EC Number   |
General Information |
Reference |
|---|
   3.5.1.28 | evolution |
Ami1 belongs to the amidase_3 domain family |
-, 755454 |
| 3.5.1.28 | evolution |
AmiC and AmiA structure comparisons. Neisseria gonorrhoeae has only one cell separation amidase (AmiC) in contrast to other baceria, e.g. Escherichia coli |
754131 |
| 3.5.1.28 | evolution |
peptidoglycan recognition proteins (PGRPs) are a family of pattern recognition receptors that recognize peptidoglycans and modulate innate immune responses. Some PGRPs retain N-acetylmuramoyl-L-alanine amidase activity to hydrolyse bacterial peptidoglycans |
753816 |
| 3.5.1.28 | evolution |
the enzyme belongs to the Pfam family Amidase_3, the mode of substrate binding is likely shared by the Amidase_3 family proteins |
-, 734236 |
| 3.5.1.28 | evolution |
the enzyme's the C-terminus does not display homology to any identifiable domain |
755094 |
| 3.5.1.28 | evolution |
three main cell wall lytic enzymes, CwlB (also named LytC), CwlC, and CwlH, are identified in Bacillus subtilis. CwlB is the major vegetative autolysin produced at the end of exponential growth phase, and it is also present during sporulation. CwlC and CwlH are sporulation-specific autolysins whose production is Sigma K-dependent |
-, 752553 |
| 3.5.1.28 | evolution |
two proteins, namely RC0497 and RC1358, belong to the AmpD superfamily containing an amidase_2 domain as defined in the Pfam database (PF01510) and potentially endowed with amidase activity, phylogenetic analysis. The PG_binding_1 domain is present only in RC0497 at the C-terminus, but missing in RC1358 |
-, 752896 |
| 3.5.1.28 | malfunction |
analysis of peptidoglycan (PG) muropeptide composition and glycan chain length distribution of wild-type strain 26695 and its amiA mutant: the analysis shows that Helicobacter pylori lacks muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant is also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. Modifications in PG composition of amiA mutant, overview. The susceptibility of the cells to different antibiotics is unaltered in the amiA mutant cells compared to wild-type cells |
-, 754640 |
| 3.5.1.28 | malfunction |
CwlC point mutations at the two conserved catalytic glutamic acid residues, Glu24 and Glu140, result in a complete loss of cell wall lytic activity. The CwlC protein consists of an N-terminal N-acetylmuramoyl-L-alanine amidase (MurNAc-LAA) domain and a C-terminal amidase02 domain. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis |
-, 752553 |
| 3.5.1.28 | malfunction |
deletion of amiC from Neisseria gonorrhoeae results in severely impaired cell separation and altered peptidoglycan (PG) fragment release. Mutation Q316K results in an AmiC with increased enzymatic activity on macromolecular PG and on the synthetic PG derivative. Mutation Q316K also results in cell separation and PG fragment release defects |
-, 754131 |
