AK5: Human adenylate kinase 5
PDB Code: 2BWJ
Adenylate kinases (AK’s) are essential for the maintenance of cellular energetic economy and are key enzymes in the synthesis and regulation of adenine nucleotides. AK’s are required for a variety of cellular metabolic processes as well as for RNA and DNA synthesis. In general AK’s catalyze the exchange of adenine nucleotide phosphate moieties (ATP + AMP <->  2ADP) and facilitate transfer of both β- and γ-phosphoryls in ATP. AK5has been shown to phosphorylate both AMP and dAMP at equal efficiency with ATP as phosphate donor, and AMP, CMP, and dCMP with GTP as phosphate donor. Thus, the substrate specificity of AK5 overlaps with that of the closely sequence-related UMP/CMP kinases.
The cellular phosphotransfer becomes particularly important in tissues with an increase energy demand. AK’s play also an important role in the activation of therapeutic nucleoside analogues used for the treatment of cancer and against virus infections.
AK5 has been identified by EST database searching for novel nucleoside monophosphate kinases. The gene encodes a 198-amino acid protein which contains a nucleoside triphosphate binding glycine-rich region, a nucleoside monophosphate-binding site, and the lid domain that closes over the substrate upon binding. Within the AK family AK5 is most closely related to AK1 58% (sequence identity). AK5 is specifically expressed in the brain and transfection experiments with an AK5-GFP fusion protein demonstrated that it is localized in the cytosol.

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