Inactivation of protein tyrosine phosphatases by dietary isothiocyanates

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• 作者：Sarah M. Lewis^a ; Ya Li^a ; ^d ; Michael J. Catalano^a ; Adrian R. Laciak^a ; Harkewal Singh^a ; Derrick R. Seiner^a ; Thomas J. Reilly^c ; John J. Tanner^a ; ^b ; Kent S. Gates^a ; ^b ; ^{gatesk@missouri.edu" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Phosphatase ; PTP ; Isothiocyanate ; Enzyme inactivation ; Sulforaphane
• 刊名：Bioorganic & Medicinal Chemistry Letters
• 出版年：2015
• 出版时间：15 October 2015
• 年：2015
• 卷：25
• 期：20
• 页码：4549-4552
• 全文大小：652 K

文摘

Isothiocyanates are bioactive dietary phytochemicals that react readily with protein thiol groups. We find that isothiocyanates are time-dependent inactivators of cysteine-dependent protein tyrosine phosphatases (PTPs). Rate constants for the inactivation of PTP1B and SHP-2 by allyl isothiocyanate and sulforaphane range from 2 to 16 M⁻¹ s⁻¹. Results in the context of PTP1B are consistent with a mechanism involving covalent, yet reversible, modification of the enzyme’s active site cysteine residue.