PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34156827-2 2021 We recently demonstrated that human viperin (HsVip) catalyzes the conversion of CTP to 3"-deoxy-3",4"-didehydro-CTP (ddhCTP or ddh-synthase), which acts as a chain terminator for virally encoded RNA-dependent RNA polymerases from several flaviviruses. Cytidine Triphosphate 80-83 radical S-adenosyl methionine domain containing 2 Homo sapiens 36-43 34156827-7 2021 Furthermore, we define the unique chemical and physical determinants supporting ddh-synthase activity and nucleotide selectivity, including the crystallographic characterization of a fungal viperin-like enzyme that utilizes UTP as a substrate and a cnidaria viperin-like enzyme that utilizes CTP as a substrate. Cytidine Triphosphate 292-295 radical S-adenosyl methionine domain containing 2 Homo sapiens 258-265 31917549-1 2020 Viperin is a radical S-adenosylmethionine (SAM) enzyme that inhibits viral replication by converting cytidine triphosphate (CTP) into 3"-deoxy-3",4"-didehydro-CTP and by additional undefined mechanisms operating through its N- and C-terminal domains. Cytidine Triphosphate 101-122 radical S-adenosyl methionine domain containing 2 Homo sapiens 0-7 33108121-5 2020 This unique role explains why evolution has led to the early emergence in animals of an antiviral immunity enzyme, viperin, that synthesizes a toxic analogue of CTP. Cytidine Triphosphate 161-164 radical S-adenosyl methionine domain containing 2 Homo sapiens 115-122 32603630-4 2020 Most recently, however, viperin was demonstrated to catalyze the conversion of cytidine triphosphate (CTP) to 3"-deoxy-3",4"-didehydro-CTP (ddhCTP), a previously unknown ribonucleotide. Cytidine Triphosphate 79-100 radical S-adenosyl methionine domain containing 2 Homo sapiens 24-31 32603630-4 2020 Most recently, however, viperin was demonstrated to catalyze the conversion of cytidine triphosphate (CTP) to 3"-deoxy-3",4"-didehydro-CTP (ddhCTP), a previously unknown ribonucleotide. Cytidine Triphosphate 102-105 radical S-adenosyl methionine domain containing 2 Homo sapiens 24-31 32061099-2 2020 Recently, it has been reported that the radical-SAM activity of viperin transforms cytidine triphosphate (CTP) to its analogue 3"-deoxy-3",4"-didehydro-CTP (ddhCTP). Cytidine Triphosphate 83-104 radical S-adenosyl methionine domain containing 2 Homo sapiens 64-71 32061099-2 2020 Recently, it has been reported that the radical-SAM activity of viperin transforms cytidine triphosphate (CTP) to its analogue 3"-deoxy-3",4"-didehydro-CTP (ddhCTP). Cytidine Triphosphate 106-109 radical S-adenosyl methionine domain containing 2 Homo sapiens 64-71 32061099-2 2020 Recently, it has been reported that the radical-SAM activity of viperin transforms cytidine triphosphate (CTP) to its analogue 3"-deoxy-3",4"-didehydro-CTP (ddhCTP). Cytidine Triphosphate 152-155 radical S-adenosyl methionine domain containing 2 Homo sapiens 64-71 32061099-2 2020 Recently, it has been reported that the radical-SAM activity of viperin transforms cytidine triphosphate (CTP) to its analogue 3"-deoxy-3",4"-didehydro-CTP (ddhCTP). Cytidine Triphosphate 152-155 radical S-adenosyl methionine domain containing 2 Homo sapiens 64-71 32232843-2 2020 Recently, it was found that RSAD2 catalyses transformation of cytidine triphosphate (CTP) to its analogue 3 -deoxy-3 ,4 -didehydro-CTP (ddhCTP). Cytidine Triphosphate 62-83 radical S-adenosyl methionine domain containing 2 Homo sapiens 28-33 32232843-2 2020 Recently, it was found that RSAD2 catalyses transformation of cytidine triphosphate (CTP) to its analogue 3 -deoxy-3 ,4 -didehydro-CTP (ddhCTP). Cytidine Triphosphate 85-88 radical S-adenosyl methionine domain containing 2 Homo sapiens 28-33 31917549-1 2020 Viperin is a radical S-adenosylmethionine (SAM) enzyme that inhibits viral replication by converting cytidine triphosphate (CTP) into 3"-deoxy-3",4"-didehydro-CTP and by additional undefined mechanisms operating through its N- and C-terminal domains. Cytidine Triphosphate 124-127 radical S-adenosyl methionine domain containing 2 Homo sapiens 0-7 31917549-2 2020 Here, we describe crystal structures of viperin bound to a SAM analogue and CTP or uridine triphosphate (UTP) and report kinetic parameters for viperin-catalyzed reactions with CTP or UTP as substrates. Cytidine Triphosphate 76-79 radical S-adenosyl methionine domain containing 2 Homo sapiens 40-47 31917549-2 2020 Here, we describe crystal structures of viperin bound to a SAM analogue and CTP or uridine triphosphate (UTP) and report kinetic parameters for viperin-catalyzed reactions with CTP or UTP as substrates. Cytidine Triphosphate 177-180 radical S-adenosyl methionine domain containing 2 Homo sapiens 40-47 31917549-2 2020 Here, we describe crystal structures of viperin bound to a SAM analogue and CTP or uridine triphosphate (UTP) and report kinetic parameters for viperin-catalyzed reactions with CTP or UTP as substrates. Cytidine Triphosphate 177-180 radical S-adenosyl methionine domain containing 2 Homo sapiens 144-151 31917549-3 2020 Viperin orients the C4" hydrogen atom of CTP and UTP similarly for abstraction by a 5"-deoxyadenosyl radical, but the uracil moiety introduces unfavorable interactions that prevent tight binding of UTP. Cytidine Triphosphate 41-44 radical S-adenosyl methionine domain containing 2 Homo sapiens 0-7 29925952-4 2018 Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3"-deoxy-3",4"-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. Cytidine Triphosphate 61-82 radical S-adenosyl methionine domain containing 2 Homo sapiens 25-32 30872404-7 2019 We show that IRAK1 and TRAF6 increase viperin activity ~10-fold to efficiently catalyze the radical-mediated dehydration of CTP to ddhCTP. Cytidine Triphosphate 124-127 radical S-adenosyl methionine domain containing 2 Homo sapiens 38-45 29925952-4 2018 Here we demonstrate that viperin catalyses the conversion of cytidine triphosphate (CTP) to 3"-deoxy-3",4"-didehydro-CTP (ddhCTP), a previously undescribed biologically relevant molecule, via a SAM-dependent radical mechanism. Cytidine Triphosphate 84-87 radical S-adenosyl methionine domain containing 2 Homo sapiens 25-32