Literature summary for 3.2.1.101 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 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Organism

Organism	UniProt	Comment	Textmining
Niallia circulans	Q9Z4P9	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Niallia circulans

Synonyms

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

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Release 2023.1 (January 2023)