Recycling of murein by Escherichia coli.
AUTOR(ES)
Goodell, E W
RESUMO
The tripeptide (L-Ala-D-Glu-meso-diaminopimelic acid [A2pm]), tetrapeptide (L-Ala-D-Glu-A2pm-D-Ala), and dipeptide (A2pm-D-Ala) which are shed by Escherichia coli from the murein sacculus were found to be reused by the cells to synthesize murein. The tripeptide was used directly, without degradation, to form UDP-N-acetylmuramyl-L-Ala-D-Glu-A2pm. The tetrapeptide lost its carboxy-terminal D-Ala, apparently in the periplasm, before being used. The dipeptide was degraded to D-Ala and A2pm before uptake.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=219113Documentos Relacionados
- Murein segregation in Escherichia coli.
- Absence of oligomeric murein intermediates in Escherichia coli.
- Novel type of murein transglycosylase in Escherichia coli.
- Analysis of murein and murein precursors during antibiotic-induced lysis of Escherichia coli.
- Two different species of murein transglycosylase in Escherichia coli.