The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-l-alanine amidase
JV Höltje, U Kopp, A Ursinus… - FEMS microbiology …, 1994 - academic.oup.com
JV Höltje, U Kopp, A Ursinus, B Wiedemann
FEMS microbiology letters, 1994•academic.oup.comConstruction 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-
anhydromuramyl-L-alanine amidase AmpD is likely to be involved in recycling of the …
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-
anhydromuramyl-L-alanine amidase AmpD is likely to be involved in recycling of the …
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-anhydromuramyl-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 β-lactamase induction.
Oxford University Press