Kinases are a class of molecules in biochemistry that transfer phosphate groups from high-energy donor molecules (such as ATP) to specific target molecules (substrates), a process called phosphorylation.
At present, the common kinase products in the industry are roughly divided into four categories: protein kinases, fat kinases, fructokinases and mutant kinases. The largest family of kinases are protein kinases.
Protein kinases act on specific proteins and alter their activity. These kinases play a wide range of roles in cellular signaling and its complex life activities. Different other kinases act on small molecules (lipids, sugars, amino acids, nucleosides, etc.), either to signal or to prepare them for various biochemical reactions in metabolism.
Protein kinases are a key family of enzymes, of which 518 members comprising more than 2% of the genome are involved in various cell signaling pathways in humans (SignalChem, 2019). Kinases exert their effects by phosphorylating their respective downstream specific substrate proteins. They catalyze the transport of γ-phosphate from ATP or GTP to hydroxyl groups of serine, threonine and tyrosine in substrate proteins or to glycosyl moieties in lipids. Kinase dysregulation can lead to changes in enzyme activity and/or enzyme expression, subcellular localization, kinase stability, protein-protein interactions, and the like. Dysregulation of kinase-mediated signaling pathways is responsible for all major human pathological conditions, such as cancer, cardiovascular disease, neurodegenerative diseases and metabolic disorders.
Members of the protein kinase superfamily are key regulators of cell signaling pathways. Kinases are involved in mediating a variety of important functions, as reflected in 50 distinct kinase families, some of which are conserved across yeast, invertebrates, and mammals. Of the 518 human protein kinases, 478 belong to a single superfamily whose catalytic domains are sequence-related. They can cluster into groups, families and subfamilies with increasing sequence similarity and biochemical function. The kinase dendrogram shows the sequence similarity between these catalytic regions: the distance along the branch between two kinases is proportional to the difference between the two sequences.
Genetic alterations of protein kinases impair their biological functions, resulting in dysregulation of cellular pathways such as apoptosis, cell cycle regulation, proliferation, angiogenesis, differentiation, and cellular metabolism. Mutations in kinase-encoding genes have been observed in many pathological conditions ranging from cancer, inflammatory disease, and cardiovascular disease to neurodegeneration. In addition, certain kinase mutations are associated with acquired drug resistance. Therefore, mutant kinases quickly become important drug targets, and become the focus of drug discovery and development efforts.
These kinases are named after their substrates, such as:
- Adenylate kinase;
- Creatine kinase;
- Pyruvate kinase;
- Nucleoside diphosphate kinase;
- Thymidine kinase.
Creative BioMart provides a list of kinases proteins below. Please contact us for more information.
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