Literature summary for 3.2.1.8 extracted from

Soliman, M.E.; Ruggiero, G.D.; Pernia, J.J.; Greig, I.R.; Williams, I.H.
Computational mutagenesis reveals the role of active-site tyrosine in stabilising a boat conformation for the substrate: QM/MM molecular dynamics studies of wild-type and mutant xylanases (2009), Org. Biomol. Chem., 7, 460-468.

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Protein Variants

Protein Variants	Comment	Organism
Y69F	the barrier for conversion of the 4C1 chair to the more-stable 2,5B boat in the wild-type enzyme-substrate complex is significantly lower than it is for the mutant. The mutation reduces the degree of oxacarbenium-ion character in the proximal xylose ring of the enzyme-substrate complex	Niallia circulans

Organism

Organism	UniProt	Comment	Textmining
Niallia circulans	P09850	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the proximal sugar-ring of the substrate distorts from 4C1 chair to 2,5B boat conformation. Key role of Tyr69 in stabilizing the boat in preference to the 4C1 chair conformation	Niallia circulans	?	-	?

Subunits

Subunits	Comment	Organism
More	catalytic residues are Glu78 and Glu172	Niallia circulans

Synonyms

Synonyms	Comment	Organism
endo-beta-1,4-xylanase	-	Niallia circulans
G/11 endo-1,4-beta-xylanase	-	Niallia circulans

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Release 2023.1 (January 2023)