http://purl.uniprot.org/citations/21898642 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21898642 | http://www.w3.org/2000/01/rdf-schema#comment | "Aminopropyltransferases are essential enzymes that form polyamines in eukaryotic and most prokaryotic cells. Spermidine synthase (SpdS) is one of the most well-studied enzymes in this biosynthetic pathway. The enzyme uses decarboxylated S-adenosylmethionine and a short-chain polyamine (putrescine) to make a medium-chain polyamine (spermidine) and 5'-deoxy-5'-methylthioadenosine as a byproduct. Here, we report a new spermidine synthase inhibitor, decarboxylated S-adenosylhomocysteine (dcSAH). The inhibitor was synthesized, and dose-dependent inhibition of human, Thermatoga maritima, and Plasmodium falciparum spermidine synthases, as well as functionally homologous human spermine synthase, was determined. The human SpdS/dcSAH complex structure was determined by X-ray crystallography at 2.0 Å resolution and showed consistent active site positioning and coordination with previously known structures. Isothermal calorimetry binding assays confirmed inhibitor binding to human SpdS with K(d) of 1.1 ± 0.3 μM in the absence of putrescine and 3.2 ± 0.1 μM in the presence of putrescine. These results indicate a potential for further inhibitor development based on the dcSAH scaffold."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.org/dc/terms/identifier | "doi:10.1002/pro.717"xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "Ealick S.E."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "McCloskey D.E."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "Pegg A.E."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "Thomas H.J."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "Secrist J.A."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/author | "Seckute J."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/name | "Protein Sci"xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/pages | "1836-1844"xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/title | "Binding and inhibition of human spermidine synthase by decarboxylated S-adenosylhomocysteine."xsd:string |
http://purl.uniprot.org/citations/21898642 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/21898642 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21898642 |
http://purl.uniprot.org/citations/21898642 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21898642 |
http://purl.uniprot.org/uniprot/#_P19623-mappedCitation-21898642 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21898642 |
http://purl.uniprot.org/uniprot/P19623 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21898642 |