Biomaterial Database

Phosphorylation of exogenous substrates by the insulin receptor-associated protein kinase. 1983

L A Stadtmauer, and O M Rosen

A glycoprotein-enriched fraction derived from 3T3-L1 adipocyte membranes by Triton X-100 extraction and chromatography on wheat germ agglutinin-agarose contains an insulin-activable protein kinase that catalyzes the phosphorylation of tyrosine residues in proteins (Petruzzelli, L. M., Ganguly, S., Smith, C.J., Cobb, M. H., Rubin, C.S., and Rosen, O. M. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 6792-6796). The best peptide substrates for the enzyme are angiotensin II, and a synthetic peptide related to the amino acid sequence surrounding the site of tyrosine phosphorylation in the transforming protein kinase of Rous sarcoma virus. Kinetic analysis of the phosphorylation reaction with angiotensin II showed that insulin decreased the Km from 5.0 to 2.6 mM, and increased the Vmax from 0.6 to 2.2 pmol/min/10 fmol of insulin binding capacity. For the src-related peptide, the addition of insulin decreased the Km from 1.6 to 1.2 mM and increased the Vmax from 0.17 to 2.2 pmol/min/10 fmol of insulin binding capacity. Angiotensin III inhibitor, proctolin, beta-lipotropin (61-65) and Tyr-Arg were poorer substrates for the protein kinase. Protein substrates for the insulin-stimulated protein kinase include anti-src IgG, tubulin, casein, and histone H2b. The data suggest that the substrate specificity of the insulin-activable protein kinase is similar to that reported for the src and epidermal growth factor receptor protein kinases.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D010766	Phosphorylation	The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.	Phosphorylations
D011494	Protein Kinases	A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.	Protein Kinase,Kinase, Protein,Kinases, Protein
D011972	Receptor, Insulin	A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE.	Insulin Receptor,Insulin Receptor Protein-Tyrosine Kinase,Insulin Receptor alpha Subunit,Insulin Receptor beta Subunit,Insulin Receptor alpha Chain,Insulin Receptor beta Chain,Insulin-Dependent Tyrosine Protein Kinase,Receptors, Insulin,Insulin Receptor Protein Tyrosine Kinase,Insulin Receptors
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D002478	Cells, Cultured	Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.	Cultured Cells,Cell, Cultured,Cultured Cell
D000273	Adipose Tissue	Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white.	Fatty Tissue,Body Fat,Fat Pad,Fat Pads,Pad, Fat,Pads, Fat,Tissue, Adipose,Tissue, Fatty
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities