2 results match your criteria: "From the Center for Structural Biology and Department of Biochemistry.[Affiliation]"
Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE.
J Biol Chem
February 2016
From the Center for Structural Biology and Department of Biochemistry, Comprehensive Cancer Center of Wake Forest Baptist Medical Center, Winston-Salem, North Carolina 27157
Article Synopsis
- FASN is crucial for synthesizing palmitate, with its expression elevated in cancer, and its activity modulated by various mechanisms.
- The type II thioesterase TE2 influences fatty acid chain length and has links to breast cancer, but competing interactions with the type I thioesterase TE1 are not well understood.
- Recent findings reveal the structural differences between TE1 and TE2, with TE2 having a unique capping domain that impacts its catalytic functionality, leading to the release of shorter fatty acids during synthesis.
Peroxiredoxins (Prxs) detoxify peroxides and modulate H2O2-mediated cell signaling in normal and numerous pathophysiological contexts. The typical 2-Cys subclass of Prxs (human Prx1-4) utilizes a Cys sulfenic acid (Cys-SOH) intermediate and disulfide bond formation across two subunits during catalysis. During oxidative stress, however, the Cys-SOH moiety can react with H2O2 to form Cys sulfinic acid (Cys-SO2H), resulting in inactivation.
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