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Literature summary for 3.2.1.B43 extracted from

  • Ohmae, M.; Sakaguchi, K.; Kaneto, T.; Fujikawa, S.; Kobayashi, S.
    Keratanase II-catalyzed synthesis of keratan sulfate oligomers by using sugar oxazolines as transition-state analogue substrate monomers a novel insight into the enzymatic catalysis mechanism (2017), Chembiochem, 8, 1710-1720 .
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus sp. Ks36
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information transglycosylation to form beta-(1->3)-glycosidic bond through a substrate-assisted mechanism. N-Acetyllactosamine oxazoline derivatives with sulfate groups at the C-6 are effectively oligomerized by the enzyme under weak alkaline conditions, to give alternating 6-sulfated keratan sulfate oligomers in good yields. The enzyme also recognized N-acetyllactosamine oxazoline derivatives with sulfate groups at both the C-6 and the C-6', which provides fully 6-sulfated KS oligomers in good yields under similar conditions. Nonsulfated LacNAc oxazoline is difficult to oligomerize enzymatically. The catalysis mechanism of KSase II involves a sugar oxazolinium ion that requires the 6-sulfate group in the GlcNAc residue not only in hydrolysis of keratan sulfate chains, but also in oligomerization of oxazoline monomers Bacillus sp. Ks36 ?
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Synonyms

Synonyms Comment Organism
keratanase II
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Bacillus sp. Ks36
KSase II
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Bacillus sp. Ks36