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Gene Review:

ampD - N-acetyl-anhydromuranmyl-L-alanine amidase

Escherichia coli CFT073

Jacobs, C. et al., Everett, M. et al., Jones, M.E. et al.

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Disease relevance of ampD

Escherichia coli JRG582 is an ampD ampE deletion derivative of strain HfrH and accordingly it is derepressed for expression of the cloned inducible beta-lactamase gene of Citrobacter freundii, carried on plasmid pNU305 [1].
Cells lacking either AmpG or AmpD lose up to 40% of their peptidoglycan per generation, whereas Escherichia coli normally suffers minimal losses and instead recycles 40 or 50% of the tripeptide, L-alanyl-D-glutamyl-meso-diaminopimelic acid, from its peptidoglycan each generation [2].

High impact information on ampD

In contrast, the ampD mutant accumulates a novel cell wall muropeptide, 1,6-anhydro N-acetylmuramyl-L-alanyl-D-glutamyl-meso-diaminopimelic acid (anhMurNAc-tripeptide), in its cytoplasm [2].
This work suggests that AmpG is the permease for a large muropeptide and AmpD is a novel cytosolic N-acetylmuramyl-L-alanine amidase that cleaves anhMurNAc-tripeptide to release tripeptide, which is then recycled [2].
The inducible phenotype was dependent on the E. coli ampD and ampG gene products [3].

References

GcvA, a LysR-type transcriptional regulator protein, activates expression of the cloned Citrobacter freundii ampC beta-lactamase gene in Escherichia coli: cross-talk between DNA-binding proteins. Everett, M., Walsh, T., Guay, G., Bennett, P. Microbiology (Reading, Engl.) (1995) [Pubmed]
Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction. Jacobs, C., Huang, L.J., Bartowsky, E., Normark, S., Park, J.T. EMBO J. (1994) [Pubmed]
Inducible expression of the chromosomal cdiA from Citrobacter diversus NF85, encoding an ambler class A beta-lactamase, is under similar genetic control to the chromosomal ampC, encoding an ambler class C enzyme, from Citrobacter freundii OS60. Jones, M.E., Bennett, P.M. Microb. Drug Resist. (1995) [Pubmed]

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