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Literature summary for 6.1.1.14 extracted from

  • Kern, D.; Giege, R.; Ebel, J.P.
    Glycyl-tRNA synthetase from baker's yeast. Interconversion between active and inactive forms of the enzyme (1981), Biochemistry, 20, 122-131.
    View publication on PubMed

General Stability

General Stability Organism
in absence of protease inhibitors and/or dithioerythritol, the enzyme rapidly loses its activity Saccharomyces cerevisiae
protectors of SH groups at concentrations of 20 mM are required to obtain an optimal aminoacylation rate Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000088
-
tRNAGly
-
Saccharomyces cerevisiae
0.021
-
ATP
-
Saccharomyces cerevisiae
0.25
-
Gly
-
Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Mg2+ optimal MgCl2/ATP ratio is 1.5 Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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 Saccharomyces cerevisiae
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 Saccharomyces cerevisiae
135000 142000 sucrose density gradient centrifugation, dimeric enzyme form Saccharomyces cerevisiae
158000 160000 PAGE under nondenaturing conditions, gel filtration, dimeric enzyme form Saccharomyces cerevisiae
210000
-
sucrose density gradient centrifugation, tetrameric enzyme form Saccharomyces cerevisiae
250000
-
PAGE under nondenaturing conditions, gel filtration, tetrameric enzyme form Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0074
-
tetrameric enzyme form Saccharomyces cerevisiae
0.55
-
dimeric enzyme form Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycine + tRNAGly
-
Saccharomyces cerevisiae AMP + diphosphate + glycyl-tRNAGly
-
?
additional information catalyzes glycine-dependent ATP-diphosphate exchange Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
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 Saccharomyces cerevisiae
tetramer 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 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35 40 aminoacylation of tRNAGly Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
aminoacylation of tRNAGly Saccharomyces cerevisiae