Insulin receptor tyrosine kinase-catalyzed phosphorylation of 422(aP2) protein. Substrate activation by long-chain fatty acid.
作者： R C Hresko , R D Hoffman , J R Flores-Riveros , M D Lane
DOI: 10.1016/S0021-9258(17)45329-4
关键词:
摘要: It was established previously that the 15-kDa protein phosphorylated in 3T3-L1 adipocytes treated with insulin and phenylarsine oxide is O-phospho-Tyr19 422(aP2) protein, a fatty acid-binding protein. To assess its capacity to serve as substrate of receptor tyrosine kinase vitro, native isolated from purified homogeneity. Receptor-catalyzed phosphorylation on Tyr19 markedly activated when long-chain acid, e.g. oleic bound Fatty acid had no effect autophosphorylation by intrinsic kinase. Both saturated (C14, C16, C18) unsaturated (all cis-delta 9 -delta C18, 9,12 9,12,15 5,8,11,14 C20) acids caused activation. The Km for greatly reduced (from 170 3 microM) little or Vmax. Upon binding susceptibility Tyr128 iodination lactoperoxidase method increased greatly. These results indicate upon undergoes conformational change whereby Tyr19, which lies within consensus-type sequence substrates, becomes accessible lactoperoxidase.
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