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1 confirms that the enzyme is a zinc-dependent N-acetylmuramoyl-l-alanine amidase.
2 ding frame whose predicted product resembles N-acetylmuramoyl-L-alanine amidases.
4 ure to translocate three Tat substrates, the N-acetylmuramoyl-l-alanine amidases, AmiA and AmiC, and
5 ns, the latter of which functions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine
8 report that human PGRP-L is a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase (EC 3.5.1.28), an enz
9 ed Tat-dependent proteins and found that two N-acetylmuramoyl-l-alanine amidases, encoded by amiA and
10 bacterial proteins (triacylglycerol lipase, N-acetylmuramoyl-L-alanine amidase, flagellin, outer mem
13 s mutant phenotype is the first found for an N-acetylmuramoyl-l-alanine amidase PGRP that cleaves pep
15 glycan recognition protein 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacte
16 glycan recognition protein 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacte
17 dation products, we showed that Lc-Lys is an N-acetylmuramoyl-L-alanine amidase, whereas Lc-Lys-2 is
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