Role of lipid modification on a starch-debranching enzyme, Klebsiella pullulanase

Comparison of properties of lipid-modified and unmodified pullulanases

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

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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 pullula-nase 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.

Original languageEnglish
Pages (from-to)389-394
Number of pages6
JournalMolecular Microbiology
Volume6
Issue number3
Publication statusPublished - 1992 Feb
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Role of lipid modification on a starch-debranching enzyme, Klebsiella pullulanase : Comparison of properties of lipid-modified and unmodified pullulanases. / Yamashita, Mitsuo; Nakagawa, A.; Katsuragi, N.; Murooka, Y.

In: Molecular Microbiology, Vol. 6, No. 3, 02.1992, p. 389-394.

Research output: Contribution to journalArticle

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