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KMID : 0545120080180040746
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Journal of Microbiology and Biotechnology
2008 Volume.18 No. 4 p.746 ~ p.753
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Characterization of a Bifunctional HPr Kinase/Phosphorylase from Leuconostoc mesenteroides SY1
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Park Jae-Yong
Lee Kang-Wook
Lee Ae-Ran
Jeong Woo-Ju
Chun Ji-Yeon
Lee Jong-Hoon
Kim Jeong-Hwan
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Abstract
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The hprK gene encoding bifunctional HPrK/P (kinase/ phosphorylase) was cloned from L. mesenteroides SY1, a strain isolated from kimchi. hprK was transcribed as a monocistronic gene. His-tagged HPrH16A and HPrK/P were produced in E. coli BL21(DE3) using pET26b(+) and purified. HPrK/P phosphorylation assay with purified proteins showed that the kinase activity of HPrK/P increased at slightly acidic pHs. Divalent cations such as Mg2+ and Mn2+ and glycolytic intermediates such as fructose-1, 6-bisphosphate (FBP) and phosphoenolpyruvate (PEP) increased the kinase activity of HPrK/P, but inorganic phosphate strongly inhibited it. Kinetic studies for the kinase activity of HPrK/P showed that the apparent Km values were 0.18 and 14.57 μM for ATP and HPr, respectively. The Km value for the phosphorylase activity of HPrK/P was 14.16 μM for P-Ser-HPr (HPr phosphorylated at the serine residue).
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KEYWORD
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HPr kinase/phosphorylase, hprK, Leuconostoc mesenteroides, catabolite repression
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