Literature summary for 5.3.1.5 extracted from

Langan, P.; Sangha, A.K.; Wymore, T.; Parks, J.M.; Yang, Z.K.; Hanson, B.L.; Fisher, Z.; Mason, S.A.; Blakeley, M.P.; Forsyth, V.T.; Glusker, J.P.; Carrell, H.L.; Smith, J.C.; Keen, D.A.; Graham, D.E.; Kovalevsky, A.
L-Arabinose binding, isomerization, and epimerization by D-xylose isomerase X-ray/neutron crystallographic and molecular simulation study (2014), Structure, 22, 1287-1300 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the mechanism of ring-opening for L-arabinose is the same as for the reaction with D-xylose. In the reactive Michaelis complex L-arabinose is distorted to the high-energy 5S1 conformation. Amino acid substitutions in a hydrophobic pocket near C5 of L-arabinose can enhance sugar binding. L-ribulose and L-ribose are found in furanose forms when bound to the enzyme	Streptomyces rubiginosus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces rubiginosus	P24300	-	-

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Release 2023.1 (January 2023)