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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

Reaction

ATP
+
glycine
+
tRNAGly
=
AMP
+
diphosphate
+
glycyl-tRNAGly

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 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.14 glycine-tRNA ligase

Molecular Weight

Molecular Weight on EC 6.1.1.14 - glycine-tRNA ligase

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
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