Tyrosine Kinase-enzyme

Tyrosine kinase belongs to the enzyme that can transfer a phosphate group from ATP to a protein in a cell. Tyrosine kinases are a subgroup of the larger class of protein kinases that attache phosphate groups to other amino acids, such as serine and threonine in tyrosine kinase phosphorylation process. Tyrosine kinase are a family of enzymes, which catalyze the tyrosine kinase phosphorylation of selecting tyrosine residues in target proteins. Tyrosine kinase phosphorylation is an important mechanism in communicating signals within a cell and regulating cellular activity in responsive to the stimuli in external and internal cell. These cellular activities refer to cell division, cell differentiation, cell growth, cell migration, cell metabolism and programmed cell death. Phosphorylation at tyrosine residues controls a wide range of properties in proteins such as tyrosine kinase activity, subcellular localization, and interaction between molecules. The receptor tyrosine kinase function in transmembrane signaling, whereas the non receptor tyrosine kinase within the cell function in signal transduction to the nucleus. Tyrosine kinase activity in the nucleus involves cell-cycle control and properties of transcription factors. SRC oncogene has a transforming non receptor tyrosine kinase activity, and find that EGFR was identified as the first receptor tyrosine kinase, which paved the way for the understanding of the role and significance of tyrosine kinase in cancer research. Tyrosine kinases are implicated in several steps of neoplastic development and progression.

Schematic representation of the mode of action of tyrosine kinase.

VEGFR kinase

AXL Family

ROR Family

TIE Family