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Characterization of a bacterial laminaribiose phosphorylase
Motomitsu Kitaoka1, Yasuyuki Matsuoka, Kiyotaka Mori
1National Food Research Institute, National Agriculture and Food Research Organization, Tsukuba, Ibaraki, Japan. mkitaoka@affrc.go.jp
Bioscience, Biotechnology, and Biochemistry
|February 9, 2012
Summary
Bacterial laminaribiose phosphorylase (LBP(bac)) from Paenibacillus sp. YM-1 specifically breaks down laminaribiose. Its gene (lbpA) is linked to a transporter, suggesting extracellular sugar utilization.
Area of Science:
- Enzymology
- Microbial biochemistry
- Carbohydrate metabolism
Background:
- Bacterial laminaribiose phosphorylase (LBP(bac)) was identified in Paenibacillus sp. YM-1.
- LBPs are enzymes involved in carbohydrate breakdown.
- Distinct LBPs exist with varying substrate specificities and biological roles.
Purpose of the Study:
- To characterize the substrate specificity and biochemical properties of bacterial laminaribiose phosphorylase (LBP(bac)).
- To investigate the genetic context and potential function of LBP(bac) within Paenibacillus sp. YM-1.
- To compare LBP(bac) with other known laminaribiose phosphorylases, such as LBP(Eug).
Main Methods:
- Enzyme purification from cell-free extracts.
- Enzyme activity assays with various oligosaccharides.
- Gene cloning and sequence analysis.
- Bioinformatic analysis of gene clusters.
Main Results:
- LBP(bac) selectively phosphorolyzed laminaribiose into α-glucose 1-phosphate and glucose.
- It showed limited activity on higher laminarioligosaccharides, differing from LBP(Eug).
- LBP(bac) belongs to the glucoside hydrolase family 94.
- Genes for an oligosaccharide transporter were found upstream of the lbpA gene.
Conclusions:
- LBP(bac) exhibits distinct substrate specificity compared to LBP(Eug).
- The genetic linkage suggests LBP(bac) functions in the extracellular utilization of laminaribiose.
- This contrasts with the intracellular role of LBP(Eug) in paramylon degradation.
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