Structural highlights
Publication Abstract from PubMed
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-beta-D-glucopyranosyl-D-gluconic acid: phosphate alpha-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 alpha-D-glucose 1-phosphate and D-gluconic acid to enter glycolysis and the pentose phosphate pathway, respectively.
Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi.,Nihira T, Saito Y, Nishimoto M, Kitaoka M, Igarashi K, Ohtsubo K, Nakai H FEBS Lett. 2013 Nov 1;587(21):3556-61. doi: 10.1016/j.febslet.2013.09.014. Epub, 2013 Sep 19. PMID:24055472[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nihira T, Saito Y, Nishimoto M, Kitaoka M, Igarashi K, Ohtsubo K, Nakai H. Discovery of cellobionic acid phosphorylase in cellulolytic bacteria and fungi. FEBS Lett. 2013 Nov 1;587(21):3556-61. doi: 10.1016/j.febslet.2013.09.014. Epub, 2013 Sep 19. PMID:24055472 doi:http://dx.doi.org/10.1016/j.febslet.2013.09.014
