Literature summary for 5.4.99.62 extracted from

Lee, K.H.; Ryu, K.S.; Kim, M.S.; Suh, H.Y.; Ku, B.; Song, Y.L.; Ko, S.; Lee, W., Oh, B.H.
Crystal structures and enzyme mechanisms of a dual fucose mutarotase/ribose pyranase (2009), J. Mol. Biol., 391, 178-191.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Mus musculus
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	Escherichia coli

Crystallization (Comment)

Organism

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

Mus musculus

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

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D64N	mutant exhibits significantly reduced catalytic activity toward D-ribose	Escherichia coli
H22A	mutant exhibits significantly reduced catalytic activity toward D-ribose	Escherichia coli
Y111F	mutant exhibits significantly reduced catalytic activity toward D-ribose	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEN8	bifunctional L-fucose mutarotase, EC 5.1.3.29, and L-rhamnose mutarotase	-
Mus musculus	Q8R2K1	bifunctional L-fucose mutarotase, EC 5.1.3.29, and L-rhamnose mutarotase	-

Synonyms

Synonyms	Comment	Organism
FucU	-	Escherichia coli
FucU	-	Mus musculus