gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization.
AUTOR(ES)
Suzuki, H
RESUMO
Escherichia coli cells showed maximum activity of gamma-glutamyltranspeptidase (EC 2.3.2.2) when they were grown at 20 degrees C, 14% of maximum activity at 37 degrees C, and none at 43 degrees C. The enzyme activity of intact cells grown at 20 degrees C was stably maintained after the temperature was changed to 45 degrees C. The activity increased during the exponential phase, and maximum activity was found at stationary phase. Its intracellular localization in the periplasmic space was confirmed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=213642Documentos Relacionados
- gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties.
- DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt.
- gamma-Glutamyltranspeptidase from Proteus mirabilis: localization and activation by phospholipids.
- Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis.
- Escherichia coli K-12 can utilize an exogenous gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase is essential.
