6.1.1.14: glycine-tRNA ligase
This is an abbreviated version!
For detailed information about glycine-tRNA ligase, go to the full flat file.
Word Map on EC 6.1.1.14
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6.1.1.14
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cord
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glycinergic
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postsynaptic
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strychnine
-
alpha1
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synthetases
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synapses
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ligand-gated
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aminoacyl-trna
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homomeric
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gabaars
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neurotransmission
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electrophysiological
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aminoacylation
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charcot-marie-tooth
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strychnine-sensitive
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gephyrin
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patch-clamp
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hyperekplexia
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presynaptic
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heteromeric
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startle
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pentameric
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gabaergic
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extrasynaptic
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picrotoxin
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glycylation
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glycine-induced
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single-channel
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glycine-activated
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cys-loop
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anticodon
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mipscs
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subunit-specific
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bicuculline
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glycine-gated
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outside-out
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subunit-containing
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alars
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two-electrode
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alpha2beta
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mesolimbic
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pore-lining
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hisrs
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glycine-mediated
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accumbal
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gabaar-mediated
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molecular biology
-
medicine
- 6.1.1.14
- cord
-
glycinergic
-
postsynaptic
- strychnine
- alpha1
- synthetases
-
synapses
-
ligand-gated
- aminoacyl-trna
-
homomeric
-
gabaars
-
neurotransmission
-
electrophysiological
- aminoacylation
- charcot-marie-tooth
-
strychnine-sensitive
-
gephyrin
-
patch-clamp
- hyperekplexia
-
presynaptic
-
heteromeric
-
startle
-
pentameric
-
gabaergic
-
extrasynaptic
- picrotoxin
-
glycylation
-
glycine-induced
-
single-channel
-
glycine-activated
-
cys-loop
-
anticodon
-
mipscs
-
subunit-specific
- bicuculline
-
glycine-gated
-
outside-out
-
subunit-containing
- alars
-
two-electrode
-
alpha2beta
-
mesolimbic
-
pore-lining
- hisrs
-
glycine-mediated
-
accumbal
-
gabaar-mediated
- molecular biology
- medicine
Reaction
Synonyms
GARS, Glycine--tRNA ligase, Glycyl translase, glycyl tRNA synthetase, Glycyl-transfer ribonucleate synthetase, Glycyl-transfer ribonucleic acid synthetase, Glycyl-transfer RNA synthetase, Glycyl-tRNA synthetase, glycyl-tRNA synthetase 1, GlyRS, GlyRS1, GlyRS2, GRS1, More, Synthetase, glycyl-transfer ribonucleate
ECTree
6.1.1.14 glycine-tRNA ligaseAdvanced search results
results (
results (General Stability
General Stability on EC 6.1.1.14 - glycine-tRNA ligase
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
ATP and nonsubstrate ATP analogues render the enzyme more resistant to digestion by several proteases, e.g. thrombin, Arg-C, and chymotrypsin
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in absence of protease inhibitors and/or dithioerythritol, the enzyme rapidly loses its activity
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protectors of SH groups at concentrations of 20 mM are required to obtain an optimal aminoacylation rate
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unstable after dilution to less than 0.02 mg/ml in absence of nonspecific carrier proteins
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