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Literature summary for 3.2.1.B43 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

Organism UniProt Comment Textmining
Niallia circulans
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-
-
Niallia circulans KsT202
-
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
keratanase II
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Niallia circulans
KSase II
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Niallia circulans