A mutant phospholipase D with enhanced thermostability from Streptomyces sp.

Tadashi Hatanaka, Tomofumi Negishi, Koichi Mori

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

To investigate the contribution of amino acid residues to the thermostability of phospholipase D (PLD), a chimeric form of two Streptomyces PLDs (thermolabile K1PLD and thermostable TH-2PLD) was constructed. K/T/KPLD, in which residues 329-441 of K1PLD were recombined with the homologous region of TH-2PLD, showed a thermostability midway between those of K1PLD and TH-2PLD. By comparing the primary structures of Streptomyces PLDs, the seven candidates of thermostability-related amino acid residues of K1PLD were identified. The K1E346DPLD mutant, in which Glu346 of K1PLD was substituted with Asp by site-directed mutagenesis, exhibited enhanced thermostability, which was almost the same as that of TH-2PLD.

Original languageEnglish
Pages (from-to)75-82
Number of pages8
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1696
Issue number1
DOIs
Publication statusPublished - Jan 14 2004
Externally publishedYes

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Phospholipase D
Streptomyces
Amino Acids
Mutagenesis
Site-Directed Mutagenesis
1-dodecylpyridoxal

Keywords

  • Biocatalyst
  • Phospholipase D
  • Streptomyces
  • Thermostability

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics

Cite this

A mutant phospholipase D with enhanced thermostability from Streptomyces sp. / Hatanaka, Tadashi; Negishi, Tomofumi; Mori, Koichi.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1696, No. 1, 14.01.2004, p. 75-82.

Research output: Contribution to journalArticle

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