The negative regulator of beta-lactamase induction AmpD is a 
N-acetyl-anhydromuramyl-L-alanine amidase

Höltje, J-V; Kopp, U; Ursinus, A; Wiedemann, B

doi:10.1111/j.1574-6968.1994.tb07159.x

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The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase

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Höltje, J-V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Ursinus, A
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Höltje, J.-V., Kopp, U., Ursinus, A., & Wiedemann, B. (1994). The negative regulator of beta-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiology Letters, 122(1-2), 159-164. doi:10.1111/j.1574-6968.1994.tb07159.x.

Cite as: https://hdl.handle.net/21.11116/0000-000D-F187-A

Abstract

Construction of a malE-ampD gene fusion allowed purification of biologically active fusion protein by affinity chromatography. The cloned malE-ampD gene fusion complemented a chromosomal ampD mutation. Purified MalE-AmpD fusion protein was found to have murein amidase activity with a pronounced specificity for 1,6-anhydromuropeptides, the characteristic murein turnover products in Escherichia coli. Being a N-acetyl-anhydromuranmyl-L-alanine amidase AmpD is likely to be involved in recycling of the turnover products. It is suggested that the negative regulatory effect of AmpD is due to the hydrolysis of anhydro-muropeptides which may function as signals for beta-lactamase induction.