منابع مشابه
Molecular cloning of adenylate kinase from the human filarial parasite Onchocerca volvulus
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...
متن کاملLocalization of Adenylate Kinase 4 in Mouse Tissues
Adenylate kinase (AK) is a key enzyme in the high-energy phosphoryl transfer reaction in living cells. Of its isoforms, AK4 has a similar sequence and subcellular localization to that of AK3 in the mitochondrial matrix. However, unlike AK3, AK4 lacks the guanosine triphosphate: adenosine monophosphate phosphotransferase activity. To elucidate the physiological role of AK4, we explored the prote...
متن کاملAdenylate Kinase in Human Tissues I. ORGAN SPECIFICITY OF ADEXYLATE KIKASE ISOENZY;LIES*
The organ specificity of human adenylate kinase isoenzymes was established among adenylate kinase isoenzymes of different tissue origins by differences in the degree of inhibitions by sulfhydryl reagents; by differences in isoelectric points ; by differences of enzyme distribution patterns ; and in some instances, by differences in molecular weights. The organ specificity of the adenylate kinas...
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...
متن کاملConformational Transitions in Adenylate Kinase
Large conformational changes in the LID and NMP domains of adenylate kinase (AKE) are known to be key to ligand binding and catalysis, yet the order of binding events anddomainmotion is not well understood. Combining the multiple available structures for AKEwith the energy landscape theory for protein folding, a theoretical model was developed for allostery, order of binding events, and efficie...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42867-6