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Literature summary extracted from

  • Belz, T.; Jin, Y.; Coines, J.; Rovira, C.; Davies, G.J.; Williams, S.J.
    An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor (2017), Chem. Commun. (Camb.), 53, 9238-9241 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.101 the non-hydrolyzable S-linked azasugars, 1,6-alpa-mannosylthio- and 1,6-alpha-mannobiosylthioisofagomine bind with high affinity to the enzyme. X-ray crystallography shows an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener Niallia circulans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.101 [(3R,4R, 5R)-4,5-dihydroxypiperidin-3-yl]methyl 1-thio-alpha-D-mannopyranoside
-
 Niallia circulans
3.2.1.101 [(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl 6-S-alpha-D-mannopyranosyl-1,6-dithio-alpha-D-mannopyranoside
-
 Niallia circulans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.101 Niallia circulans Q9Z4P9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.101
-
 Niallia circulans

Synonyms

EC Number Synonyms Comment Organism
3.2.1.101 BcGH76
-
 Niallia circulans
3.2.1.101 endo-1,6-alpha-mannanase
-
 Niallia circulans