Up-regulated during late spermiogenesis, when the flagellum is being assembled.
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity).
Belongs to the adenylate kinase family. AK1 subfamily.
Adenylate kinase isoenzyme 1, AK 1, ATP-AMP transphosphorylase 1, ATP:AMP phosphotransferase, Adenylate monophosphate kinase, Myokinase, Ak1
Proteins
Metabolism
23116Da
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