallus gallus
AMP + diphosphate + glycyl-tRNAGly
-
133
Gallus gallus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Staphylococcus aureus
AMP + diphosphate + glycyl-tRNAGly
-
133
Staphylococcus aureus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Brevibacillus brevis
AMP + diphosphate + glycyl-tRNAGly
-
133
Brevibacillus brevis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Aliivibrio fischeri
AMP + diphosphate + glycyl-tRNAGly
-
133
Aliivibrio fischeri
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Alcaligenes faecalis
AMP + diphosphate + glycyl-tRNAGly
-
133
Alcaligenes faecalis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
eukaryota
AMP + diphosphate + glycyl-tRNAGly
-
133
eukaryota
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Chlamydia trachomatis
AMP + diphosphate + glycyl-tRNAGly
-
133
Chlamydia trachomatis
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Haemophilus influenzae
AMP + diphosphate + glycyl-tRNAGly
-
133
Haemophilus influenzae
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Mycoplasma genitalium
AMP + diphosphate + glycyl-tRNAGly
-
133
Mycoplasma genitalium
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Mus musculus
AMP + diphosphate + glycyl-tRNAGly
-
133
Mus musculus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Thermus thermophilus
AMP + diphosphate + glycyl-tRNAGly
-
133
Thermus thermophilus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Escherichia coli
AMP + diphosphate + glycyl-tRNAGly
-
133
Escherichia coli
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Homo sapiens
AMP + diphosphate + glycyl-tRNAGly
-
133
Homo sapiens
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Rattus norvegicus
AMP + diphosphate + glycyl-tRNAGly
-
133
Rattus norvegicus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Saccharomyces cerevisiae
AMP + diphosphate + glycyl-tRNAGly
-
133
Saccharomyces cerevisiae
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Bos taurus
AMP + diphosphate + glycyl-tRNAGly
-
133
Bos taurus
-
6.1.1.14
ATP + glycine + tRNAGly
-
133
Geobacillus stearothermophilus
AMP + diphosphate + glycyl-tRNAGly
-
133
Geobacillus stearothermophilus
-
6.1.1.14
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
133
Bombyx mori
AMP + diphosphate + glycyl-tRNAGly
-
133
Bombyx mori
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Gallus gallus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Aliivibrio fischeri
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Alcaligenes faecalis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
eukaryota
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Chlamydia trachomatis
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Haemophilus influenzae
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Mycoplasma genitalium
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Mus musculus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Escherichia coli
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Rattus norvegicus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Bos taurus
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Bombyx mori
?
-
-
-
-
6.1.1.14
ATP + glycine + tRNAGly
insertion of glycine into proteins
133
Geobacillus stearothermophilus
?
-
-
-
-
6.1.1.14
additional information
-
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
additional information
-
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
additional information
-
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
additional information
-
133
Bombyx mori
?
-
-
-
-
6.1.1.14
additional information
formation of glycine hydroxamate
133
Gallus gallus
?
-
-
-
-
6.1.1.14
additional information
formation of glycine hydroxamate
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
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
133
Escherichia coli
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Salmonella enterica subsp. enterica serovar Typhimurium
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Gallus gallus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Staphylococcus aureus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Brevibacillus brevis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Aliivibrio fischeri
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Alcaligenes faecalis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
eukaryota
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Chlamydia trachomatis
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Haemophilus influenzae
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Mycoplasma genitalium
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Mus musculus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Thermus thermophilus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Escherichia coli
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Rattus norvegicus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Saccharomyces cerevisiae
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Bos taurus
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Bombyx mori
?
-
-
-
-
6.1.1.14
additional information
in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
133
Geobacillus stearothermophilus
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
6.1.1.14
dimer
alpha2
Bombyx mori
6.1.1.14
dimer
-
Saccharomyces cerevisiae
6.1.1.14
dimer
alpha2
Thermus thermophilus
6.1.1.14
More
polypeptide is weakly associated with multienzyme complexes consisting of aminoacyl-tRNA synthetases
eukaryota
6.1.1.14
More
-
Homo sapiens
6.1.1.14
tetramer
alpha2,beta2
Brevibacillus brevis
6.1.1.14
tetramer
alpha2,beta2
Escherichia coli
6.1.1.14
tetramer
-
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.14
7
8
-
Rattus norvegicus