Information on EC 6.1.1.14 - glycine-tRNA ligase

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

137, 143, 144, 156, 158, 650213, 652187

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 140

Substrates: 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
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

92, 133

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 147

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 139

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 135, 137, 145, 148, 149, 151, 152, 154, 155, 157, 159

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: binds two molecules of glycyl-AMP per tetramer
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Escherichia coli overproducing

Substrates: activity with tRNAs with modified nucleotides
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 136, 137, 676881, 706875, 728398, 746265

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

651399, 671098

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

675540, 744600, 745302

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

745358, 745876

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: the fusion protein catalyzes the aminoacylation of bovine tRNA
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: two-step reaction
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: enzyme mutations with reduced enzyme activity cause distal spinal muscular atrophy type V or Charcot-Marie-Tooth type 2D, i.e. dSMAV/CMT2D
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS allelic variants are causally associated with the Charcot-Marie-Tooth disease, the most common genetic disorder of the peripheral nervous system
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: tRNA binding site structure, and wild-type and S581L mutant active site structures, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 706875

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: enzyme mutation Nmf249 causes Charcot-Marie-Tooth peripheral neuropathy type 2D, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: usage of calf liver tRNA
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: chloroplastic and mitochondrial tRNA substrate specificity of chloroplastic isozyme GlyRS2, isozyme GlyRS1 is much less efficient
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 137, 150, 151, 651424, 652038, 652455, 746265

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: activity with tRNAs with modified nucleotides
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: wild-type and mutant tRNAGly substrates
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: replacement of ATP by CTP, UTP, ITP, GTP, or TTP results in a decrease in the reaction rate to less than 7% of that with ATP
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: can also charge the tRNAs of certain other bacteria and yeast
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: replacement of ATP by CTP, UTP, ITP, GTP, or TTP results in a decrease in the reaction rate to less than 7% of that with ATP
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: can also charge the tRNAs of certain other bacteria and yeast
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

133, 141, 651043, 746265

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: activity with tRNAs with modified nucleotides
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: substrate specificity with tRNAGly of diverse origins
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: -
Products: -

additional information

Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: catalyzes alanine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: enzyme has two active sites for aminoacylation. tRNA2Gly binds with the enzyme in a molar ratio of 1:1. tRNA2Gly forms a 2:1 complex with the enzyme and is aminoacylated 2fold faster
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: formation of glycine hydroxamate
Products: -

additional information

Substrates: formation of glycine hydroxamate
Products: -

additional information

Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

157

Substrates: beta-subunit plays a major role in tRNA recognition
Products: -

additional information

Substrates: the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
Products: -

additional information

Substrates: the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
Products: -

additional information

Substrates: catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
Products: -

additional information

155

Substrates: catalyzes the synthesis of P1,P4-di(adenosine)tetraphosphate (Ap4A), P1,P3-di(adenosine)triphosphate (Ap3A) and ADP from the enzyme bound glycyl adenylate
Products: -

additional information

155

Substrates: catalyzes a glycine-independent transfer of the gamma-phosphate group from ATP to nucleoside 5'-diphosphate
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: formation of glycine hydroxamate
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: structure-function analysis
Products: -

additional information

Substrates: structure-function analysis
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: -
Products: -

additional information

Substrates: the third base pair, G3*C70 is important for glycylation in yeast
Products: -

additional information

Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
Products: -

additional information

Substrates: enzyme binds the 3'-ends of mRNA from yeast competing with the cognate tRNAGly substrate
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: enzyme plays an important role in transcription termination by affecting 3'-end formation
Products: -

additional information

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: -
Products: -

additional information

Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: participates in peptidoglycan synthesis
Products: -

additional information

Substrates: catalyzes glycine-dependent ATP-diphosphate exchange
Products: -

additional information

Substrates: participates in peptidoglycan synthesis
Products: -

additional information

Substrates: -
Products: -

additional information

Substrates: the discriminator base at position 73, the second-base pair, C2*G71, in the acceptor stem, and the anticodon nucleotides, C35 and C36 contribute to the specific aminoacylation
Products: -

additional information

Substrates: the first base pair, G1*C72 is important for glycylation in E. coli and Thermus thermophilus
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + glycine + tRNAGly

20 entries

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

24 entries

additional information

22 entries

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

Substrates: protein synthesis
Products: -

ATP + glycine + tRNAGly

Substrates: protein synthesis
Products: -

ATP + glycine + tRNAGly

Substrates: insertion of glycine into proteins
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

650213, 652187

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

706875, 728398, 746265

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

651399, 744600, 745302

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

745358, 745876

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: enzyme mutations with reduced enzyme activity cause distal spinal muscular atrophy type V or Charcot-Marie-Tooth type 2D, i.e. dSMAV/CMT2D
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS allelic variants are causally associated with the Charcot-Marie-Tooth disease, the most common genetic disorder of the peripheral nervous system
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, the most common heritable disease of the peripheral nervous system, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: enzyme mutation Nmf249 causes Charcot-Marie-Tooth peripheral neuropathy type 2D, overview
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

651424, 652038, 652455, 746265

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

Substrates: -
Products: -

ATP + glycine + tRNAGly

AMP + diphosphate + glycyl-tRNAGly

651043, 746265

Substrates: -
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: enzyme plays an important role in transcription termination by affecting 3'-end formation
Products: -

additional information

Salmonella enterica subsp. enterica serovar Typhimurium

Substrates: phylogenetic analysis
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

additional information

Substrates: participates in peptidoglycan synthesis
Products: -

additional information

Substrates: participates in peptidoglycan synthesis
Products: -

additional information

Substrates: in a side reaction the enzyme also synthesizes dinucleoside polyphosphates, which probably participate in regulation of cell function
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

ATP

ATP

ATP

ATP

ATP

673686, 676881, 706875, 728398, 746265

ATP

651424, 652038, 652455, 746265

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

ATP

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Co2+

Li+

slightly stimulates in presence of Mg2+

Mg2+

15 entries

Mn2+

6 entries

PO43-

phosphorylation and dephosphorylation seem to be a means of regulation

additional information

the enzyme is twice as active in Tris-HCl or Hepes-NaOH as it is in potassium phosphate buffer

Co2+

can replace Mg2+ in activation

Co2+

activates with 5% of the efficiency of ATP

Mg2+

required

133, 156

Mg2+

cannot be effectively replaced by other bivalent cations or spermidine

Mg2+

optimal concentration is 3-5 mM

Mg2+

Mg2+

Mg2+

Mg2+

Mg2+

Mg2+

Mg2+

required

133, 150

Mg2+

optimal MgCl2/ATP ratio is 1.5

Mg2+

required

Mg2+

optimal Mg2+/ATP ratio is 5:1

Mg2+

can be replaced by Co2+ or Mn2+, with lower efficiency

Mg2+

required

Mn2+

can replace Mg2+ in activation

Mn2+

stimulates

Mn2+

stimulates

Mn2+

can replace Mg2+ in activation

Mn2+

inhibition in presence of Mg2+

Mn2+

activates with 77% of the efficiency of Mg2+

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

5'-adenylylimidodiphosphate

i.e. AMPPNP, a nonsubstrate ATP analogue, competitive inhibition

5,5'-dithiobis(2-nitrobenzoate)

adenylylmethylenediphosphate

i.e. AMPPCP, a nonsubstrate ATP analogue, competitive inhibition

alpha,beta-methyleneadenosine 5'-diphosphate

i.e. AMPCPP, a nonsubstrate ATP analogue, competitive inhibition

Aminoethyl-AMP

AMP

citrate

glycyl sulfamoyl adenosine

Inorganic sulfide

activity is restored by addition of glutathione, cysteine or cysteamine

KCl

inhibits acylation of yeast tRNA, little effect on acylation of homologous tRNAGly

Nalidixic acid

133, 151

novobiocin

151

Oxolinic acid

133, 151

p-chloromercuribenzoate

p-chloromercuriphenylsulfonic acid

activity is not restored by treatment with 2-mercaptoethanol

phosphate

spermine

additional information

reversible denaturation by urea or guanidine-HCl, wild-type enzyme and N-terminally truncated mutant both dissociate to monomers and exhibit a cooperative transition at higher denaturant concentration, wild-type unfolds by a multistate process and 2 parallel state unfoldings, which are absent in the truncated mutant

AMP

competitive inhibition

AMP

p-chloromercuribenzoate

p-chloromercuribenzoate

phosphate

phosphate

Go to Disease Search

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DISEASE

TITLE OF PUBLICATION

LINK TO PUBMED

Brain Neoplasms

Intracellular glycine receptor function facilitates glioma formation in vivo.

24994934

Breast Neoplasms

A proteomic approach based on multiple parallel separation for the unambiguous identification of an antibody cognate antigen.

20872419

Carcinogenesis

Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis.

22345558

Charcot-Marie-Tooth Disease

A novel adenoviral vector-mediated mouse model of Charcot-Marie-Tooth type 2D (CMT2D).

23990368

Charcot-Marie-Tooth Disease

A novel mutation in glycyl-tRNA synthetase caused Charcot-Marie-Tooth disease type 2D with facial and respiratory muscle involvement.

25420567

Charcot-Marie-Tooth Disease

A Novel Mutation of GARS in a Chinese Family With Distal Hereditary Motor Neuropathy Type V.

30083128

Charcot-Marie-Tooth Disease

A novel mutation of the glycyl-tRNA synthetase (GARS) gene associated with Charcot-Marie-Tooth type 2D in a Chinese family.

26000875

Charcot-Marie-Tooth Disease

Allele-specific RNA interference prevents neuropathy in Charcot-Marie-Tooth disease type 2D mouse models.

31557132

Charcot-Marie-Tooth Disease

Charcot-Marie-Tooth disease type 2D with a novel glycyl-tRNA synthetase gene (GARS) mutation.

20169446

Charcot-Marie-Tooth Disease

Charcot-Marie-Tooth-linked mutant GARS is toxic to peripheral neurons independent of wild-type GARS levels.

22144914

Charcot-Marie-Tooth Disease

Clinical and Genetic Features in a Series of Eight Unrelated Patients with Neuropathy Due to Glycyl-tRNA Synthetase (GARS) Variants.

31985473

Charcot-Marie-Tooth Disease

Cocrystal structures of glycyl-tRNA synthetase in complex with tRNA suggest multiple conformational states in glycylation.

24898252

Charcot-Marie-Tooth Disease

Further evidence for genetic heterogeneity of distal HMN type V, CMT2 with predominant hand involvement and Silver syndrome.

17663003

Charcot-Marie-Tooth Disease

GARS axonopathy: not every neuron's cup of tRNA.

20152552

Charcot-Marie-Tooth Disease

Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.

12690580

Charcot-Marie-Tooth Disease

Neuromuscular junction maturation defects precede impaired lower motor neuron connectivity in Charcot-Marie-Tooth type 2D mice.

24368416

Charcot-Marie-Tooth Disease

Neuropilin 1 sequestration by neuropathogenic mutant glycyl-tRNA synthetase is permissive to vascular homeostasis.

28835631

Charcot-Marie-Tooth Disease

Novel GARS mutation presenting as autosomal dominant intermediate Charcot-Marie-Tooth disease.

30394614

Charcot-Marie-Tooth Disease

Two novel mutations of GARS in Korean families with distal hereditary motor neuropathy type V.

23279345

Dehydration

Hyperekplexia mutation of glycine receptors: decreased gating efficacy with altered binding thermodynamics.

12123749

Dermatomyositis

Autoantibodies to glycyl-transfer RNA synthetase in myositis. Association with dermatomyositis and immunologic heterogeneity.

8546723

Dermatomyositis

Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis.

7961834

Encephalomyelitis

Systemic delivery of human GlyR IgG antibody induces GlyR internalization into motor neurons of brainstem and spinal cord with motor dysfunction in mice.

32910464

Epilepsy

Allosteric Modulation of Glycine Receptors.

21557733

Epilepsy

Subunit-Specific Photocontrol of Glycine Receptors by Azobenzene-Nitrazepam Photoswitcher.

33298457

Epilepsy, Temporal Lobe

Allosteric Modulation of Glycine Receptors.

21557733

Hyperekplexia

A Missense Mutation A384P Associated with Human Hyperekplexia Reveals a Desensitization Site of Glycine Receptors.

29440552

Hyperekplexia

A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition.

32354853

Hyperekplexia

Anxiety and Startle Phenotypes in Glrb Spastic and Glra1 Spasmodic Mouse Mutants.

32848605

Hyperekplexia

Glycine receptor mutants of the mouse: what are possible routes of inhibitory compensation?

23118727

Hyperekplexia

Human Hyperekplexic Mutations in Glycine Receptors Disinhibit the Brainstem by Hijacking GABAA Receptors.

31450193

Hyperekplexia

Hyperekplexia mutation of glycine receptors: decreased gating efficacy with altered binding thermodynamics.

12123749

Hyperekplexia

Hyperekplexia mutation R271L of alpha1 glycine receptors potentiates allosteric interactions of nortropeines, propofol and glycine with [3H]strychnine binding.

17655979

Hyperekplexia

Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.

7542038

Hyperekplexia

Hyperekplexia phenotype of glycine receptor alpha1 subunit mutant mice identifies Zn(2+) as an essential endogenous modulator of glycinergic neurotransmission.

17114051

Hyperekplexia

Individual knock out of glycine receptor alpha subunits identifies a specific requirement of glra1 for motor function in zebrafish.

31048868

Hyperekplexia

Presynaptic glycine receptors as a potential therapeutic target for hyperekplexia disease.

24390226

Hyperekplexia

Subunit-Specific Photocontrol of Glycine Receptors by Azobenzene-Nitrazepam Photoswitcher.

33298457

Hyperekplexia

The role of charged residues in independent glycine receptor folding domains for intermolecular interactions and ion channel function.

28429370

Hyperekplexia

The role of tonic glycinergic conductance in cerebellar granule cell signalling and the effect of gain-of-function mutation.

30875431

Hyperglycinemia, Nonketotic

Glycine receptor mutants of the mouse: what are possible routes of inhibitory compensation?

23118727

Hyperglycinemia, Nonketotic

Inactivation of the glycine transporter 1 gene discloses vital role of glial glycine uptake in glycinergic inhibition.

14622582

Hypersensitivity

Modulation of glycine receptor single-channel conductance by intracellular phosphorylation.

32179786

Lipodystrophy

Familial asymmetric distal upper limb amyotrophy (Hirayama disease): report of a Greek family.

19430273

Lipodystrophy

Further evidence for genetic heterogeneity of distal HMN type V, CMT2 with predominant hand involvement and Silver syndrome.

17663003

Lipodystrophy

Relative contribution of mutations in genes for autosomal dominant distal hereditary motor neuropathies: a genotype-phenotype correlation study.

18325928

Lipodystrophy, Congenital Generalized

Familial asymmetric distal upper limb amyotrophy (Hirayama disease): report of a Greek family.

19430273

Lipodystrophy, Congenital Generalized

Further evidence for genetic heterogeneity of distal HMN type V, CMT2 with predominant hand involvement and Silver syndrome.

17663003

Lipodystrophy, Congenital Generalized

Relative contribution of mutations in genes for autosomal dominant distal hereditary motor neuropathies: a genotype-phenotype correlation study.

18325928

Lung Diseases, Interstitial

Antibodies to glycyl-transfer RNA synthetase in patients with myositis and interstitial lung disease.

1622421

Lung Diseases, Interstitial

Correlation of Antisynthetase Antibody Levels with Disease Course in a Patient with Interstitial Lung Disease and Elevated Muscle Enzymes.

19078036

Lupus Erythematosus, Systemic

Correlation of Antisynthetase Antibody Levels with Disease Course in a Patient with Interstitial Lung Disease and Elevated Muscle Enzymes.

19078036

Mitochondrial Diseases

Compound heterozygous mutations in glycyl-tRNA synthetase are a proposed cause of systemic mitochondrial disease.

24669931

Movement Disorders

Subunit-specific potentiation of recombinant glycine receptors by NV-31, a bilobalide-derived compound.

18329806

Muscle Spasticity

Altered potassium channel function in the superficial dorsal horn of the spastic mouse.

17690143

Muscle Spasticity

Anxiety and Startle Phenotypes in Glrb Spastic and Glra1 Spasmodic Mouse Mutants.

32848605

Muscle Spasticity

Despite GABAergic neurotransmission, GABAergic innervation does not compensate for the defect in glycine receptor postsynaptic aggregation in spastic mice.

18445051

Muscle Spasticity

Distinct physiological mechanisms underlie altered glycinergic synaptic transmission in the murine mutants spastic, spasmodic, and oscillator.

16672662

Muscular Atrophy

Effect of Electroacupuncture on the Expression of Glycyl-tRNA Synthetase and Ultrastructure Changes in Atrophied Rat Peroneus Longus Muscle Induced by Sciatic Nerve Injection Injury.

27274754

Muscular Atrophy, Spinal

An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy.

19470612

Muscular Atrophy, Spinal

Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy.

17544401

Muscular Atrophy, Spinal

Familial asymmetric distal upper limb amyotrophy (Hirayama disease): report of a Greek family.

19430273

Muscular Atrophy, Spinal

Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.

12690580

Muscular Atrophy, Spinal

GRS defective axonal distribution as a potential contributor to distal spinal muscular atrophy type V pathogenesis in a new model of GRS-associated neuropathy.

25218976

Muscular Atrophy, Spinal

Mutant glycyl-tRNA synthetase (Gars) ameliorates SOD1(G93A) motor neuron degeneration phenotype but has little affect on Loa dynein heavy chain mutant mice.

19593442

Myoclonus

Systemic delivery of human GlyR IgG antibody induces GlyR internalization into motor neurons of brainstem and spinal cord with motor dysfunction in mice.

32910464

Myositis

Antibodies to glycyl-transfer RNA synthetase in patients with myositis and interstitial lung disease.

1622421

Myositis

Autoantibodies to glycyl-transfer RNA synthetase in myositis. Association with dermatomyositis and immunologic heterogeneity.

8546723

Myositis

Clinical Features and Cytokine Profile in Myositis Patients with Anti-EJ Autoantibodies Detected by a Novel Immunoprecipitation Assay.

31019965

Myositis

Primary structure and functional expression of human Glycyl-tRNA synthetase, an autoantigen in myositis.

7961834

Neoplasms

Extracellular vesicles derived from macrophages display glycyl-tRNA synthetase 1 and exhibit anti-cancer activity.

33708357

Neoplasms

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

27348078

Neoplasms

Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis.

22345558

Nervous System Diseases

Glycine Receptor Drug Discovery.

28528670

Nervous System Diseases

Hyperekplexia mutation R271L of alpha1 glycine receptors potentiates allosteric interactions of nortropeines, propofol and glycine with [3H]strychnine binding.

17655979

Neuralgia

Neuropathic pain model of peripheral neuropathies mediated by mutations of glycyl-tRNA synthetase.

25120326

Peripheral Nervous System Diseases

An Active Dominant Mutation of Glycyl-tRNA Synthetase Causes Neuropathy in a Charcot-Marie-Tooth 2D Mouse Model.

16982418

Peripheral Nervous System Diseases

An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy.

19470612

Peripheral Nervous System Diseases

Charcot-Marie-Tooth-linked mutant GARS is toxic to peripheral neurons independent of wild-type GARS levels.

22144914

Peripheral Nervous System Diseases

Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening.

21737751

Peripheral Nervous System Diseases

HDAC6 is a therapeutic target in mutant GARS-induced Charcot-Marie-Tooth disease.

29415205

Peripheral Nervous System Diseases

Neuropathic pain model of peripheral neuropathies mediated by mutations of glycyl-tRNA synthetase.

25120326

Seizures

Zinc enhances the inhibitory effects of strychnine-sensitive glycine receptors in mouse hippocampal neurons.

17913992

Spinal Muscular Atrophies of Childhood

Mutational analysis of glycyl-tRNA synthetase (GARS) gene in Hirayama disease.

19412816

Stiff-Person Syndrome

The GLRA1 missense mutation W170S associates lack of Zn2+ potentiation with human hyperekplexia.

24198360

Tinnitus

Activation of 5-HT2A/C receptor reduces glycine receptor-mediated currents in cultured auditory cortical neurons.

26371055

Entries 1 - 20 of 86

Show complete table

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.013 - 0.37

ATP

10 entries

0.00035 - 0.67

Gly

8 entries

0.13 - 0.145

glycine

5 entries

0.0026

tRNA1Gly

aminoacylation

0.000088 - 0.0033

tRNAGly

15 entries

0.0091

tRNAGly(C2*71-G2*C71)

acceptor stem mutant substrate

0.0018

tRNAGly(C2*G71-C2*A71)

acceptor stem mutant substrate

0.0045

tRNAGly(G1*C72-A1*U72)

acceptor stem mutant substrate

0.00096

tRNAGly(G1*C72-G1*U72)

acceptor stem mutant substrate

0.0031

tRNAGly(U73-A73)

mutant substrate

0.0046

tRNAGly(U73-C73)

mutant substrate

0.0059

tRNAGly(U73-G73)

mutant substrate

additional information

13 entries

0.013

ATP

0.013

ATP

wild-type enzyme

0.014

ATP

N55-truncation mutant enzyme

0.014

ATP

ATP, , ATP-diphosphate exchange, without tRNA

0.021

ATP

0.04

ATP

ATP-diphosphate exchange in presence of tRNA

0.042

ATP

glycyl-tRNA formation

0.19

ATP

ATP-diphosphate exchange

0.22

ATP

glycyl-tRNA synthesis

0.37

ATP

0.00035

Gly

wild-type enzyme

0.00055

Gly

N55-truncation mutant

0.03

Gly

ATP-diphosphate exchange, without tRNA

0.14

Gly

ATP-diphosphate exchange in presence of tRNA

0.16

Gly

glycyl-tRNA formation

0.18

Gly

0.25

Gly

0.67

Gly

glycyl-tRNA synthesis

0.13

glycine

wild type isoform GlyRS1(KMM1), in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.135

glycine

wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.14

glycine

wild type isoform GlyRS1 without K motif, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.145

glycine

wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.145

glycine

wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.000088

tRNAGly

0.0002

tRNAGly

glycyl-tRNA formation

0.00023

tRNAGly

native substrate from E. coli

0.00028

tRNAGly

native substrate from yeast

0.00028

tRNAGly

wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.00068

tRNAGly

native substrate from E. coli

0.00073

tRNAGly

wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.001

tRNAGly

tRNA2Gly, , aminoacylation

0.001

tRNAGly

Gly, , ATP-diphosphate exchange

0.001

tRNAGly

N55-truncation mutant enzyme

0.0012

tRNAGly

wild-type enzyme

0.00137

tRNAGly

wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.0021

tRNAGly

native substrate from yeast

0.0025

tRNAGly

substrate from liver

0.0033

tRNAGly

substrate from Bombyx mori

additional information

one enzyme form gives a sigmoidal response and a Hill coefficient of 2.2, while the other shows Michaelis-Menten kinetics

148

additional information

Km-values for mutant tRNAs

additional information

Km-values for mutant tRNAs

additional information

Km-values for mutant tRNAs

Salmonella enterica subsp. enterica serovar Typhimurium

additional information

overview

additional information

overview

additional information

overview

additional information

overview

additional information

overview

additional information

overview

additional information

dissociation constants for complexes of wild-type or mutant enzyme with tRNA and mRNA

additional information

kinetics for tRNAGly substrates of diverse prokaryotic and eukaryotic origins

additional information

thermodynamic parameters of substrate and inhibitor binding

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

15.9

tRNA1Gly

aminoacylation

8.1

tRNA2Gly

aminoacylation

0.19 - 0.73

tRNAGly

additional information

0.19

tRNAGly

wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.33

tRNAGly

wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

0.73

tRNAGly

wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

additional information

additional information

additional information

additional information

kcat for tRNAGly substrates of diverse prokaryotic and eukaryotic origins

show all columns Go to kcat/KM Value Search

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

140 - 1230

tRNAGly

140

tRNAGly

wild type isoform GlyRS1 without insertion peptide, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

220

tRNAGly

wild type isoform GlyRS2, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

1230

tRNAGly

wild type isoform GlyRS1, in 50 mM HEPES (pH 7.5), 50 mM KCl, 15 mM MgCl2, 5 mM dithiothreitol, at 25°C

show all columns Go to Ki Value Search

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Ki VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.02

5'-adenylylimidodiphosphate

0.0008

adenylylmethylenediphosphate

0.06

alpha,beta-methyleneadenosine 5'-diphosphate

0.08

AMP

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.0074

tetrameric enzyme form

0.124

purified recombinant enzyme

0.47

0.55

dimeric enzyme form

1.65

8.7

additional information

additional information

additional information

additional information

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7 - 8

7.2

7.5

7.6

enzyme form B, ATP-diphosphate exchange and glycine-charging activity

enzyme form A, glycine-charging activity

8 - 8.5

8.5

enzyme form A, ATP-diphosphate exchange

7.2

aminoacylation of tRNAGly

7.2

assay at

7.2

assay at

7.5

assay at

7.5

assay at

8 - 8.5

8 - 8.5

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

35 - 40

aminoacylation of tRNAGly

additional information

wild-type enzyme is active at 42°C, temperature-sensitive mutant enzyme not

assay at

assay at

show all columns Go to Organism Search

assay at

assay at

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Aeropyrum pernix

Aeropyrum pernix DSM 11879

Q9YBF8

SwissProt

brenda

Q9YBF8

SwissProt

brenda

brenda

brenda

brenda

92, 133

brenda

133, 147

brenda

alpha subunit

UniProt

brenda

alpha subunit

UniProt

brenda

Escherichia coli overproducing

133, 139

brenda

brenda

overproducing strain

brenda

brenda

brenda

brenda

brenda

brenda

Oryctolagus cuniculus

652046

brenda

2 dual-targeted isozymes

brenda

brenda

mitochondrial isoform GlyRS1

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt

brenda

brenda

brenda

brenda

SwissProt

brenda

brenda

2 dual-targeted isozymes

SwissProt

brenda

137, 156, 158, 652187

brenda

2 enzyme forms

143, 144

brenda

enzyme forms A and B

brenda

recombinant purified enzyme, expressed in Escherichia coli

brenda

wild-type and truncated enzyme forms

133, 140

brenda

133, 137, 138, 146, 151, 152, 154, 155, 157, 159

brenda

2 enzyme forms

148

brenda

overproducing strain

brenda

wild-type and mutant enzymes with altered amino acid binding site

135

brenda

wild-type and temperature-sensitive mutant

brenda

133, 134, 136, 137

brenda

651399, 675540, 676908

SwissProt

brenda

691544, 706875, 728398

brenda

744600, 745302, 745358, 745876

SwissProt

brenda

brenda

gene GARS

SwissProt

brenda

gene GARS

673686, 676881, 713735

brenda

brenda

BALB mice, gene GARS

brenda

mouse models of Charcot-Marie-Tooth disease type 2D, CMT2D, are established

brenda

133, 137, 138, 150, 151, 651424, 652455, 662193, 693172, 746265

brenda

2 genes grs1 and grs2 encoding GlyRS1, a mitochondrial and cytoplasmic isozyme, and GlyRS2, a dispensable mitochondrial isozyme

brenda

isoform GlyRS2

Q06817

UniProt

brenda

mitochondrial isoform GlyRS1

UniProt

brenda

133, 138, 141, 714047, 746265

brenda

class II enzyme

brenda

gene glyS

UniProt

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

brain

Ehrlich ascites carcinoma cell

brenda

brenda

brenda

brenda

peripheral

brenda

brenda

gene expression

brenda

brenda

brenda

uterus

brenda

Yoshida AH-130 cell

brenda

brenda

brenda

in the early-globular stage

brenda

embryo

brenda

brenda

brenda

92, 133

brenda

liver

brenda

liver

brenda

brenda

brenda

144

brenda

silk gland

posterior

143, 156, 158

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

brenda

of peripheral nerves

brenda

brenda

brenda

isozyme GlyRS2

brenda

isozyme GlyRS2

brenda

brenda

brenda

brenda

5737

652038, 746265

brenda

cytoplasm

brenda

gene product of GRS1 has enzymic activity both in cytoplasm and mitochondria

5737

brenda

cytoplasm

brenda

brenda

isozyme GlyRS1, active

brenda

brenda

brenda

isozyme GlyRS1, active

brenda

brenda

isozyme GlyRS2, enzyme is imported from the cytosol, nucleus-encoded

brenda

isozymes GlyRS1, enzyme is imported from the cytosol, nucleus-encoded, isozyme GlyRS1 is inactive in the mitochondria

brenda

brenda

706875, 728398, 746265

brenda

brenda

gene contains a mitochondrial targeting sequence

brenda

brenda

isozymes GlyRS1 and GlyRS2, enzymes are imported from the cytosol, nucleus-encoded, isozyme GlyRS1 is inactive in the mitochondria

brenda

mitochondrion

652038, 746265

brenda

mitochondrion

brenda

gene product of GRS1 has enzymic activity both in cytoplasm and mitochondria

brenda

mitochondrion

brenda

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show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

metabolism

the essential enzyme for protein synthesis also plays a critical role in neddylation by specifically binding to NEDD8 and enhancing neddylation. The enzyme preferentially binds and protects Ubc12N8 and E, and regulates cell cycle progression

physiological function

glycyl-tRNA synthetase specifically binds to the poliovirus internal ribosome entry site to activate translation initiation

malfunction

Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase

malfunction

Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase

malfunction

GARS gene mutations are involved in autosomal dominant motor distal neuronopathy/axonopathy, CMT2D/dSMA-V, and sporadic juvenile muscular atrophy of the distal upper extremity or Hirayama's disease, phenotype and mechanism, overview

713735

malfunction

enzyme knockdown decreases the global level of neddylation and causes cell cycle abnormality

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PDB

SCOP

CATH

UNIPROT

ORGANISM

5f5w, download, 3D-view

3rf1, download, 3D-view

SCOPe (3rf1)

CATH (3rf1)

A1VZ59

Campylobacter jejuni subsp. jejuni 81-176

Escherichia coli K-12

14 entries

Thermanaerothrix daxensis

7lu4, download, 3D-view

SCOPe (7lu4)

CATH (7lu4)

A0A0P6Y0P9

1j5w, download, 3D-view

3rgl, download, 3D-view

3ufg, download, 3D-view

7eiv, download, 3D-view

SCOPe (7eiv)

CATH (7eiv)

P00960, P00961

Escherichia coli K-12

7qcf, download, 3D-view

SCOPe (7qcf)

CATH (7qcf)

P00960

Escherichia coli K-12

2pme, download, 3D-view

2pmf, download, 3D-view

2q5h, download, 3D-view

2q5i, download, 3D-view

2zt5, download, 3D-view

2zt6, download, 3D-view

2zt7, download, 3D-view

2zt8, download, 3D-view

2zxf, download, 3D-view

4kqe, download, 3D-view

4kr2, download, 3D-view

4kr3, download, 3D-view

4qei, download, 3D-view

5e6m, download, 3D-view

1ati, download, 3D-view

SCOPe (1ati)

CATH (1ati)

1b76, download, 3D-view

SCOPe (1b76)

CATH (1b76)

1ggm, download, 3D-view

SCOPe (1ggm)

CATH (1ggm)

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

117000

135000 - 142000

sucrose density gradient centrifugation, dimeric enzyme form

155000

gel filtration, calculation from sedimentation constant

158000 - 160000

PAGE under nondenaturing conditions, gel filtration, dimeric enzyme form

160000

gel filtration, sedimentation velocity

189000

gel filtration, mitochondrial enzyme

202000

gel filtration, cytoplasmic enzyme

205000

high speed sedimentation equilibrium measurement

210000

sucrose density gradient centrifugation, tetrameric enzyme form

226000

gel filtration, enzyme form E1

227000

sedimentation equilibrium ultracentrifugation

230000

gel filtration

240000

PAGE

250000

PAGE under nondenaturing conditions, gel filtration, tetrameric enzyme form

27000

2-3 * 27000, about, partially processed isozyme GlyRS1, SDS-PAGE

270000

polyacrylamide 4/30% gradient PAGE

30000

33000

2 * 33000 (alpha) + 2 * 80000 (beta), SDS-PAGE

40000

x * 40000 + x * 78000, alpha-alpha interactions contibute to the stability of the native enzyme while beta-beta interactions do not, SDS-PAGE

51000

x * 51000, SDS-PAGE

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

66000

gel filtration, enzyme form E2

67600

72000

x * 72000, wild-type enzyme, SDS-PAGE

76919

x * 76919, wild-type enzyme, calculation from nucleotide sequence

77530

x * 77530, calculation from nucleotide sequence

78000

x * 40000 + x * 78000, alpha-alpha interactions contibute to the stability of the native enzyme while beta-beta interactions do not, SDS-PAGE

80000

81000

2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE

90000

2 * 90000, SDS-PAGE

additional information

primary structure of both subunits

154

117000

isozyme GlyRS2

117000

x * 117000, SDS-PAGE

30000

2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE

30000

4 * 30000, about, partially processed isozyme GlyRS2, SDS-PAGE

80000

isozyme GlyRS1

80000

2 * 80000, SDS-PAGE

80000

2 * 33000 (alpha) + 2 * 80000 (beta), SDS-PAGE

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

dimer or trimer

2-3 * 27000, about, partially processed isozyme GlyRS1, SDS-PAGE

heterotetramer

homodimer

tetramer

additional information

x * 117000, SDS-PAGE

x * 76919, wild-type enzyme, calculation from nucleotide sequence

x * 87000-90000, SDS-PAGE, gel filtration in 6 M guanidine-HCl

x * 77530, calculation from nucleotide sequence

x * 75000, SDS-PAGE

x * 72000, wild-type enzyme, SDS-PAGE

x * 51000, SDS-PAGE

dimer

alpha2

dimer

2 * 90000, SDS-PAGE

dimer

2 * 80000, SDS-PAGE

dimer

homodimer, crystal structure

dimer

homodimer, crystal structure, overall structural organization of GlyRS, overview

dimer

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

dimer

alpha2

heterotetramer

2 * 67400 + x * ?, calculated from amino acid sequence

heterotetramer

2 * 69100 + x * ?, SDS-PAGE

heterotetramer

heterotetramer

homodimer

homodimer

homodimer

tetramer

4 * 30000, about, partially processed isozyme GlyRS2, SDS-PAGE

tetramer

alpha2,beta2

tetramer

2 * 30000 (alpha) + 2 * 81000 (beta), enzyme form E1, SDS-PAGE, 2 * 30000, SDS-PAGE, enzyme form E2, E2 is a component of E1, SDS-PAGE

tetramer

alpha2,beta2

tetramer

2 * 33000 (alpha) + 2 * 80000 (beta), SDS-PAGE

tetramer

x * 40000 + x * 78000, alpha-alpha interactions contibute to the stability of the native enzyme while beta-beta interactions do not, SDS-PAGE

Escherichia coli overproducing

tetramer

x * 40000 + x * 78000, alpha-alpha interactions contibute to the stability of the native enzyme while beta-beta interactions do not, SDS-PAGE

tetramer

tetramer

additional information

polypeptide is weakly associated with multienzyme complexes consisting of aminoacyl-tRNA synthetases

additional information

additional information

sequence aligns well with a Bombyx mori sequence and a Saccharomyces cerevisiae sequence, but diverges widely from that of the Escherichia coli enzyme

137

additional information

structural alignment with the GlyRS from Thermus thermophilus

additional information

structural alignment with the GlyRS from Thermus thermophilus

additional information

comparison of structures of enzymes of diverse origins

show all columns Go to Posttranslational Modification Search

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

cytoplasmic and mitochondrial isoforms have the same polypeptide sequence except for a 23 amino acid mitochondrial leader peptide

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

alpha-subunit the enzyme and its complexes with ATP, and ATP and glycine, sitting drop vapor diffusion method, using 0.1 M Bis-Tris propane:NaOH pH 7.0 and 0.7 M magnesium formate (complex with glycine), or 0.1 M Tris-HCl pH 8.5 and 0.3 M magnesium chloride (complex with ATP), or 0.1 M Na2HPO4-citrate acid pH 4.2, 0.2 M lithium sulfate and 20% (w/v) PEG 1000 (complex with ATP and glycine)

apo form of full-length E71G mutant and tRNA-bound mutant complex E71G/C157R, vapor diffusion method, using 13-15% (w/v) PEG 6000, 0.1 M sodium citrate buffer (pH 5.5), and 0.1 M NaCl

745358

purified His-tagged wild-type and S581L mutant enzymes, sitting drop vapour diffusion nanocrystallization method, mutant S581L GlyRS from 20% PEG 3350, 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, wild-type GlyRS from 20% PEG 3350, 0.2M sodium bromide, 0.1 M bis-Tris propane pH 8.5, X-ray diffraction structure determination and anaylsis at 2.8A and 3.1 A resolution, respectively

purified recombinant soluble enzyme, hanging drop vapour diffusion method, 0.001 ml of 8 mg/ml protein in 10 mM HEPES, pH 7.0, with 20 mM NaCl is mixed with 0.001 ml of reservoir solution containing 10% PEG 6000, 0.1 HEPES pH 6.5, 0.01 Tris-HCl, pH 8.5, 0.5 NaCl and 0.1 magnesium acetate at room temperature, 2 days, X-ray diffraction structure determination and analysis at 3.0 A resolution

vapor diffusion method, using 0.2% (w/v) 4-diaminobutane, 0.2% (w/v) cystamine dihydrochloride, 0.2% (w/v) diloxanide furoate, 0.2% (w/v) sarcosine, 0.2% (w/v) spermine, and 0.02 M HEPES sodium (pH 6.8) at a 2:1:1 ratio

at 2.75 A resolution

141

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

P61L

mutant enzymes with an altered amino acid binding site. Pro61Leu substitution in the alpha chain confers an elevation of the Km value for Gly, 25fold, and for ATP, 45fold, in the aminoacylation reaction, but only a minor pertubation of the Km for tRNA

135

A57V

found in a screen of 33 patients

C157R

the activity of the mutant enzyme is 62% of wild type

D500N

E71G

E71G/C157R

the activity of the mutant enzyme is 20% of wild type

G240R

G526R

G598A

H418R

I280F

L129P

P234KY

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

P244L

disease phenotype CMT2D

Q640A

the mutation reduces the enzymatic activity by more than 10fold

Q675A

the mutation reduces the enzymatic activity by more than 10fold

Q675N

the mutation reduces the enzymatic activity by more than 10fold

Q82N

the mutant shows slightly increased activity compared to the wild type enzyme

R283A

the mutants retain 2% glycylation activity compared to the wild type enzyme

R283K

the mutants retain 20% glycylation activity compared to the wild type enzyme

R548A

the mutant shows strongly reduced activity compared to the wild type enzyme

R596Q

the mutation causes systemic mitochondrial disease

744600

R67A

the mutant shows reduced activity compared to the wild type enzyme

S281A

the mutant shows reduced activity compared to the wild type enzyme

S581L

S635L

the mutation causes systemic mitochondrial disease

744600

S91A

the mutant shows reduced activity compared to the wild type enzyme

T617A

the mutation reduces the enzymatic activity by more than 10fold

T631A

the mutant shows reduced activity compared to the wild type enzyme

Y604F

GarsC201R/+

mouse model, decreased grip strength, poor skilled motor function, increased total GARS protein at p15, reduction in large diameter axon in sciatic nerve, normal lifespan

GarsC201R/C201R

mouse model, reduced weight and viability, impaired limb movement, life expectancy 17 days

GarsC201R/XM256

mouse model, embryonic lethal

GarsNmf249/+

mouse model, sensory and motor deficits, abnormal neuromuscular junction morphology, impaired nerve impule transmission, reduced nerve conduction velocities, loss of large diameter peripheral axons, life expectancy 6-8 weeks

GarsNmf249/Nmf249

mouse model, embryonic lethal

GarsNmf249/XM256

mouse model, embryonic lethal

GarsP278KY/+

GarsXM256/+

mouse model, reduced GARS RNA levels, normal neuromuscular junction morphology, normal nerve conduction velocities, normal lifespan

GarsXM256/XM256

mouse model, embryonic lethal

P552F

temperature-sensitive mutant grs1-1 shows altered substrate specificities, the mutant strain can be complemented by expression of the wild-type enzyme

additional information

13 entries

D500N

naturally occuring mutation in the catalytic domain, the mutation lies in the disordered insertion III and causes Charcot-Marie-Tooth peripheral neuropathies

D500N

disease phenotype CMT2D/dSMA-V

E71G

modeled in yeast the mutation causes growth defects and impaired viability

E71G

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

E71G

the mutant shows increased activity compared to the wild type enzyme

E71G

disease phenotype CMT2D/dSMA-V

E71G

the mutant shows slightly elevated aminoacylation activity over wild type

745358

G240R

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

G240R

the GARS mutation does not impair transcription or translation, modeled in yeast the mutation causes growth defects and impaired viability

G240R

disease phenotype CMT2D

G526R

modeled in yeast the mutation causes growth defects and impaired viability

G526R

naturally occuring mutation at the site for synthesis of glycyl-adenylate, G526 is a strictly conserved residue in the middle of motif 3, the mutant is inactive and shows tighter dimer interaction compared to the wild-type enzyme, long-range structural effects of the Charcot-Marie-Tooth disease-causing mutation in the human enzyme, overview

G526R

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

G526R

disease phenotype dSMA-V

G598A

naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

G598A

severe HMN

H418R

modeled in yeast the mutation causes growth defects and impaired viability

H418R

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

H418R

disease phenotype dSMA-V

I280F

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

I280F

disease phenotype CMT2

L129P

modeled in yeast the mutation causes growth defects and impaired viability

L129P

naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

L129P

disease phenotype dSMA-V

S581L

naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies

S581L

the naturally occuring dominant mutation to reduced aminoacylation activity and to motor nerve degeneration

S581L

disease phenotype lower limb predominant, CMT2

Y604F

the mutant shows strongly reduced activity compared to the wild type enzyme

Y604F

the mutation reduces the enzymatic activity by more than 10fold

additional information

direction of a marker protein into isolated pea chloroplasts by the N-terminal domain of the enzyme, construction of the embryo-defective development mutant edd1 by usage of transposons as insertional mutagens, the reversible mutation leads to arrest of embryo growth and is lethal, generation of transgenic plants

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

additional information

additional information

additional information

temperature-sensitive mutant

additional information

fusion of carboxyl terminus of the alpha-chain to the amino-terminus of the beta-chain through a short peptide linker. The fusion protein is active to within 2fold to 3fold of the wild-type, unfused chains

159

additional information

additional information

expression in Escherichia coli as a fusion protein with 13 kDa biotinylated tag with an apparent MW of 90 kDa

additional information

GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, most catalytic-domain mutations are at the dimer interface, overview, mapping mutations onto human GlyRS crystal structure show them within a band encompassing both sides of the dimer interface, with two CMT-causing mutations being at sites that are complementary partners of a kissing contact across the dimer interface, the CMT phenotype does not correlate with aminoacylation activity, overview

additional information

mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells, and four of the five mutations show loss-of-function, GARS-associated granules occur in the neurite projections of cultured neurons and in the peripheral nerve axons of normal human tissue

additional information

additional information

a dominant mutation Nmf249 of gene GARS causes Charcot-Marie-Tooth peripheral neuropathy type 2D, phenotype analysis, the dominant phenotype is not caused by loss of GlyRS aminoacylation function, mutant mice have abnormal neuromuscular junction morphology and impaired transmission, reduced nerve conduction velocities, and a loss of large-diameter peripheral axons, without defects in myelination, overview, construction of a loss-of-function mutant by gene-trap insertion, which shows no dominant phenotype, overview

additional information

a defective mutant grs1-1 allel confers the temperature-sensitive growth defect by affection with the 3'-end formation

651424

show all columns Go to Temperature Stability Search

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

half-life of temperature-sensitive mutant: 30 min

80% loss of activity after 1 min in absence of substrates, 60% loss of activity after 10 min in presence of aminoethyl-AMP and Mg2+

83.2

melting temperature of the alpha-subunit

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

aminoethyl-AMP protects from heat inactivation

ATP and nonsubstrate ATP analogues render the enzyme more resistant to digestion by several proteases, e.g. thrombin, Arg-C, and chymotrypsin

DTT or 25% glycerol stabilizes

glycerol required for stabilization

glycyl-adenylate stabilizes the enzyme

in absence of protease inhibitors and/or dithioerythritol, the enzyme rapidly loses its activity

protectors of SH groups at concentrations of 20 mM are required to obtain an optimal aminoacylation rate

sensitive to repeated freezing and thawing

unstable after dilution to less than 0.02 mg/ml in absence of nonspecific carrier proteins

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-15°C, enzyme concentration 0.5 mg/ml, 40% glycerol, 30% loss of activity after 8 months

-80°C, retains approximately 90% of its activity after 3 months

Go to Purification (commentary) Search

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

2 enzyme forms: E1 and E2

glutathione Sepharose column chromatography

glutathione-Sepharose column chromatography, and gel filtration

Ni-affinity column chromatography

Ni-NTA column chromatography

recombinant C-terminally His6-tagged cytosolic enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

recombinant enzyme from Escherichia coli, 10fold

recombinant His-atgged wild-type enzyme and P552F mutant from Escherichia coli

recombinant His-tagged isozymes GlyRS1 and 2 from Escherichia coli

recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

recombinant isozyme GlyRS1 from Escherichia coli

Superdex 200 gel filtration

133, 146, 149, 155

156, 158

Ni-NTA column chromatography

Ni-NTA column chromatography

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

2 genes: grs1 encodes mitochondrial and cytoplasmic isozyme, grs2 encodes a mitochondrial dipensable isozyme, expression in Escherichia coli as HIs-tagged proteins, both cytoplasmic and mitochondrial phenotypes of a knockout allele of grs1 are complemented by the expression of the single gene of Schizosaccharomyces pombe, expression of gene grs2 in a grs1-deficient yeast mutant cannot complement the lethal phenotype

as a fusion protein with 13 kDa biotinylated tag with an apparent MW of 90 kDa

DNA sequence determination and analysis of full-length edd1 wild-type gene, encoding the enzyme, gene contains a chloroplast targeting sequence, determination of the promoter, functional complementation of enzyme-deficient Arabidopsis plants thereby generation of transgenic plants

DNA sequence determination and analysis, chromosomal localization in region 7p15.1-p15.3, the gene contains only 1 transcriptional start point in 3 different cell lines, but 5 potential initiation codons, expression may be translationally regulated, N-terminal mitochondrial targeting sequence

651399

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli Rosetta (DE3) cells

expressed in Saccharomyces cerevisiae grs1-deficient cells

expressed in Saccharomyces cerevisiae strain InvSc1

expression in Escherichia coli

134, 136

expression of CMT-causing mutant variants and wild-type enzymes in neuroblastoma cells that sprout primitive neurites

expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)

expression of His-tagged wild-type and p552F mutant enzyme in Escherichia coli

expression of wild-type and N-terminally truncated enzyme, the latter lacking 55 N-terminal amino acid residues, in Escherichia coli BL21(DE3)

gene GARS, allele-specific expression analysis, expression of wild-type enzyme in Escherichia coli strain BL21(DE3), expression of EGFP-tagged enzyme in COS-7 cells, wild-type GARS-EGFP associates with granules in both the cell body and neurite projections of 42% of EGFP-positive transfected MN-1 cells

gene GARS, DNA and amino acid sequence determination and analysis, genetic mapping

gene GARS, lacking the mitochondrial-specific coding region, expression as C-terminally His6-tagged cytosolic enzyme in Escherichia coli strain BL21(DE3)

gene glyS, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli BL21(DE3)

gene glyS, GlyRS phylogenetic analysis, deduction of ancestral sequence of GlyRS, and introduction of individual or pairs of ancestral residues into Thermus thermophilus GlyRS resulting in ancestral mutants, which are expressed in Escherichia coli strain BL21(DE3), overview

675441

gene grs1 is essential

651424

overexpression of isozyme GlyRS1 in Escherichia coli strain TG2

139

133, 152

137

expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells

expressed in Saccharomyces cerevisiae grs1-deficient cells

expressed in Saccharomyces cerevisiae grs1-deficient cells

expressed in Saccharomyces cerevisiae grs1-deficient cells

Go to Renatured Search

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

show all columns Go to Application Search

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

medicine

molecular biology

translation of mRNA for yeast glycyl-tRNA synthetase is alternatively initiated from UUG and a downstream AUG initiation codon. Unlike an AUG initiation codon, efficiency of this non-AUG initiation codon is significantly affected by its sequence context, in particular the nucleotides at positions -3 to -1 relative to the initiation codon. A/A/R (R: A or G) and C/G/C appear to be the most and least favorable sequences at these positions, respectively. Mutation of the native context sequence -3 to -1 from AAA to CGC reduce translation initiation from the UUG codon up to 32fold and resulted in loss of mitochondrial respiration

693172

medicine

the distribution of mutations in the seven genes identified for hereditary motor neuropathy (HMN) is investigated in a cohort of 112 familial and isolated patients with a diagnosis of HMN. Nine different disease-causing mutations are found in small heat shock 22 kDa protein 8, small heat shock 27 kDa protein 1, Berardinelli-Seip congenital lipodystrophy and senataxin in 17 patients. No mutations are found in glycyl-tRNA synthetase, dynactin 1 and VAPB(VAMP)-associated protein B and C

691544

medicine

Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase

medicine

Charcot-Marie-Tooth disease, CMT, type 2D, a hereditary axonal neuropathy, is caused by mutations in glycyl-tRNA synthetase

top print hide References Search

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Walker, E.J.; Treacy, G.B.; Jeffrey, P.D.

Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes

Biochemistry

1934-1941

1983

Bos taurus

6849897

brenda

Freist, W.; Logan, D.T.; Gauss, D.H.

Glycyl-tRNA synthetase

Biol. Chem. Hoppe-Seyler

377

343-356

1996

Aliivibrio fischeri, Alcaligenes faecalis, Geobacillus stearothermophilus, Brevibacillus brevis, Bombyx mori, Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Chlamydia trachomatis, Escherichia coli, eukaryota, Thermus thermophilus, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus, Mus musculus, Mycoplasma genitalium, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium

8839980

brenda

Williams, J.; Osvath, S.; Khong, T.F.; Pearse.M.; Power, D.

Cloning, sequencing and bacterial expression of human glycine tRNA synthetase

Nucleic Acids Res.

1307-1310

1995

Homo sapiens

7753621

brenda

135

Toth, M.J.; Schimmel, P.

A mutation in the small subunit of glycyl-tRNA synthetase affects amino acid activation and subunit association parameters

J. Biol. Chem.

265

1005-1009

1990

Escherichia coli

2295596

brenda

Ge, Q.; Trieu, E.P.; Targoff, I.N.

Primary structure and functional expression in human glycyl-tRNA synthetase, an autoantigen in myositis

J. Biol. Chem.

269

28790-28797

1994

Homo sapiens

7961834

brenda

137

Shiba, K.; Schimmel, P.; Motegi, H.; Noda, T.

Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation

J. Biol. Chem.

269

30049-30055

1994

Bombyx mori, Escherichia coli, Homo sapiens, Saccharomyces cerevisiae

7962006

brenda

Nameki, N.; Tamura, K.; Asahara, H.; Hasegawa, T.

Recognition of tRNAGly by three widely diverged glycyl-tRNA synthetases

J. Mol. Biol.

268

640-647

1997

Escherichia coli, Saccharomyces cerevisiae, Thermus thermophilus

9171287

brenda

139

Wagar, E.A.; Giese, M.J.; Yasin, B.; Pang, M.

The glycyl-tRNA synthetase of Chlamydia trachomatis

J. Bacteriol.

177

5179-5185

1995

Chlamydia trachomatis

7665503

brenda

Wu, H.; Nada, S.; Dignam, D.

Analysis of truncated forms of Bombyx mori glycyl-tRNA synthetase: Function of an N-terminal structure in RNA binding

Biochemistry

16327-16336

1995

Bombyx mori

8845358

brenda

141

Logan, D.T.; Mazauric, M.H.; Kern, D.; Moras, D.

Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus

EMBO J.

4156-4167

1995

Thermus thermophilus

7556056

brenda

Niyomporn, B.; Dahl, J.L.; Strominger, J.L.

Biosynthesis of the peptidoglycan of bacterial cell walls. IX. Purification and properties of glycyl transfer ribonucleic acid synthetase from Staphylococcus aureus

J. Biol. Chem.

243

773-778

1968

Staphylococcus aureus, Staphylococcus aureus H

4295604

brenda

Kurosawa, S.; Komano, T.; Onodera, K.

Glycine activating enzyme in the posterior silkgland of silkworm

Agric. Biol. Chem.

779-784

1972

Bombyx mori

brenda

144

Kurosawa, S.; Onodera, K.

Correlation between two glycine tRNAs and corresponding glycyl tRNA synthetase

Agric. Biol. Chem.

1051-1053

1972

Bombyx mori

brenda

Roback, E.R.; Friesen, J.D.; Fiil, N.P.

A temperature-sensitive glycyl-transfer ribonucleic acid synthetase mutant of Escherichia coli

Can. J. Microbiol.

421-426

1972

Escherichia coli

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