Display Settings:

Format

Send to:

Choose Destination

anhydromuropeptides recycling

Anhydromuropeptides (mainly : CPD0-1080) are steadily released during growth by lytic transglycosylases and endopeptidases and imported back into the cytoplasm for recycling. During bacterial growth, a very large proportion of the peptidoglycan polymer is degraded and reused in a process termed cell wall recycling. For example, the Gram-negative bacterium : TAX-562 recovers about half of its cell wall within one generation . The anhydromuropeptides are imported by the : EG12183-encoded : AMPG-MONOMER. Once inside the cytoplasm, the anhydromuropeptides are hydrolyzed by : EC-3.5.1.28 (: EG10041), : EC-3.2.1.52 (: G6567) and : G6621-MONOMER (: G6621), yielding : N-ACETYL-D-GLUCOSAMINE, : CPD0-882, : L-ALA-GAMMA-D-GLU-DAP and : D-ALANINE . : CPD0-882 is phosphorylated by : EC-2.7.1.170 (: G6880) and then converted into : N-ACETYL-D-GLUCOSAMINE-6-P by : EC-4.2.1.126 (: G7263). This is a branch point, as this compound could be directed either for further degradation (see pathways of : N-Acetylglucosamine-Degradation) or for recycling into new peptidoglycan monomers, as described in this pathway . The final product of this pathway, : UDP-N-ACETYLMURAMATE, is one of the precursors for peptidoglycan biosynthesis. The tripeptide : L-ALA-GAMMA-D-GLU-DAP, which is generated by : EC-3.4.17.13, can be degraded further, as described in : PWY0-1546. However, the vast majority is recycled by muropeptide ligase (: EG12440). This enzyme is a dedicated recycling enzyme that attaches the recovered Ala-Glu-DAP tripeptide to : UDP-N-ACETYLMURAMATE, thereby substituting three amino acid ligases of the peptidoglycan de novo biosynthetic pathway . Although exogenously provided : CPD0-882 can be taken up by :TAX-562, it can not serve as the sole source of carbon for growth, suggesting that it may be toxic to the cell .

from BIOCYC source record: ECO_PWY0-1261
Type: pathway
Taxonomic scope
:
organism-specific biosystem
Organism
:
Escherichia coli
BSID:
218

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center