Literature summary for 5.3.1.5 extracted from

Munshi, P.; Snell, E.H.; van der Woerd, M.J.; Judge, R.A.; Myles, D.A.; Ren, Z.; Meilleur, F.
Neutron structure of the cyclic glucose-bound xylose isomerase E186Q mutant (2014), Acta Crystallogr. Sect. D, 70, 414-420 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Streptomyces rubiginosus

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of E186Q mutant with cyclic glucose bound at the active site, to 2.2 A resolution. Residue His54 is doubly protonated and is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. An extended hydrogen-bonding network connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186	Streptomyces rubiginosus

Crystallization (Comment)

Organism

structure of E186Q mutant with cyclic glucose bound at the active site, to 2.2 A resolution. Residue His54 is doubly protonated and is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. An extended hydrogen-bonding network connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186

Streptomyces rubiginosus

Protein Variants

Protein Variants	Comment	Organism
E186Q	crystallization data	Streptomyces rubiginosus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces rubiginosus	P24300	-	-

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Release 2023.1 (January 2023)