The mouse guanylate kinase double mutant E72Q/D103N is a functional adenylate kinase
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چکیده
منابع مشابه
Structural characterization of the closed conformation of mouse guanylate kinase.
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 pl...
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Adenylate kinases (ADK) are ubiquitous enzymes that contribute to the homeostasis of adeninenucleotides in living cells. In this study, the cloning of a cDNA encoding an adenylate kinase from the filariaOnchocerca volvulus has been described. Using PCR technique, a 281 bp cDNA fragment encoding part ofan adenylate kinase was isolated from an O. volvulus cDNA library. Use of this fragment as a p...
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There is no functional annotation for the majority of the several hundreds of receptor-like kinases in plants. A direct way of inferring the function of these proteins is to study the phenotype that results from loss of function mutants such as T-DNA mutant lines. In this research a function (phenotype) to At2g37050 gene that encodes a receptor like kinase in Arabidopsis T-DNA line was...
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Phototransduction is carried out by a signaling pathway that links photoactivation of visual pigments in retinal photoreceptor cells to a change in their membrane potential. Upon photoactivation, the second messenger of phototransduction, cyclic GMP, is rapidly degraded and must be replenished during the recovery phase of phototransduction by photoreceptor guanylate cyclases (GCs) GC1 (or GC-E)...
متن کاملThe crystal structure of human adenylate kinase 6: An adenylate kinase localized to the cell nucleus.
Adenylate kinases (AKs) play important roles in nucleotide metabolism in all organisms and in cellular energetics by means of phosphotransfer networks in eukaryotes. The crystal structure of a human AK named AK6 was determined by in-house sulfur single-wavelength anomalous dispersion phasing methods and refined to 2.0-A resolution with a free R factor of 21.8%. Sequence analyses revealed that h...
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ژورنال
عنوان ژورنال: Protein Engineering, Design and Selection
سال: 2001
ISSN: 1741-0134,1741-0126
DOI: 10.1093/protein/14.11.903