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2.4.1.281: 4-O-beta-D-mannosyl-D-glucose phosphorylase

This is an abbreviated version!
For detailed information about 4-O-beta-D-mannosyl-D-glucose phosphorylase, go to the full flat file.

Word Map on EC 2.4.1.281

Reaction

4-O-beta-D-mannopyranosyl-D-glucopyranose
+
phosphate
=
D-glucose
 +
alpha-D-mannose 1-phosphate

Synonyms

BF0772, MP1, RaMp1, RaMp2, Rumal_0852

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.281 4-O-beta-D-mannosyl-D-glucose phosphorylase

Crystallization

Crystallization on EC 2.4.1.281 - 4-O-beta-D-mannosyl-D-glucose phosphorylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.68 A resolution. The enzyme shows a homohexameric structure, which is formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. In complexes with substrates, 4-O-beta-D-mannosyl-D-glucose and phosphate, and the product D-mannose-1-phosphate the structures reveal that the invariant residue Asp131, is supposed to be the general acid/base, does not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction
crystal structure with/without 4-O-beta-D-mannosyl-D-glucose. His245 of loop 3 forms a hydrogen-bond network with the substrate through a water molecule, and is indispensible for substrate binding