ADP-dependent glucokinase (ADPGK) produces glucose-6-phosphate with adenosine diphosphate (ADP) as the phosphate group donor, in contrast to ATP-dependent hexokinases (HKs). Originally found in archaea, ADPGK is involved in glycolysis. However, its biological function in most eukaryotic organisms is still unclear, and the molecular mechanism of action requires further investigation. This paper provides a concise overview of ADPGK's origin, biological function and clinical application. It aims to furnish scientific information for the diagnosis and treatment of human metabolic diseases, neurological disorders, and malignant tumours, and to suggest new strategies for the development of targeted drugs.
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http://dx.doi.org/10.3389/fonc.2024.1358904 | DOI Listing |
Front Oncol
March 2024
Department of Internal Medicine, Fujian Medical University Union Hospital, Fuzhou, Fujian, China.
Mil Med Res
February 2024
Department of Urology, the Third Medical Centre, Chinese PLA General Hospital, Beijing, 100039, China.
Mil Med Res
February 2024
Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN, 38105, USA.
Mil Med Res
December 2023
Department of Urology, West China Hospital, Sichuan University, Chengdu, 610041, China.
Background: Cell metabolism plays a pivotal role in tumor progression, and targeting cancer metabolism might effectively kill cancer cells. We aimed to investigate the role of hexokinases in prostate cancer (PCa) and identify a crucial target for PCa treatment.
Methods: The Cancer Genome Atlas (TCGA) database, online tools and clinical samples were used to assess the expression and prognostic role of ADP-dependent glucokinase (ADPGK) in PCa.
Arch Biochem Biophys
June 2023
Laboratorio de Bioquímica y Biología Molecular, Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago, Chile. Electronic address:
Although ADP-dependent sugar kinases were first described in archaea, at present, the presence of an ADP-dependent glucokinase (ADP-GK) in mammals is well documented. This enzyme is mainly expressed in hematopoietic lineages and tumor tissues, although its role has remained elusive. Here, we report a detailed kinetic characterization of the human ADP-dependent glucokinase (hADP-GK), addressing the influence of a putative signal peptide for endoplasmic reticulum (ER) destination by characterizing a truncated form.
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