Characterization of a bacterial laminaribiose phosphorylase

Abstract

Bacterial laminaribiose phosphorylase (LBP bac) was first identified and purified from cell-free extract of Paenibacillus sp. YM-1. It phosphorolyzed laminaribiose into α-glucose 1-phosphate and glucose, but did not phosphorolyze other glucobioses. It slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The specificity of the degree of polymerization of the substrate was clearly different from that of the enzyme of Euglena gracilis (LBP Eug): LBP bac was more specific to laminaribiose than LBP Eug. It showed acceptor specificity in reverse phosphorolysis similar to LBP Eug. Cloning of the gene encoding LBP bac (lbpA) has revealed that LBP bac is a member of the glucoside hydrolase family 94, which includes cellobiose phosphorylase, cellodextrin phosphorylase, and N,N0-diacetylchitobiose phosphorylase. The genes that encode the components of an ATP-binding cassette sugar transporter specific to laminarioligosaccharides were identified upstream of lbpA, suggesting that the role of LBP bac is to utilize laminaribiose generated outside the cell. This role is different from that of LBP Eug, which participates in the utilization of paramylon, the intracellular storage 1,3-β-glucan. © 2012 W. S. Maney & Son Ltd.