GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:15687192
| Citation |
Fukushima, T, Kitajima, T and Sekiguchi, J (2005) A polysaccharide deacetylase homologue, PdaA, in Bacillus subtilis acts as an N-acetylmuramic acid deacetylase in vitro. J. Bacteriol. 187:1287-92 |
|---|---|
| Abstract |
A polysaccharide deacetylase homologue, PdaA, was determined to act as an N-acetylmuramic acid deacetylase in vitro. Histidine-tagged truncated PdaA (with the putative signal sequence removed) was overexpressed in Escherichia coli cells and purified. Measurement of deacetylase activity showed that PdaA could deacetylate peptidoglycan treated with N-acetylmuramoyl-L-alanine amidase CwlH but could not deacetylate peptidoglycan treated with or without DL-endopeptidase LytF (CwlE). Reverse-phase high-performance liquid chromatography and mass spectrometry (MS) and MS-MS analyses indicated that PdaA could deacetylate the N-acetylmuramic acid residues of purified glycan strands derived from Bacillus subtilis peptidoglycan. |
| Links |
PubMed PMC545626 Online version:10.1128/JB.187.4.1287-1292.2005 |
| Keywords |
Amidohydrolases/biosynthesis; Amidohydrolases/genetics; Amidohydrolases/isolation & purification; Amidohydrolases/metabolism; Bacillus subtilis/enzymology; Chromatography, High Pressure Liquid; Endopeptidases/metabolism; Mass Spectrometry; Muramic Acids/metabolism; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Recombinant Proteins/biosynthesis; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0019213: deacetylase activity |
ECO:0000314: |
F |
Figure 4. The mass spectrometry and MS-MS analyses indicated that PdaA could deacetylate the N-acetylmuramic acid residues of purified glycan strands derived from Bacillus subtilis peptidoglycan. |
complete | ||||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
