A mutant phospholipase D with enhanced thermostability from Streptomyces sp.

Tadashi Hatanaka, Tomofumi Negishi, Koichi Mori

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)


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
Issue number1
Publication statusPublished - Jan 14 2004
Externally publishedYes


  • Biocatalyst
  • Phospholipase D
  • Streptomyces
  • Thermostability

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology


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