Literature DB >> 3745198

10-Thiastearic acid inhibits both dihydrosterculic acid biosynthesis and growth of the protozoan Crithidia fasciculata.

R A Pascal, S J Mannarelli, D L Ziering.   

Abstract

10-Thiastearic acid is a specific inhibitor of the biosynthesis of dihydrosterculic acid (9,10-methyleneoctadecanoic acid) in the trypanosomatid protozoan Crithidia fasciculata. A 50% inhibition of the biosynthesis of dihydrosterculate is observed in the presence of 4 microM 10-thiastearate in the protozoan growth medium, but little effect is seen on the distribution of the other fatty acids. In addition, the growth of the protozoa is slowed by the presence of 10-thiastearate, with 50% growth inhibition produced at about 10 microM. A possible mechanism of this inhibition and the implication of this result with regard to the design of antiprotozoal agents are discussed.

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Year:  1986        PMID: 3745198

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  5 in total

1.  Replication of human immunodeficiency virus 1 and Moloney murine leukemia virus is inhibited by different heteroatom-containing analogs of myristic acid.

Authors:  M L Bryant; R O Heuckeroth; J T Kimata; L Ratner; J I Gordon
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

2.  Gas-liquid chromatographic properties of positional isomers of methyl thia, selena, and tellura laurate analogs.

Authors:  M S Jie; O Bakare; Y K Cheung; S H Chau
Journal:  Lipids       Date:  1997-06       Impact factor: 1.880

Review 3.  Biochemistry of the Leishmania species.

Authors:  R H Glew; A K Saha; S Das; A T Remaley
Journal:  Microbiol Rev       Date:  1988-12

4.  Altered membrane association of p60v-src and a murine 63-kDa N-myristoyl protein after incorporation of an oxygen-substituted analog of myristic acid.

Authors:  R O Heuckeroth; J I Gordon
Journal:  Proc Natl Acad Sci U S A       Date:  1989-07       Impact factor: 11.205

5.  Heteroatom-substituted fatty acid analogs as substrates for N-myristoyltransferase: an approach for studying both the enzymology and function of protein acylation.

Authors:  R O Heuckeroth; L Glaser; J I Gordon
Journal:  Proc Natl Acad Sci U S A       Date:  1988-12       Impact factor: 11.205

  5 in total

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