5.4.99.62: D-ribose pyranase
This is an abbreviated version!
For detailed information about D-ribose pyranase, go to the full flat file.
Reaction
Synonyms
FucU, RbsD
ECTree
5.4.99.62 D-ribose pyranaseAdvanced search results
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results (Crystallization
Crystallization on EC 5.4.99.62 - D-ribose pyranase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
to 2.3 A resolution. Protein shows a decameric toroidal assembly. The intersubunit cleft of the protein binds specific forms of D-ribose, but it does not have an enzyme activity toward the sugar
to 1.9 A resolution. Protein forms a decameric toroid with each active site formed by two adjacent subunits. While one subunit provides most of the fucose-interacting residues including a catalytic tyrosine residue, the other subunit provides a catalytic His-Asp dyad. This active-site feature is critical both for the mutarotase activity toward L-fucose and for the pyranase activity toward D-ribose
to 1.9 A resolution. Protein assembles into four different oligomeric forms, among which the smallest homodimeric form is most abundant and would be the predominant species under physiological conditions. This homodimer has two fucose-binding sites that are devoid of the His-Asp dyad and catalytically inactive, indicating that the mutarotase and the pyranase activities appear dispensable in vertebrates
