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Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi
Author(s) -
Nihira Takanori,
Saito Yuka,
Nishimoto Mamoru,
Kitaoka Motomitsu,
Igarashi Kiyohiko,
Ohtsubo Ken‧ichi,
Nakai Hiroyuki
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.09.014
Subject(s) - phosphorolysis , biochemistry , neurospora crassa , glycoside hydrolase , enzyme , glycogen phosphorylase , biology , cellobiose , bacteria , gluconic acid , chemistry , microbiology and biotechnology , cellulase , purine nucleoside phosphorylase , genetics , purine , gene , mutant
A novel phosphorylase was characterized as new member of glycoside hydrolase family 94 from the cellulolytic bacterium Xanthomonas campestris and the fungus Neurospora crassa . The enzyme catalyzed reversible phosphorolysis of cellobionic acid. We propose 4‐ O ‐β‐ d ‐glucopyranosyl‐ d ‐gluconic acid: phosphate α‐ d ‐glucosyltransferase as the systematic name and cellobionic acid phosphorylase as the short names for the novel enzyme. Several cellulolytic fungi of the phylum Ascomycota also possess homologous proteins. We, therefore, suggest that the enzyme plays a crucial role in cellulose degradation where cellobionic acid as oxidized cellulolytic product is converted into α‐ d ‐glucose 1‐phosphate and d ‐gluconic acid to enter glycolysis and the pentose phosphate pathway, respectively.