Article ID Journal Published Year Pages File Type
1937265 Biochemical and Biophysical Research Communications 2007 6 Pages PDF
Abstract

Cellobiose 2-epimerase (EC 5.1.3.11) was first identified in 1967 as an extracellular enzyme that catalyzes the reversible epimerization between cellobiose and 4-O-β-d-glucopyranosyl-d-mannose in a culture broth of Ruminococcus albus 7 (ATCC 27210T). Here, for the first time, we describe the purification of cellobiose 2-epimerase from R. albus NE1. The enzyme was found to 2-epimerize the reducing terminal glucose moieties of cellotriose and cellotetraose in addition to cellobiose. The gene encoding cellobiose 2-epimerase comprises 1170 bp (389 amino acids) and is present as a single copy in the genome. The deduced amino acid sequence of the mature enzyme contains the possible catalytic residues Arg52, His243, Glu246, and His374. Sequence analysis shows the gene shares a very low level of homology with N-acetyl-d-glucosamine 2-epimerases (EC 5.1.3.8), but no significant homology to any other epimerases reported to date.

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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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