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Literature summary extracted from

  • Yamazaki, Y.; Kimura, S.; Ohmae, M.
    Reaction specificity of keratanase II in the transglycosylation using the sugar oxazolines having keratan sulfate repeating units (2018), Carbohydr. Res., 456, 61-68 .
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B43 Niallia circulans
-
-
-
3.2.1.B43 Niallia circulans KsT202
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B43 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 ?
-
 ?
3.2.1.B43 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

EC Number Synonyms Comment Organism
3.2.1.B43 keratanase II
-
 Niallia circulans
3.2.1.B43 KSase II
-
 Niallia circulans