메뉴 건너뛰기




Volumn 51, Issue 4, 2004, Pages 381-388

Current progress in the fatty acid metabolism in Cryptosporidium parvum

Author keywords

Apicomplexan; Cryptosporidium parvum; Fatty acid synthesis

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ACYLTRANSFERASE; COCCIDIOSTATIC AGENT; FATTY ACID; FATTY ACID ELONGASES; FATTY ACID SYNTHASE; PROTOZOAL PROTEIN;

EID: 3242893055     PISSN: 10665234     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1550-7408.2004.tb00384.x     Document Type: Review
Times cited : (57)

References (58)
  • 2
    • 0027208244 scopus 로고
    • Type-selective inhibition of microbial fatty acid synthases by thiolactomycin
    • Arimura, N. & Kaneda, T. 1993. Type-selective inhibition of microbial fatty acid synthases by thiolactomycin. Arch. Microbiol., 160:158-161.
    • (1993) Arch. Microbiol. , vol.160 , pp. 158-161
    • Arimura, N.1    Kaneda, T.2
  • 4
    • 0035108032 scopus 로고    scopus 로고
    • Triclosan and fatty acid synthesis in Plasmodium falciparum: New weapon for an old enemy
    • Bhat, G. P. & Surolia, N. 2001. Triclosan and fatty acid synthesis in Plasmodium falciparum: new weapon for an old enemy. J. Biosci., 26:1-3.
    • (2001) J. Biosci. , vol.26 , pp. 1-3
    • Bhat, G.P.1    Surolia, N.2
  • 5
    • 0031040894 scopus 로고    scopus 로고
    • Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity
    • Black, P. N., Zhang, Q., Weimar, J. D. & DiRusso, C. C. 1997. Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem., 272:4896-4903.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4896-4903
    • Black, P.N.1    Zhang, Q.2    Weimar, J.D.3    DiRusso, C.C.4
  • 6
    • 0347597735 scopus 로고    scopus 로고
    • Characterization of a Cryptosporidium parvum gene encoding a protein with homology to long-chain fatty acid synthetase
    • Camero, L., Shulaw, W. P. & Xiao, L. 2003. Characterization of a Cryptosporidium parvum gene encoding a protein with homology to long-chain fatty acid synthetase. J. Eukaryot. Microbiol., 50(Suppl.): 534-538.
    • (2003) J. Eukaryot. Microbiol. , vol.50 , Issue.SUPPL. , pp. 534-538
    • Camero, L.1    Shulaw, W.P.2    Xiao, L.3
  • 7
    • 0032882626 scopus 로고    scopus 로고
    • Cryptosporidium is more closely related to the gregarines than to coccidia as shown by phylogenetic analysis of apicomplexan parasites inferred using small-subunit ribosomal RNA gene sequences
    • Carreno, R. A., Martin, D. S. & Barta, J. R. 1999. Cryptosporidium is more closely related to the gregarines than to coccidia as shown by phylogenetic analysis of apicomplexan parasites inferred using small-subunit ribosomal RNA gene sequences. Parasitol. Res., 85:899-904.
    • (1999) Parasitol. Res. , vol.85 , pp. 899-904
    • Carreno, R.A.1    Martin, D.S.2    Barta, J.R.3
  • 9
    • 0032215021 scopus 로고    scopus 로고
    • Arabidopsis cDNA encoding a membrane-associated protein with an acyl-CoA binding domain
    • Chye, M. L. 1998. Arabidopsis cDNA encoding a membrane-associated protein with an acyl-CoA binding domain. Plant. Mol. Biol., 38:827-838.
    • (1998) Plant. Mol. Biol. , vol.38 , pp. 827-838
    • Chye, M.L.1
  • 10
    • 0033118479 scopus 로고    scopus 로고
    • Isolation of a gene encoding Arabidopsis membrane-associated acyl-CoA binding protein and immunolocalization of its gene product
    • Chye, M. L., Huang, B. Q. & Zee, S. Y. 1999. Isolation of a gene encoding Arabidopsis membrane-associated acyl-CoA binding protein and immunolocalization of its gene product. Plant. J., 18:205-214.
    • (1999) Plant. J. , vol.18 , pp. 205-214
    • Chye, M.L.1    Huang, B.Q.2    Zee, S.Y.3
  • 11
    • 0034488568 scopus 로고    scopus 로고
    • Single amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeats
    • Chye, M. L., Li, H. Y. & Yung, M. H. 2000. Single amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeats. Plant. Mol. Biol., 44:711-721.
    • (2000) Plant. Mol. Biol. , vol.44 , pp. 711-721
    • Chye, M.L.1    Li, H.Y.2    Yung, M.H.3
  • 12
    • 3242888376 scopus 로고    scopus 로고
    • Both Type I and Type II Fatty Acid Synthases in Toxoplasma gondii
    • (2003), Abstract No. 14C
    • Crawford, M. J., Zhu, G. & Roos, D. S. 2003. Both Type I and Type II Fatty Acid Synthases in Toxoplasma gondii. Molecular Parasitology Meeting XIV (2003), Abstract No. 14C.
    • (2003) Molecular Parasitology Meeting XIV
    • Crawford, M.J.1    Zhu, G.2    Roos, D.S.3
  • 13
    • 0029862742 scopus 로고    scopus 로고
    • Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii
    • Denton, H., Brown, S. M., Roberts, C. W., Alexander, J., McDonald, V., Thong, K. W. & Coombs, G. H. 1996. Comparison of the phosphofructokinase and pyruvate kinase activities of Cryptosporidium parvum, Eimeria tenella and Toxoplasma gondii. Mol. Biochem. Parasitol., 76:23-29.
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 23-29
    • Denton, H.1    Brown, S.M.2    Roberts, C.W.3    Alexander, J.4    McDonald, V.5    Thong, K.W.6    Coombs, G.H.7
  • 14
    • 0030805124 scopus 로고    scopus 로고
    • Glycolytic enzyme activities in Cryptosporidium parvum oocysts
    • Entrala, E. & Mascaro, C. 1997. Glycolytic enzyme activities in Cryptosporidium parvum oocysts. FEMS Microbiol. Lett., 151:51-57.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 51-57
    • Entrala, E.1    Mascaro, C.2
  • 15
    • 0002339281 scopus 로고    scopus 로고
    • The General Biology of Cryptosporidium
    • Fayer, R. (ed.), CRC Press, Inc., Boca Raton, Florida
    • Fayer, R., Speer, C. A. & Dubey, J. P. 1997. The General Biology of Cryptosporidium. In: Fayer, R. (ed.), Cryptosporidium and Cryptosporidiosis. CRC Press, Inc., Boca Raton, Florida. p. 1-42.
    • (1997) Cryptosporidium and Cryptosporidiosis , pp. 1-42
    • Fayer, R.1    Speer, C.A.2    Dubey, J.P.3
  • 16
    • 0037738615 scopus 로고    scopus 로고
    • The apicoplast: A plastid in Plasmodium falciparum and other apicomplexan parasites
    • Foth, B. J. & McFadden, G. I. 2003. The apicoplast: a plastid in Plasmodium falciparum and other apicomplexan parasites. Int. Rev. Cytol., 224:57-110.
    • (2003) Int. Rev. Cytol. , vol.224 , pp. 57-110
    • Foth, B.J.1    McFadden, G.I.2
  • 18
    • 0142061141 scopus 로고    scopus 로고
    • Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites
    • Gornicki, P. 2003. Apicoplast fatty acid biosynthesis as a target for medical intervention in apicomplexan parasites. Int. J. Parasitol., 33: 885-896.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 885-896
    • Gornicki, P.1
  • 19
    • 0032515066 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial biocides target the FabI component of fatty acid synthesis
    • Heath, R. J., Yu, Y. T., Shapiro, M. A., Olson, E. & Rock, C. O. 1998. Broad-spectrum antimicrobial biocides target the FabI component of fatty acid synthesis. J. Biol. Chem., 273:30316-30320.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30316-30320
    • Heath, R.J.1    Yu, Y.T.2    Shapiro, M.A.3    Olson, E.4    Rock, C.O.5
  • 21
    • 0025606149 scopus 로고
    • Molecular genetics of polyketides and its comparison to fatty acid biosynthesis
    • Hopwood, D. A. & Sherman, D. H. 1990. Molecular genetics of polyketides and its comparison to fatty acid biosynthesis. Ann. Rev. Genetics, 24:37-66.
    • (1990) Ann. Rev. Genetics , vol.24 , pp. 37-66
    • Hopwood, D.A.1    Sherman, D.H.2
  • 23
    • 0037189489 scopus 로고    scopus 로고
    • The carboxyltransferase activity of the apicoplast acetyl-CoA carboxylase of Toxoplasma gondli is the target of aryloxyphenoxypropionate inhibitors
    • Jelenska, J., Sirikhachornkit, A., Haselkorn, R. & Gornicki, P. 2002. The carboxyltransferase activity of the apicoplast acetyl-CoA carboxylase of Toxoplasma gondli is the target of aryloxyphenoxypropionate inhibitors. J. Biol. Chem., 277:23208-23215.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23208-23215
    • Jelenska, J.1    Sirikhachornkit, A.2    Haselkorn, R.3    Gornicki, P.4
  • 24
    • 0842283488 scopus 로고    scopus 로고
    • Analogues of thiolactomycin as potential anti-malarial and anti-trypanosomal agents
    • Jones, S. M., Urch, J. E., Brun, R., Harwood, J. L., Berry, C. & Gilbert, I. H. 2004. Analogues of thiolactomycin as potential anti-malarial and anti-trypanosomal agents. Bioorg. Med. Chem., 12:683-692.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 683-692
    • Jones, S.M.1    Urch, J.E.2    Brun, R.3    Harwood, J.L.4    Berry, C.5    Gilbert, I.H.6
  • 26
    • 0033960380 scopus 로고    scopus 로고
    • Role of acyl-CoA binding protein in acyl-CoA metabolism and acyl-CoA-mediated cell signaling
    • Knudsen, J., Neergaard, T. B., Gaigg, B., Jensen, M. V. & Hansen, J. K. 2000. Role of acyl-CoA binding protein in acyl-CoA metabolism and acyl-CoA-mediated cell signaling. J. Nutr., 130:294S-298S.
    • (2000) J. Nutr. , vol.130
    • Knudsen, J.1    Neergaard, T.B.2    Gaigg, B.3    Jensen, M.V.4    Hansen, J.K.5
  • 29
    • 0347513216 scopus 로고    scopus 로고
    • Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
    • LaGier, M. J., Tachezy, J., Stejskal, F., Kutisova, K. & Keithly, J. S. 2003. Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum. Microbiol., 149:3519-3530.
    • (2003) Microbiol. , vol.149 , pp. 3519-3530
    • LaGier, M.J.1    Tachezy, J.2    Stejskal, F.3    Kutisova, K.4    Keithly, J.S.5
  • 30
    • 0344931797 scopus 로고    scopus 로고
    • The cloning and expression of Pfacs1, a Plasmodium falciparum fatty acyl coenzyme A synthetase-1 targeted to the host erythrocyte cytoplasm
    • Matesanz, F., Duran-Chica, I. & Alcina, A. 1999. The cloning and expression of Pfacs1, a Plasmodium falciparum fatty acyl coenzyme A synthetase-1 targeted to the host erythrocyte cytoplasm. J. Mol. Biol., 291:59-70.
    • (1999) J. Mol. Biol. , vol.291 , pp. 59-70
    • Matesanz, F.1    Duran-Chica, I.2    Alcina, A.3
  • 31
    • 0037244046 scopus 로고    scopus 로고
    • The Plasmodium falciparum fatty acyl-CoA synthetase family (PfACS) and differential stage-specific expression in infected erythrocytes
    • Matesanz, F., Tellez, M. M. & Alcina, A. 2003. The Plasmodium falciparum fatty acyl-CoA synthetase family (PfACS) and differential stage-specific expression in infected erythrocytes. Mol. Biochem. Parasitol., 126:109-112.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 109-112
    • Matesanz, F.1    Tellez, M.M.2    Alcina, A.3
  • 34
    • 0035977004 scopus 로고    scopus 로고
    • Identification of a mammalian long-chain fatty acyl elongase regulated by sterol regulatory element-binding proteins
    • Moon, Y. A., Shah, N. A., Mohapatra, S., Warrington, J. A. & Horton, J. D. 2001a. Identification of a mammalian long-chain fatty acyl elongase regulated by sterol regulatory element-binding proteins. J. Biol. Chem., 276:45358-45366.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45358-45366
    • Moon, Y.A.1    Shah, N.A.2    Mohapatra, S.3    Warrington, J.A.4    Horton, J.D.5
  • 35
    • 0030878240 scopus 로고    scopus 로고
    • ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation
    • Oh, C. S., Toke, D. A., Mandala, S. & Martin, C. E. 1997. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem., 272:17376-17384.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17376-17384
    • Oh, C.S.1    Toke, D.A.2    Mandala, S.3    Martin, C.E.4
  • 36
    • 0036203391 scopus 로고    scopus 로고
    • Cryptosporidium virulence determinants - Are we there yet?
    • Okhuysen, P. C. & Chappell, C. L. 2002. Cryptosporidium virulence determinants - are we there yet? Int. J. Parasitol., 32:517-525.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 517-525
    • Okhuysen, P.C.1    Chappell, C.L.2
  • 37
    • 0031259927 scopus 로고    scopus 로고
    • Biosynthesis of polyketides
    • Rawlings, B. J. 1997. Biosynthesis of polyketides. Natural Product Reports, 14:523-556.
    • (1997) Natural Product Reports , vol.14 , pp. 523-556
    • Rawlings, B.J.1
  • 38
    • 0036139124 scopus 로고    scopus 로고
    • Carbon flux and fatty acid synthesis in plants
    • Rawsthorne, S. 2002. Carbon flux and fatty acid synthesis in plants. Prog. Lipid Res, 41:182-196.
    • (2002) Prog. Lipid Res , vol.41 , pp. 182-196
    • Rawsthorne, S.1
  • 39
    • 0344630333 scopus 로고    scopus 로고
    • Cryptosporidium parvum Cpn60 targets a relict organelle
    • Riordan, C. E., Ault, J. G., Langreth, S. G. & Keithly, J. S. 2003. Cryptosporidium parvum Cpn60 targets a relict organelle. Curr. Genet., 44:138-147.
    • (2003) Curr. Genet. , vol.44 , pp. 138-147
    • Riordan, C.E.1    Ault, J.G.2    Langreth, S.G.3    Keithly, J.S.4
  • 40
    • 0037327813 scopus 로고    scopus 로고
    • Fatty acid and sterol metabolism: Potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa
    • Roberts, C. W., McLeod, R., Rice, D. W., Ginger, M., Chance, M. L. & Goad, L. J. 2003. Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa. Mol. Biochem. Parasitol., 126:129-142.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 129-142
    • Roberts, C.W.1    McLeod, R.2    Rice, D.W.3    Ginger, M.4    Chance, M.L.5    Goad, L.J.6
  • 43
    • 0037461276 scopus 로고    scopus 로고
    • Structure-activity studies of the inhibition of FabI, the enoyl reductase from Escherichia coli, by triclosan: Kinetic analysis of mutant FabIs
    • Sivaraman, S., Zwahlen, J., Bell, A. F., Hedstrom, L. & Tonge, P. J. 2003. Structure-activity studies of the inhibition of FabI, the enoyl reductase from Escherichia coli, by triclosan: kinetic analysis of mutant FabIs. Biochemistry, 42:4406-4413.
    • (2003) Biochemistry , vol.42 , pp. 4406-4413
    • Sivaraman, S.1    Zwahlen, J.2    Bell, A.F.3    Hedstrom, L.4    Tonge, P.J.5
  • 44
    • 0028557012 scopus 로고
    • The animal fatty acid synthase: One gene, one polypeptide, seven enzymes
    • Smith, S. 1994. The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. FASEB J., 8:1248-1259.
    • (1994) FASEB J. , vol.8 , pp. 1248-1259
    • Smith, S.1
  • 45
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N. & Surolia, A. 2001. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med., 7:167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 47
    • 0029774363 scopus 로고    scopus 로고
    • Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae
    • Toke, D. A. & Martin, C. E. 1996. Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae. J. Biol. Chem., 271:18413-18422.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18413-18422
    • Toke, D.A.1    Martin, C.E.2
  • 48
  • 52
    • 0036307786 scopus 로고    scopus 로고
    • Progress with parasite plastids
    • Wilson, R. J. 2002. Progress with parasite plastids. J. Mol. Biol., 319: 257-274.
    • (2002) J. Mol. Biol. , vol.319 , pp. 257-274
    • Wilson, R.J.1
  • 54
    • 0033965297 scopus 로고    scopus 로고
    • Cryptosporidium parvum appears to lack a plastid genome
    • Zhu, G., Marchewka, M. J. & Keithly, J. S. 2000b. Cryptosporidium parvum appears to lack a plastid genome. Microbiology, 146:315-321.
    • (2000) Microbiology , vol.146 , pp. 315-321
    • Zhu, G.1    Marchewka, M.J.2    Keithly, J.S.3
  • 55
    • 0037130946 scopus 로고    scopus 로고
    • Cryptosporidium parvum: The first protist known to encode a putative polyketide synthase
    • Zhu, G., LaGier, M. J., Stejskal, F., Millership, J. J., Cai, X. & Keithly, J. S. 2002. Cryptosporidium parvum: the first protist known to encode a putative polyketide synthase. Gene, 298:79-89.
    • (2002) Gene , vol.298 , pp. 79-89
    • Zhu, G.1    LaGier, M.J.2    Stejskal, F.3    Millership, J.J.4    Cai, X.5    Keithly, J.S.6
  • 56
    • 1642554358 scopus 로고    scopus 로고
    • Expression and functional characterization of a giant Type I fatty acid synthase (CpFAS1) gene from Cryptosporidium parvum
    • Zhu, G., Li, Y., Cai, X., Millership, J. J., Marchewka, M. J. & Keithly, J. S. 2004. Expression and functional characterization of a giant Type I fatty acid synthase (CpFAS1) gene from Cryptosporidium parvum. Mol. Biochem. Parasitol., 134:127-135.
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 127-135
    • Zhu, G.1    Li, Y.2    Cai, X.3    Millership, J.J.4    Marchewka, M.J.5    Keithly, J.S.6
  • 58
    • 0033539685 scopus 로고    scopus 로고
    • Growth of Toxoplasma gondii is inhibited by aryloxyphenoxypropionate herbicides targeting acetyl-CoA carboxylase
    • Zuther, E., Johnson, J. J., Haselkorn, R., McLeod, R. & Gornicki, P. 1999. Growth of Toxoplasma gondii is inhibited by aryloxyphenoxypropionate herbicides targeting acetyl-CoA carboxylase. Proc. Natl. Acad. Sci. USA, 96:13387-13392.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13387-13392
    • Zuther, E.1    Johnson, J.J.2    Haselkorn, R.3    McLeod, R.4    Gornicki, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.