Purification and characterization of lysophospholipase-transacylase (h-LPTA) from a highly virulent strain of Candida albicans

Fariba Mirbod, Yoshiko Banno, Mahmoud A. Ghannoum, Ashraf S. Ibrahim, Shigeru Nakashima, Yasuo Kitajima, Garry T. Cole, Yoshinori Nozawa

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49 Scopus citations


A lysophospholipase-transacylase (h-LPTA) was purified to homogeneity from a clinical isolate of Candida albicans (C. albicans) that had high extracellular phospholipase activity (strain 16240). The purified enzyme was a glycoprotein with molecular mass of 84 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The specific activities of the enzyme were 117 μmol/min per mg protein for fatty acid release and 459 μmol/min per mg protein for phosphatidylcholine (PC) formation. An apparent Km of the hydrolase activity of the enzyme for 1-palmitoyl-sn-glycero-3-phosphocholine (1-palmitoyl-lyso-PC) was 60.6 μM. The enzyme had a pH optimum at 6.0. Transacylase activity of the enzyme was partially inhibited by palmitoy1camitine (35% inhibition) and N-ethylmaleimide. In contrast, the hydrolase activity of the enzyme was stimulated by palmitoylcamitine but was partially inhibited by N-ethylmaleimide. The enzyme exhibited broad specificity to lyso-phospholipads. The h-LPTA activity was not dependent on divalent cations (Ca2+ and Mg2+) and was not inhibited by addition of EDTA or EGTA. These results show that C. albicans strain 16240 with high extracellular phospholipase activity produced h-LPTA in large amount. This enzyme is biochemically distinct from the LPTA enzyme previously isolated from C. albicans 3125.

Original languageEnglish (US)
Pages (from-to)181-188
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Issue number2
Publication statusPublished - Jul 13 1995
Externally publishedYes



  • (C. albicans)
  • Enzyme characterization
  • Lysophospholipase-transacylase
  • Phospholipase
  • Virulence factor

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Endocrinology

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