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Kasinathan C, Chopra A, Khuller GK. Phosphatidate phosphatase of dermatophytes. Lipids. 1982;17(12):859-63doi: 10.1007/BF02534579.
Kasinathan, C., Chopra, A., & Khuller, G. K. (1982). Phosphatidate phosphatase of dermatophytes. Lipids, 17(12), 859-63. https://doi.org/10.1007/BF02534579
Kasinathan, C, et al. "Phosphatidate phosphatase of dermatophytes." Lipids vol. 17,12 (1982): 859-63. doi: https://doi.org/10.1007/BF02534579
Kasinathan C, Chopra A, Khuller GK. Phosphatidate phosphatase of dermatophytes. Lipids. 1982 Dec;17(12):859-63. doi: 10.1007/BF02534579. PMID: 27519433.
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Lipids. 1982 Dec;17(12):859-63. doi: 10.1007/BF02534579.

Phosphatidate phosphatase of dermatophytes.

Lipids

C Kasinathan, A Chopra, G K Khuller

Affiliations

  1. Department of Biochemistry, Postgraduate Institute of Medical Education and Research, 160 012, Chandigarh, India.

PMID: 27519433 DOI: 10.1007/BF02534579

Abstract

Phosphatidate phosphatase (EC 3.1.3.4) was detected in filamentous pathogenic fungi. In both dermatophytes,Microsporum gypseum andEpidermophyton floccosum, the enzyme was located in the mitochondrial and microsomal subcellular fractions with a pH optimum of 6.0. TheE. floccosum enzyme was more active than that ofM. gypseum. Although the enzyme in both fractions of the dermatophytes was susceptible to inhibition by Fe(2+), Mn(2+), Cu(2+), Ba(2+) and Hg(2+), theE. floccosum microsomal enzyme was completely inhibited by Mn(2+) and Fe(2+). The enzyme ofM. gypseum as well as ofE. floccosum exhibited a Mg(2+) dependency in presence of EDTA. Sulphydryl reagents did not inhibit either the mitochondrial or the microsomal enzyme of these fungi. Phosphorylcholine and lysophosphatidylcholine markedly inhibited the enzyme in the two dermatophytes; however, the inhibition was less pronounced with phosphatidylcholine.

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