ArticleInternational journal for parasitology2007
Functional characterization of the acyl-[acyl carrier protein] ligase in the Cryptosporidium parvum giant polyketide synthase.
Article in International journal for parasitology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Automatic reconstruction of metabolic pathways from identified biosynthetic gene clusters.BMC bioinformatics · 2021Article
- Molecular and Biochemical Characterization of a Type II Thioesterase From the Zoonotic Protozoan ParasiteFrontiers in cellular and infection microbiology · 2019Article
- Phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis.Scientific reports · 2017Article
- A review of the global burden, novel diagnostics, therapeutics, and vaccine targets for cryptosporidium.The Lancet. Infectious diseases · 2015Review
- Giardia fatty acyl-CoA synthetases as potential drug targets.Frontiers in microbiology · 2015Article
- Amelioration of Cryptosporidium parvum infection in vitro and in vivo by targeting parasite fatty acyl-coenzyme A synthetases.The Journal of infectious diseases · 2014Article
- The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life.Natural product reports · 2014Review
- Lipid synthesis in protozoan parasites: a comparison between kinetoplastids and apicomplexans.Progress in lipid research · 2013Review
- Novel anti-Cryptosporidium activity of known drugs identified by high-throughput screening against parasite fatty acyl-CoA binding protein (ACBP).The Journal of antimicrobial chemotherapy · 2012Article
- The reductase domain in a Type I fatty acid synthase from the apicomplexan Cryptosporidium parvum: restricted substrate preference towards very long chain fatty acyl thioesters.BMC biochemistry · 2010Article
- Cryptosporidium: genomic and biochemical features.Experimental parasitology · 2010Review
- Type I polyketide synthases that require discrete acyltransferases.Methods in enzymology · 2009Article
- Cryptosporidium parvum long-chain fatty acid elongase.Eukaryotic cell · 2007Article
- Make it or take it: fatty acid metabolism of apicomplexan parasites.Eukaryotic cell · 2007Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The apicomplexan Cryptosporidium parvum possesses a unique 1500-kDa polyketide synthase (CpPKS1) comprised of 29 enzymes for synthesising a yet undetermined polyketide. This study focuses on the biochemical characterization of the 845-amino acid loading unit containing acyl-[ACP] ligase (AL) and acyl carrier protein (ACP). The CpPKS1-AL domain has a substrate preference for long chain fatty acids, particularly for the C20:0 arachidic acid. When using [3H]palmitic acid and CoA as co-substrates, the AL domain displayed allosteric kinetics towards palmitic acid (Hill coefficient, h=1.46, K50=0.751 microM, Vmax=2.236 micromol mg(-1) min(-1)) and CoA (h=0.704, K50=5.627 microM, Vmax=0.557 micromol mg(-1) min(-1)), and biphasic kinetics towards adenosine 5'-triphosphate (Km1=3.149 microM, Vmax1=373.3 nmol mg(-1) min(-1), Km2=121.0 microM, and Vmax2=563.7 nmol mg(-1) min(-1)). The AL domain is Mg2+-dependent and its activity could be inhibited by triacsin C (IC50=6.64 microM). Furthermore, the ACP domain within the loading unit could be activated by the C. parvum surfactin production element-type phosphopantetheinyl transferase. After attachment of the fatty acid substrate to the AL domain for conversion into the fatty-acyl intermediate, the AL domain is able to transfer palmitic acid to the activated holo-ACP in vitro. These observations ultimately validate the function of the CpPKS1-AL-ACP unit, and make it possible to further dissect the function of this megasynthase using recombinant proteins in a stepwise procedure.
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