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PMID:16530188
| Citation |
Llull, D, López, R and García, E (2006) Skl, a novel choline-binding N-acetylmuramoyl-L-alanine amidase of Streptococcus mitis SK137 containing a CHAP domain. FEBS Lett. 580:1959-64 |
|---|---|
| Abstract |
The skl gene from Streptococcus mitis SK137 encodes a peptidoglycan hydrolase (Skl) that has been purified and biochemically characterized. Analysis of the degradation products obtained by digestion of pneumococcal cell walls with Skl revealed that this enzyme is an N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28), showing optimum activity at 30 degrees C and at a pH of 6.5. Skl is a unique member of the choline-binding family of proteins since it contains a cysteine, histidine-dependent amidohydrolases/peptidases (CHAP) domain. The CHAP domain of Skl showed homology to lysins of unknown especificity from a variety of streptococcal prophages. Skl represents the first characterized member of a new subfamily of CHAP-containing choline-binding proteins. |
| Links |
PubMed Online version:10.1016/j.febslet.2006.02.060 |
| Keywords |
Amino Acid Sequence; Cell Wall/metabolism; Choline/metabolism; Chromatography, Gel; Hydrogen-Ion Concentration; Molecular Sequence Data; N-Acetylmuramoyl-L-alanine Amidase/chemistry; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Protein Binding; Protein Structure, Tertiary; Sequence Analysis, DNA; Streptococcus mitis/enzymology; Streptococcus pneumoniae/metabolism |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0008745: N-acetylmuramoyl-L-alanine amidase activity |
ECO:0000314: |
F |
Analysis of the degradation products obtained by digestion of pneumococcal cell walls with Skl revealed that this enzyme is an N-acetylmuramoyl-L-alanine amidase. Figure 4A: The elution patterns showed that Skl promoted the separation of the glycan chains associated with the choline-containing teichoic acids from the lysine-containing muropeptides and indicated that Skl is either an NAM-amidase or an endopeptidase. Figure 4B: . A preparation of muropeptides was obtained by gel filtration in a Bio-Gel P4 column, and the N-terminal amino acid determined in the three pooled fractions, yielding Ala in all cases (not shown). These results taken together demonstrated that Skl is an NAM-amidase. |
complete | ||||
Notes
See also
References
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