Characterisitics and gene cloning of phospholipase D of the psychrophile, Shewanella sp

Biosci Biotechnol Biochem. 2007 Oct;71(10):2534-42. doi: 10.1271/bbb.70325. Epub 2007 Oct 7.

Abstract

Phospholipase D, with a molecular mass of 64 kDa, was purified from the psychrophile, Shewanella sp. The enzyme showed maximal activity at pH 7.8 and 40 degrees C in the presence of the Ca2+-ion, and its activity at 10 degrees C was 6.5% of maximum. The enzyme exhibited high activity to the non-micelle form of phosphatidylcholine in an aqueous solution containing water miscible alcohols such as methanol, ethanol, iso-propanol, and n-propanol. Nucleotide sequencing of the enzyme gene yielded a deduced amino acid sequence, which showed 36.2% identity to that of Streptomyces chromofuscus phospholipase D alone. The low sequence similarity to other phospholipase D enzymes suggests that the purified enzyme might be a novel phospholipase D.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular*
  • Enzyme Stability
  • Gene Expression
  • Genes, Bacterial*
  • Hydrogen-Ion Concentration
  • Inclusion Bodies / chemistry
  • Metals, Heavy / pharmacology
  • Molecular Sequence Data
  • Molecular Weight
  • Phospholipase D / chemistry
  • Phospholipase D / genetics*
  • Phospholipase D / isolation & purification
  • Phospholipase D / metabolism
  • Protein Folding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Shewanella / enzymology*
  • Shewanella / genetics
  • Temperature

Substances

  • Metals, Heavy
  • Recombinant Proteins
  • Phospholipase D