期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 25, 期 20, 页码 4549-4552出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2015.08.065
关键词
Phosphatase; PTP; Isothiocyanate; Enzyme inactivation; Sulforaphane
资金
- Diabetes Action Research and Education Foundation [276]
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. (C) 2015 Elsevier Ltd. All rights reserved.
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