gmpk - Three conformational states of GMPK Overlays wining288 of yGMPK apo CDD Conserved Protein Domain Family GMPK Jul 1 2008 Human GMPK is an obligate step for the activation of acyclic guanosine analogs such as ganciclovir which necessitate efficient phosphorylation while GMPK from bacterial pathogens in which this Equilibrium binding of GMP to 10 M GMPK The relative Structural Characterization of the Closed Conformation of Structural Characterization of the Closed Conformation of Jan 22 2024 In this study 11 GmPK genes possess the Wbox Fig 6 Table S4 in their promoters These GmPK genes probably could be upregulated by WRKY genes in soybean Further study could use the yeast onehybrid system to verify this speculation 926 of the GmPK gene promoters contained the saltregulated element SRE GT1GMSCAM4 Fig 6 Structural characterization of the closed conformation of Guanylate kinase DrugBank Online GMPK Guanylate kinase 1 Gene Name GUK1 UniProtKB Entry Q16774 SwissProt Organism Humans NCBI Taxonomy ID 9606 Amino acid sequence lclBSEQ0004617Guanylate kinase Virtual Screening of the Guanylate Monophosphate Kinase GMPK Jan 1 2011 In contrast GMPK recognized only acyclovir and ganciclovir monophosphates as substrates not their diphosphates Kinetic studies demonstrated that CPVDP has a KM value of 4515μM We were however unable to determine the KM value for CPVMP directly but a mathematical model of experimental data gave a theoretical KM value for CPVMP Guanylate kinase GMPK is an essential enzyme for the biosynthesis of GTP and dGTP by catalyzing the phosphoryl transfer from ATP to dGMP resulting in ADP and dGDP Despite the similar fold of the monomer there is an important difference between GMPKs from prokaryotes and eukaryotes eukaryotes GMPK are monomers while prokaryotes GMPK are Structural Characterization of the Closed Conformation of The LID region of GMPK apo and GMPK GMP is composed of two helices connected by a loop whereas the LID region of hCASKGK is composed of only a single helix and a long loop The overlay done by using the CORE region to align the structures shows that the LID region of hCASKGK cannot be superimposed on the LID regions of GMPK apo or GMPK GMP Crystal structures of GMP kinase in complex with ganciclovir Guanosine monophosphate kinases GMPK by catalyzing the phosphorylation of GMP or dGMP are of dual potential in assisting the activation of antiviral prodrugs or as candidates for antibiotic strategies Human GMPK is an obligate step for the activation of acyclic guanosine analogs such as ganci Finally we superimposed the three GMPK domains using the lowest energy NMR structure as a reference Fig 5 BD The relatively similar backbone conformations for each domain across the three species whether ligandfree or bound points to a rigidbody motion bringing the GMPBD and the LID domains together for catalysis Virtual Screening of the Guanylate Monophosphate Kinase GMPK May 7 2019 Finally we superimposed the three GMPK domains using the lowest energy NMR structure as a reference Fig 5 BD The relatively similar backbone conformations for each domain across the three species whether ligandfree or bound points to a rigidbody motion bringing the GMPBD and the LID domains together for catalysis Guanylate kinase tas karung GMPK is a nucleoside monophosphate kinase that catalyzes the reversible phosphoryl transfer from ATP to GMP to yield ADP and GDP In addition to phosphorylating GMP antiviral Insights into openclosed conformations of the catalytically Aug 16 2002 Prior to this work a structure of GMPK in which both substratebinding sites are occupied was not available Because of low sequence identity among the various NMP kinases and because of known structural differences between them eg the NMPbinding domain of adenylate kinase 9 is all helical whereas that of yeast GMPK consists of a fourstranded βsheet and two short helices 12 it Aug 16 2002 Guanylate kinase GMPK is a nucleoside monophosphate kinase that catalyzes the reversible phosphoryl transfer from ATP to GMP to yield ADP and GDP In addition to phosphorylating GMP antiviral prodrugs such as acyclovir ganciclovir and carbovir and anticancer prodrugs such as the thiopurines are Phosphorylation of antiviral and endogenous nucleotides to di Guanylate kinase GMPK1 ATPGMP phosphotransferase EC 2748 is a critical enzyme for the biosynthesis of GTP and dGTP by catalyzing the phosphoryl transfer from ATP to dGMP resulting in ADP and dGDP 1 2 GMPK also plays an important role in the recycling of the second messenger cGMP 3 In addition to these physiological roles GMPK is Oct 7 2015 GMPK is a member of the family of ATPNMP phosphoryltransferases nucleoside monophosphate kinases NMP kinases or NMPKs NMP kinases of different species E coli yeast mouse and human have been characterized for their structure and function showing similarities to the class of nucleoside kinases eg human deoxycytidine kinase Structural Basis for Nucleotidedependent Regulation of Characterization of the pyruvate kinase gene family in Solution structure and functional investigation of human A superposition of the 20member ensemble of hGMPK magenta and three Xray structures of GMP ADP mouse GMPK mGMPK cyan PDB code 1LVG and apogray PDB code 1EX6 and GMPbound yellow PDB Structural comparison of hGMPK with nucleotidefree and bound Guanylate kinases GMPK from Mycobacterium tuberculosis Mus musculus and Saccharomyces cereviae were submitted to virtual screening in order to determine proteinligand interactions specific to M tuberculosis The opening of the cleft between CORE LID and GMP domains was found to have a large influence on the established interactions and on the determination of ligands binding specifically In GMPK Mt it is predicted to comprise Ser35 in the Ploop and an acidic residue Glu115 in the watermediated coordination shell Unique GMPbinding site in Mycobacterium tuberculosis Guanylate kinase GMPK is a nucleoside monophosphate kinase that catalyzes the reversible phosphoryl transfer from ATP to GMP to yield ADP and GDP In addition to phosphorylating GMP antiviral prodrugs such as acyclovir ganciclovir and carbovir and anticancer prodrugs such as the thiopurines are dependent on GMPK for their activation Hence structural information on mammalian GMPK could Solution structure and functional investigation of human Characterization of guanylate kinase from gram positive and Oct 2 2020 GMPK is an enzyme that catalyzes the phosphorylation of guanosine monophosphate GMP by adenosine triphosphate ATP CDD provides a conserved protein domain family for GMPK with sequence alignment durox structure features and references
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