Organism | UniProt | Comment | Textmining |
---|---|---|---|
Niallia circulans | - |
- |
- |
Niallia circulans KsT202 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | specificity of the transglycosylation. The oxazoline derivative of 6-O-sulfonato-N-acetyllactosamine is processively oligomerized to the corresponding hexamer or longer. This result strongly implies that the enzyme has the large positively numbered subsites. In contrast, the transglycosylation of the su-LacNAc oxazoline donor with the 6-O-sulfonato-Lewis X (su-LeX) acceptor solely gave the su-LacNAc-su-LeX pentasaccharide. In addition, both the oxazoline derivatives of su-LeX and 6,6'-di-O-sulfonato-LacNAc are exclusively oligomerized to the corresponding dimers respectively. These results strongly suggest that the steric hindrance exists around the (+3)(+4) subsites in keratanase II. Furthermore, KSase II-catalyzed reaction of the excess su-LeX oxazoline with the su-LacNAc gives the su-LeX-su-LacNAc pentasaccharide as the sole transglycosylation product, also implying the steric hindrance at the catalytic center hampering processive shift of this pentasaccharide. Thus, KSase II has the sterically crowded structures at the catalytic center and around the (+3)(+4) subsites, which are all expected to be tunnel-like | Niallia circulans | ? | - |
? | |
additional information | specificity of the transglycosylation. The oxazoline derivative of 6-O-sulfonato-N-acetyllactosamine is processively oligomerized to the corresponding hexamer or longer. This result strongly implies that the enzyme has the large positively numbered subsites. In contrast, the transglycosylation of the su-LacNAc oxazoline donor with the 6-O-sulfonato-Lewis X (su-LeX) acceptor solely gave the su-LacNAc-su-LeX pentasaccharide. In addition, both the oxazoline derivatives of su-LeX and 6,6'-di-O-sulfonato-LacNAc are exclusively oligomerized to the corresponding dimers respectively. These results strongly suggest that the steric hindrance exists around the (+3)(+4) subsites in keratanase II. Furthermore, KSase II-catalyzed reaction of the excess su-LeX oxazoline with the su-LacNAc gives the su-LeX-su-LacNAc pentasaccharide as the sole transglycosylation product, also implying the steric hindrance at the catalytic center hampering processive shift of this pentasaccharide. Thus, KSase II has the sterically crowded structures at the catalytic center and around the (+3)(+4) subsites, which are all expected to be tunnel-like | Niallia circulans KsT202 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
keratanase II | - |
Niallia circulans |
KSase II | - |
Niallia circulans |