Electron paramagnetic resonance studies of spin-labeled fatty acid binding sites in Candida rugosa lipases

Article Abstract:

The binding of spin-labeled fatty acids (SLFA) to two isolipases from Candida rugosa has been studied through electron paramagnetic resonance (EPR)spectroscopy. The lipases help the fungus species adapt to nutrient differences in various physiological conditions. A minor isolipase termed lipase A which has greater ability to establish hydrophobic interactions is used in the research. EPR data reveal the presence of a tunnel in the enzyme which restricts the motion of the SLFA. These restrictions depend on the nature of the lipase and the position of the label.

Physiological aspects, Fatty acids, Binding sites (Biochemistry), Active sites (Biochemistry), Lipase, Candida

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Catalytic mechanism and metal specificity of bacterial peptide deformylase: A density functional theory QM/MM study

Article Abstract:

Catalytic mechanism and metal specificity of bacterial peptide deformylase (PDF) is theoretically investigated using a hybrid density functional theory (B3LYP) QM/MM method and by studying both [Fe.sup.2+]-PDF and [Zn.sup.2+] -PDF.

Proteases, Protein synthesis, Protein biosynthesis, Iron compounds, Density functionals, Density functional theory, Mechanical properties, Structure

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