Role of lipid modification on a starch‐debranching enzyme, Klebsieila pullulanase: comparison of properties of lipid‐modified and unmodified pullulanases

M. Yamashita, A. Nakagawa, N. Katsuragi, Y. Murooka

研究成果: Article査読

6 被引用数 (Scopus)

抄録

Klebsiella pullulanase is a lipoprotein synthesized as a precursor with a signal peptide, which is processed by lipoprotein signal peptidase. To clarify the role of lipid modification of pullulanase, we purified lipid‐modified wild‐type and the unmodified (mutant) pullulanases and compared their properties. The Km and Vmax values of both pullulanases for pullulan were the same. The optimal pH and temperature, the stabilities over pH and temperature ranges, the specificity of substrates, and the patterns of inhibition of the lipid‐modified and unmodified pullulanases were also the same. However, we found that the wild‐type pullulanase formed trimers whereas the unmodified enzyme did not, and that the migrations of the two enzymes on sodium dodecyl sulphate/electrophoresis were different when the samples were applied on the gel without heating. The results presented in this paper and in previous work show that the correct processing and translocation of pullulanase in K. aerogenes require modification of lipid. However, the enzymatic properties and physical stabilities of pullulanase were not affected by the lipid modification.

本文言語English
ページ(範囲)389-394
ページ数6
ジャーナルMolecular Microbiology
6
3
DOI
出版ステータスPublished - 1992 2月
外部発表はい

ASJC Scopus subject areas

  • 微生物学
  • 分子生物学

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