Characterization and Kinetic Mechanism of Catalytic Domain of Human Vascular Endothelial Growth Factor Receptor-2 Tyrosine Kinase (VEGFR2 TK), a Key Enzyme in Angiogenesis

• Published in: Biochemistry (Easton) Vol. 37; no. 47; pp. 16788 - 16801
• Main Authors: Parast, Camran V, Mroczkowski, Barbara, Pinko, Chris, Misialek, Shawn, Khambatta, Godrej, Appelt, Krzysztof
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 24.11.1998
• Subjects: Adenosine Triphosphate - analogs & derivatives; Adenosine Triphosphate - metabolism; Binding Sites; Binding, Competitive; Cadmium - pharmacology; Catalysis; Enzyme Activation; Humans; Kinetics; Magnesium - metabolism; Manganese - metabolism; Neovascularization, Physiologic; Phosphorylation; Protein Structure, Tertiary; Receptor Protein-Tyrosine Kinases - antagonists & inhibitors; Receptor Protein-Tyrosine Kinases - chemistry; Receptor Protein-Tyrosine Kinases - metabolism; Receptors, Growth Factor - antagonists & inhibitors; Receptors, Growth Factor - chemistry; Receptors, Growth Factor - metabolism; Receptors, Vascular Endothelial Growth Factor; Substrate Specificity; Time Factors

Vascular endothelial growth factor (VEGF) is a dimeric protein which induces formation of new blood vessels (angiogenesis) through binding to VEGF-receptor-2 tyrosine kinase (VEGFR2 TK) or KDR (kinase insert domain-containing receptor) on the surface of endothelial cells. Angiogenesis has been shown...