Literature summary for 5.3.1.5 extracted from

Varsani, L.; Cui, T.; Rangarajan, M.; Hartley, B.S.; Goldberg, J.; Collyer, C.; Blow, D.M.
Arthrobacter D-xylose isomerase: protein-engineered subunit interfaces (1993), Biochem. J., 291, 575-583.

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Cloned(Commentary)

Cloned (Comment)	Organism
wild-type and mutant enzymes, expression in Escherichia coli	Arthrobacter sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutant enzymes	Arthrobacter sp.

Protein Variants

Protein Variants	Comment	Organism
Y253C	a Tyr253 mutant in which a disulfide bridge is introduced at the A-B subunit interface shows reduced thermostability, that is identical in both oxidized and reduced forms and also reduced stability in urea. X-ray-crystallographic analysis of the Mn2+-xylitol form of oxidized Y253C shows a changed conformation of Glu185 and also alternative conformations for Asp254, which is a ligand to the site 2 metal ion. With fructose, Mg2+-Y253C has a similar Km to that of the wild-type, and its maximal velocity is also similar below pH 6.4, but declines thereafter. In presence of Co2+, Y253C has lower activity than wild-type at all pH values, but its activity also declines at alkaline pH	Arthrobacter sp.

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter sp.	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Arthrobacter sp.

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-Xylose	-	Arthrobacter sp.	D-Xylulose	-	?

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Release 2023.1 (January 2023)