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Literature summary for 5.1.3.11 extracted from

  • Fujiwara, T.; Saburi, W.; Matsui, H.; Mori, H.; Yao, M.
    Structural insights into the epimerization of beta-1,4-linked oligosaccharides catalyzed by cellobiose 2-epimerase, the sole enzyme epimerizing non-anomeric hydroxyl groups of unmodified sugars (2014), J. Biol. Chem., 289, 3405-3415.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.1.3.11

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli Rhodothermus marinus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme in apoform and complexed with D-glucose-D-mannose, epilactose, and reaction intermediate analogue cellobiitol, sitting drop vapor diffusion method, mixing of 500 nl of 5 mg/ml protein in 30 mM Tris-HCl, pH 8.5, and 60 mM NaCl, with 500 nl reservoir solution containing 0.1 M sodium acetate, pH 4.5, and 1.2 M ammonium hydrogen phosphate, 5 days, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.74-2.19 A resolution Rhodothermus marinus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-O-beta-D-mannopyranosyl-D-mannose Rhodothermus marinus
-
 4-O-beta-D-glucopyranosyl-D-mannose
-
 r
cellobiose Rhodothermus marinus
-
 4-O-beta-D-glucopyranosyl-D-mannose
-
 r
lactose Rhodothermus marinus
-
 epilactose
-
 r
additional information Rhodothermus marinus cellobiose 2-epimerase reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodothermus marinus F8WRK9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by heat treatment, anion exchange chromatography, and dialysis Rhodothermus marinus

Reaction

Reaction Comment Organism Reaction ID
cellobiose = 4-O-beta-D-glucopyranosyl-D-mannose mechanism of reversible epimerization involving three histidine residues, overview. His390 is closely related to ring opening/closure by transferring a proton between the O5 and O1 atoms of the ligand. His259 abstracts the H2 proton of the D-mannose residue at the reducing end, and consistently forms the cis-enediol intermediate by facilitated depolarization of the 2-OH group mediated by hydrogen bonding interaction with His200. His390 subsequently donates the proton to the C2 atom of the intermediate to form a D-glucose residue. The reverse reaction is mediated by the three histidines with the inverse roles of acid/base catalysts Rhodothermus marinus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-O-beta-D-mannopyranosyl-D-mannose
-
 Rhodothermus marinus 4-O-beta-D-glucopyranosyl-D-mannose
-
 r
cellobiose
-
 Rhodothermus marinus 4-O-beta-D-glucopyranosyl-D-mannose
-
 r
cellobiose
-
 Rhodothermus marinus 4-O-beta-D-glucopyranosyl-D-mannose binding structure, overview r
lactose
-
 Rhodothermus marinus epilactose
-
 r
lactose
-
 Rhodothermus marinus epilactose binding structure, overview r
additional information cellobiose 2-epimerase reversibly converts D-glucose residues into D-mannose residues at the reducing end of unmodified beta-1,4-linked oligosaccharides, including beta-1,4-mannobiose, cellobiose, and lactose Rhodothermus marinus ?
-
 ?

Synonyms

Synonyms Comment Organism
cellobiose 2-epimerase
-
 Rhodothermus marinus

General Information

General Information Comment Organism
metabolism the enzyme is responsible for conversion of beta-1,4-mannobiose to 4-O-beta-D-mannosyl-D-glucose in mannan metabolism Rhodothermus marinus
additional information determination of residues involved in substrate recognition, overview Rhodothermus marinus