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Literature summary for 6.3.1.2 extracted from

  • Kimura, K.; Sugano, S.
    Inactivation of Bacillus subtilis glutamine synthetase by metal-catalyzed oxidation (1992), J. Biochem., 112, 828-833.
    View publication on PubMed

General Stability

General Stability Organism
EDTA and EGTA stabilize. The combination of substrates, Mn2+, ATP and PMSF Bacillus subtilis
native and oxidized forms of enzyme are both cleaved in the same manner by chymotrypsin. Oxidized enzyme is completely cleaved during the 60 min incubation whereas the native enzyme is not completely digested Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol
-
Bacillus subtilis
dithiothreitol
-
Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis KN2
-
-
-

Oxidation Stability

Oxidation Stability Organism
enzyme is protected from oxidative modification by either 5 mM Mn2+ or 5 mM Mn2+ plus 5 mM ATP, but not by Mg2+. Oxidative modification induces relatively subtle changes in the dodecameric enzyme molecules, but does not denature the protein Bacillus subtilis
inactivation by metal-catalyzed oxidation Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + NH4+
-
Bacillus subtilis ADP + phosphate + L-Gln
-
?
ATP + L-Glu + NH4+
-
Bacillus subtilis KN2 ADP + phosphate + L-Gln
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
1 h, about 60% loss of activity in cell-free extract Bacillus subtilis